sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C406Y to reconstruct the assayed variant sequence.

column_label: exact cells: substrate block IQ, row C406Y, columns kcat, KM, kcat/KM, Fold. Table footnote gives kcat units as pmol per min per pmol P450 and KM as uM.

normalized_value_unit_evidence: Paper kcat normalized to 0.138 s^-1 from min^-1 / 60; paper KM normalized to 0.022 mM from uM / 1000; paper kcat/KM normalized/row-consistent as 6.272727272727273 s^-1*mM^-1. Expected row values: kcat 0.138 s^(-1); KM 0.022 mM; kcat/KM 6.272727272727273 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Kinetic data for P450 1A2 variants; substrate block IQ; row C406Y; kcat 8.3 +/- 0.3 pmol/min/pmol P450; KM 22 +/- 2 uM; kcat/KM 0.38 min^-1*uM^-1; fold 1.4.

row_label: IQ / C406Y


enzyme_display_name: unspecific monooxygenase

organism: Homo sapiens

source_db: oed

verification_status: verified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

mutation_type: substitution

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

column_label: exact cells: substrate block PhIP, row C406Y, columns kcat, KM, kcat/KM, Fold. Table footnote gives kcat units as pmol per min per pmol P450 and KM as uM.

normalized_value_unit_evidence: Paper kcat normalized to 0.433 s^-1 from min^-1 / 60; paper KM normalized to 0.066 mM from uM / 1000; paper kcat/KM normalized/row-consistent as 6.5606060606060606 s^-1*mM^-1. Expected row values: kcat 0.433 s^(-1); KM 0.066 mM; kcat/KM 6.5606060606060606 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Kinetic data for P450 1A2 variants; substrate block PhIP; row C406Y; kcat 26 +/- 0.7 pmol/min/pmol P450; KM 66 +/- 5 uM; kcat/KM 0.39 min^-1*uM^-1; fold 2.5.

row_label: PhIP / C406Y

data_origin: experimental

enzyme: unspecific monooxygenase

status: verified

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D348N to reconstruct the assayed variant sequence.

column_label: exact cells: substrate block IQ, row D348N, columns kcat, KM, kcat/KM, Fold. Table footnote gives kcat units as pmol per min per pmol P450 and KM as uM.

normalized_value_unit_evidence: Paper kcat normalized to 0.193 s^-1 from min^-1 / 60; paper KM normalized to 0.027 mM from uM / 1000; paper kcat/KM normalized/row-consistent as 7.148148148148149 s^-1*mM^-1. Expected row values: kcat 0.193 s^(-1); KM 0.027 mM; kcat/KM 7.148148148148149 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Kinetic data for P450 1A2 variants; substrate block IQ; row D348N; kcat 11.6 +/- 0.3 pmol/min/pmol P450; KM 27 +/- 2 uM; kcat/KM 0.43 min^-1*uM^-1; fold 1.6.

row_label: IQ / D348N


substrate_name: arachidonate

kcat_over_km_display: Not reported

mutation_signature: Unknown

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.

smiles: CCCCC/C=C\C/C=C\C/C=C\C/C=C\CCCC(=O)O

substrate: arachidonate


substrate_name: O2; Reduced flavoprotein; Melatonin

source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org)

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

substrate: O2; Reduced flavoprotein; Melatonin


substrate_name: Melatonin

substrate: Melatonin


substrate_name: Melatonin; O2; Reduced flavoprotein

substrate: Melatonin; O2; Reduced flavoprotein


substrate_name: Reduced flavoprotein; Melatonin; O2

source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org); CC BY-NC-ND 4.0

substrate: Reduced flavoprotein; Melatonin; O2


substrate_name: Debrisoquin; Reduced flavoprotein; O2

kcat_display: Not reported

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant G42S

substrate: Debrisoquin; Reduced flavoprotein; O2


substrate_name: H+; O2; NADPH; Coumarin

km_display: Not reported

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant isoenzyme CYP2A6 Ile471Thr

substrate: H+; O2; NADPH; Coumarin


substrate_name: NADPH; H+; O2; 7-Ethoxy-4-trifluoromethylcoumarin

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant isoenzyme CYP2B6 Gln172His


substrate_name: H+; 7-Ethoxy-4-trifluoromethylcoumarin; O2; NADPH


substrate_name: NADPH; O2; Coumarin; H+

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2A6dH (lacking N-terminal transmembrane signal anchor domain)

substrate: NADPH; O2; Coumarin; H+


substrate_name: Indole; O2

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant L240C/N297Q

substrate: Indole; O2


sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

column_label: exact cells: substrate block PhIP, row wild-type, columns kcat, KM, kcat/KM, Fold. Table footnote gives kcat units as pmol per min per pmol P450 and KM as uM.

normalized_value_unit_evidence: Paper kcat normalized to 0.183 s^-1 from min^-1 / 60; paper KM normalized to 0.071 mM from uM / 1000; paper kcat/KM normalized/row-consistent as 2.5774647887323945 s^-1*mM^-1. Expected row values: kcat 0.183 s^(-1); KM 0.071 mM; kcat/KM 2.5774647887323945 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Kinetic data for P450 1A2 variants; substrate block PhIP; row wild-type; kcat 11 +/- 0.9 pmol/min/pmol P450; KM 71 +/- 13 uM; kcat/KM 0.16 min^-1*uM^-1; fold 1.

row_label: PhIP / wild-type


verification_status: corrected

column_label: Retained PDF Table 2, Glu-P-1 substrate block, Wild-type row: kcat 5 +/- 0.2; KM 4 +/- 1; kcat/KM 1.2.

normalized_value_unit_evidence: At retained catalog precision, kcat 0.083 s^-1 and KM 0.004 mM; the independently printed kcat/KM normalizes to 20.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 Glu-P-1 wild-type row: kcat 5 +/- 0.2 pmol min^-1 per pmol P450; KM 4 +/- 1 uM; independently printed kcat/KM 1.2 min^-1 uM^-1.

row_label: Glu-P-1 / Wild-type

table_label: Table 2. Kinetic data for P450 1A2 variants

status: corrected


substrate_name: H+; O2; 2-Amino-2,4-dimethylimidazo[4,5-f]quinoline; NADPH

sequence_variant_note: Mutation signature C406Y matches the mutant residue at offset +0 and the reference residue at offset -1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

assay_conditions_summary: cofactor NADPH

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant C406Y


substrate_name: Methadone

verification_status: unverified

substrate: Methadone

status: unverified


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

column_label: Table label: TABLE 3 Kinetics and profile of arachidonic acid metabolites generated by family 1 P450s. Row block: Km(app) (␮M) 34.1 95.2 29.8 500.0 / kcat ⫽ Vmax/Et (min⫺1) 11.60 7.40 0.48 0.13 / Catalytic efficiency 关kcat/Km(app)兴 (mM⫺1 min⫺1) 340.0 77.7 16.5 0.3. Enzyme column: CYP1A2 (second numeric column of the header row CYP1A1a CYP1A2 CYP1B1 Cyp1b1). Columns read: Km(app) (␮M) cell 95.2, kcat (min^-1) cell 7.40, Catalytic efficiency (mM^-1 min^-1) cell 77.7. metric: kcat; raw value: 7.40; raw unit: min^-1; normalized value: 0.123 s^(-1); metric: Km; raw value: 95.2; raw unit: uM; normalized value: 0.095 mM; metric: kcat/Km; raw value: 77.7; raw unit: mM^-1 min^-1; normalized value: 1.2947368421052632 s^-1 mM^-1; assay condition: Reconstituted system containing CYP1A2 at 150 nM incubated in a final volume of 1 ml containing 0.01% sodium cholate, 10 mM MgCl2, 150 mM KCl, 50 mM Tris-Cl (pH 7.5), 5 mM glucose 6-phosphate, 1 U glucose-6-phosphate dehydrogenase, and 50 ␮M arachidonic acid (0.1 ␮Ci of 14C-arachidonate) for 1 min at 37°C and, subsequently, for 30 min after the addition of 0.5 mM NADPH; reaction incubation time was 30 min. Export row conditions: pH 7.5; 310.15 K.

normalized_value_unit_evidence: CYP1A2 column of Table 3, arachidonic acid substrate: kcat 7.40 min^-1 divided by 60 s/min = 0.1233333 s^-1, which is 0.123 s^(-1) at the export's three-decimal stored precision; Km(app) 95.2 ␮M = 0.0952 mM (1 ␮M = 0.001 mM), which is 0.095 mM at the export's three-decimal stored precision; the printed catalytic efficiency cell 77.7 mM^-1 min^-1 divided by 60 s/min = 1.295 s^-1 mM^-1, and the export's stored ratio 1.2947368421052632 s^-1 mM^-1 is the quotient of this row's own cells at the export's stored precision (0.123 divided by 0.095), which equals 77.684 mM^-1 min^-1 and rounds to the printed cell 77.7 at that cell's own one-decimal precision. Rendering quirks of the pdftotext -layout extract: the micro sign renders as the character ␮, the superscript minus one renders as ⫺1, the equals sign in `kcat ⫽ Vmax/Et` renders as ⫽, and the square brackets enclosing kcat/Km(app) render as 关 and 兴.

raw_value_unit_evidence: TABLE 3 Kinetics and profile of arachidonic acid metabolites generated by family 1 P450s | enzyme column header row of Table 3: CYP1A1a CYP1A2 CYP1B1 Cyp1b1 | metric rows quoted from the same table block: `Km(app) (␮M) 34.1 95.2 29.8 500.0`, `Vmax (nmol min⫺1) 0.23 1.11 0.07 0.02`, `kcat ⫽ Vmax/Et (min⫺1) 11.60 7.40 0.48 0.13`, `Catalytic efficiency 关kcat/Km(app)兴 (mM⫺1 min⫺1) 340.0 77.7 16.5 0.3` | CYP1A2 column (second numeric column) cells read: Km(app) = 95.2 ␮M; kcat = Vmax/Et = 7.40 min^-1; Catalytic efficiency kcat/Km(app) = 77.7 mM^-1 min^-1.

row_label: CYP1A2 | arachidonic acid


substrate_name: Retinol

substrate: Retinol


substrate_name: all-trans-Retinal

substrate: all-trans-Retinal


substrate_name: Reduced flavoprotein; O2; Debrisoquin

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant G42K

substrate: Reduced flavoprotein; O2; Debrisoquin


substrate_name: O2; Reduced flavoprotein; Debrisoquin

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant G42V

substrate: O2; Reduced flavoprotein; Debrisoquin


proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant G42E


substrate_name: Reduced flavoprotein; Debrisoquin; O2

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant G42F

substrate: Reduced flavoprotein; Debrisoquin; O2


substrate_name: O2; Debrisoquin; Reduced flavoprotein

substrate: O2; Debrisoquin; Reduced flavoprotein


substrate_name: Debrisoquin; O2; Reduced flavoprotein

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant G42R

substrate: Debrisoquin; O2; Reduced flavoprotein


substrate_name: Coumarin

substrate: Coumarin


substrate_name: O2; Indole

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant N297Q

substrate: O2; Indole


proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant V140M/L240C/N297Q/I300V


proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant N297Q/I300V


proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant L240C/N297Q/I366V


substrate_name: Indole

substrate: Indole


substrate_name: O2; NADPH; 7-Ethoxy-4-trifluoromethylcoumarin; H+

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant isoenzyme CYP2B6 Pro167Ala


substrate_name: NADPH; Coumarin; O2; H+

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant isoenzyme CYP2A6 Glu419Asp

substrate: NADPH; Coumarin; O2; H+


column_label: Results prose, wild-type CYP1A2: Km 923 nM and Vmax 1.11 nmol/min/nmol P450. Table 2, CYP1A2 row, Vmax/Km column: 1.32 mL/min/nmol P450.

raw_value_unit_evidence: Printed page 449 reports wild-type CYP1A2 Km 923 nM and Vmax 1.11 nmol/min/nmol P450; Table 2 reports Vmax/Km 1.32 mL/min/nmol P450.

row_label: Wild-type CYP1A2 / 7-ethoxyresorufin O-deethylation

table_label: Results prose on printed page 449 and Table 2 on printed page 450


substrate_name: H+; NADPH; 7-Ethoxyresorufin; O2

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant isoenzyme CYP1A2 Gln478His

substrate: H+; NADPH; 7-Ethoxyresorufin; O2


substrate_name: H+; NADPH; O2; 7-Ethoxy-4-trifluoromethylcoumarin

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant isoenzyme CYP2B6 Arg487Cys


proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant I300V


substrate_name: Indole; O2

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant N297Q/I300V/I366V


proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant L240C/N297Q/I300V


substrate_name: Phenacetin; O2; NADPH; H+

assay_conditions_summary: cofactor NADP+

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2A13 L110V

substrate: Phenacetin; O2; NADPH; H+


proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant L240C/N297Q/I300V/I366V


proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant V140M/L240C/N297Q/I366V


proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant V140M/L240C/I300V/I366V


proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant V140M/N297Q/I300V/I366V


substrate_name: Paclitaxel; O2; NADPH

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2C8.4 (I264M)

substrate: Paclitaxel; O2; NADPH


substrate_name: O2; NADPH; Paclitaxel

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2C8.10 (K383N)

substrate: O2; NADPH; Paclitaxel


substrate_name: Paclitaxel; NADPH; O2

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2C8.6 (G171S)

substrate: Paclitaxel; NADPH; O2


substrate_name: O2; Paclitaxel; NADPH

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2C8.14 (A238P)

substrate: O2; Paclitaxel; NADPH


substrate_name: NADPH; Paclitaxel; O2

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2C8.8 (R186G)

substrate: NADPH; Paclitaxel; O2


proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2C8.3 (R139K, K399R)


proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2C8.13 (I223M)


substrate_name: NADPH; O2; Paclitaxel

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2C8.12 (461delV)

substrate: NADPH; O2; Paclitaxel


proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2C8.2 (I269F)


proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2C8.9 (K247R)


substrate_name: Fimasartan

substrate: Fimasartan


organism: Mus musculus

substrate_name: H+; NADPH; O2; Coumarin

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant C6L

substrate: H+; NADPH; O2; Coumarin


substrate_name: H+; NADPH; Coumarin; O2

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant C6A

substrate: H+; NADPH; Coumarin; O2


substrate_name: NADPH; Coumarin; H+; O2

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant C6N

substrate: NADPH; Coumarin; H+; O2


substrate_name: Coumarin; O2; NADPH; H+

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant C6G

substrate: Coumarin; O2; NADPH; H+


substrate_name: Coumarin; NADPH; O2; H+

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant C6D

substrate: Coumarin; NADPH; O2; H+


organism: Oryctolagus cuniculus

substrate_name: O2; NADPH; 4-Methyl-N-methyl-N-(2-phenyl-2H-pyrazol-3-yl)-benzene sulfonamide


substrate_name: Progesterone

substrate: Progesterone


substrate_name: O2; beta-Eudesmol; NADPH; H+

substrate: O2; beta-Eudesmol; NADPH; H+


organism: Meleagris gallopavo

substrate_name: Aflatoxin B1; H+; O2; NADPH

substrate: Aflatoxin B1; H+; O2; NADPH


substrate_name: H+; Aflatoxin B1; NADPH; O2

substrate: H+; Aflatoxin B1; NADPH; O2


substrate_name: Scoparone; O2

substrate: Scoparone; O2


substrate_name: NADPH; H+; Retinol; O2

substrate: NADPH; H+; Retinol; O2


substrate_name: Indole; O2

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant V140M/L240C/N297Q

substrate: Indole; O2


proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant V140M/L240C/N297Q/I300V/I366V


proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant V140M/N297Q/I300V


substrate_name: (-)-Camphor

column_label: PMID 17268056; article page 233; Table 1; row (-)-Camphor / CYP2A6; columns Km (uM); Vmax (nmol product/min/nmol P450); and Vmax/Km (mM^-1 min^-1).

normalized_value_unit_evidence: Km 0.023 mM; molar-enzyme-normalized Vmax equals turnover 4.9 min^-1 = 0.08166666666666667 s^-1; efficiency 213 mM^-1 min^-1 = 3.55 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 CYP2A6 row: Km 23 uM; Vmax 4.9 nmol product min^-1 nmol P450^-1; Vmax/Km 213 mM^-1 min^-1.

row_label: (-)-Camphor / CYP2A6

table_label: Table 1. Kinetic Analysis of the Hydroxylation of (-)-Camphor by Human Liver Microsomes and Recombinant P450 Enzymes

substrate: (-)-Camphor


substrate_name: O2; (-)-Camphor; H+; NADPH

substrate: O2; (-)-Camphor; H+; NADPH


substrate_name: Deltamethrin; H+; NADPH; O2

substrate: Deltamethrin; H+; NADPH; O2


substrate_name: arachidonate

column_label: TABLE 3, arachidonic acid kinetics for the family 1 cytochromes; column 'Cyp1b1'; row 'Km(app) (uM)' = 500.0 and row 'kcat = Vmax/Et (min-1)' = 0.13; same table, same enzyme column; column header line: CYP1A1a                       CYP1A2                        CYP1B1                         Cyp1b1

normalized_value_unit_evidence: kcat: 0.13 min^(-1) / 60 = 0.0021666666666666666 s^(-1), carried at the export's three-decimal precision as 0.002 s^(-1); Km: 500.0 uM / 1000 = 0.5 mM; kcat_over_km: 0.002 / 0.5 = 0.004 s^(-1) mM^(-1), the quotient of the same-column kcat and Km(app) cells

raw_value_unit_evidence: TABLE 3, mouse Cyp1b1, Cyp1b1: Km(app) 500.0 uM; kcat = Vmax/Et 0.13 min^(-1); printed catalytic efficiency [kcat/Km(app)] 0.3 mM^(-1) min^(-1)

row_label: Km(app) and kcat = Vmax/Et rows; Cyp1b1 column

table_label: TABLE 3

substrate: arachidonate


column_label: TABLE 1 'Kinetics of retinoid and DMBA metabolism by CYP1B1 and Cyp1b1'; Cyp1b1 row block; column 'DMBA'; cell 'Km(app) (uM)' = 138.9 and cell 'kcat = Vmax/Et (min-1)' = 8.28; same table, same row block, same substrate column; column header line: Retinol         Retinal        DMBA

normalized_value_unit_evidence: kcat: 8.28 min^(-1) / 60 = 0.138 s^(-1); Km: 138.9 uM / 1000 = 0.1389 mM, carried at the export's three-decimal precision as 0.139 mM; kcat_over_km: 0.138 / 0.139 = 0.9928057553956835 s^(-1) mM^(-1), the quotient of the same-column kcat and Km(app) cells

raw_value_unit_evidence: TABLE 1, mouse Cyp1b1, DMBA: Km(app) 138.9 uM; kcat = Vmax/Et 8.28 min^(-1); printed catalytic efficiency [kcat/Km(app)] 59.6 mM^(-1) min^(-1)

row_label: Cyp1b1 block; DMBA column

table_label: TABLE 1


substrate_name: Retinol

column_label: TABLE 1 'Kinetics of retinoid and DMBA metabolism by CYP1B1 and Cyp1b1'; Cyp1b1 row block; column 'Retinol'; cell 'Km(app) (uM)' = 392.2 and cell 'kcat = Vmax/Et (min-1)' = 0.24; same table, same row block, same substrate column; column header line: Retinol         Retinal        DMBA

normalized_value_unit_evidence: kcat: 0.24 min^(-1) / 60 = 0.004 s^(-1); Km: 392.2 uM / 1000 = 0.3922 mM, carried at the export's three-decimal precision as 0.392 mM; kcat_over_km: 0.004 / 0.392 = 0.01020408163265306 s^(-1) mM^(-1), the quotient of the same-column kcat and Km(app) cells

raw_value_unit_evidence: TABLE 1, mouse Cyp1b1, Retinol: Km(app) 392.2 uM; kcat = Vmax/Et 0.24 min^(-1); printed catalytic efficiency [kcat/Km(app)] 0.6 mM^(-1) min^(-1)

row_label: Cyp1b1 block; Retinol column

substrate: Retinol


substrate_name: all-trans-Retinal

column_label: TABLE 1 'Kinetics of retinoid and DMBA metabolism by CYP1B1 and Cyp1b1'; Cyp1b1 row block; column 'Retinal'; cell 'Km(app) (uM)' = 153.9 and cell 'kcat = Vmax/Et (min-1)' = 0.52; same table, same row block, same substrate column; column header line: Retinol         Retinal        DMBA

normalized_value_unit_evidence: kcat: 0.52 min^(-1) / 60 = 0.008666666666666666 s^(-1), carried at the export's three-decimal precision as 0.009 s^(-1); Km: 153.9 uM / 1000 = 0.1539 mM, carried at the export's three-decimal precision as 0.154 mM; kcat_over_km: 0.009 / 0.154 = 0.05844155844155844 s^(-1) mM^(-1), the quotient of the same-column kcat and Km(app) cells

raw_value_unit_evidence: TABLE 1, mouse Cyp1b1, Retinal: Km(app) 153.9 uM; kcat = Vmax/Et 0.52 min^(-1); printed catalytic efficiency [kcat/Km(app)] 3.4 mM^(-1) min^(-1)

row_label: Cyp1b1 block; Retinal column

substrate: all-trans-Retinal


substrate_name: NADPH; Coumarin; O2; H+

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant C6K

substrate: NADPH; Coumarin; O2; H+


substrate_name: H+; NADPH; O2; Coumarin

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant C6S

substrate: H+; NADPH; O2; Coumarin


substrate_name: NADPH; O2; Coumarin; H+

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) wildtype C6F

substrate: NADPH; O2; Coumarin; H+


substrate_name: NADPH; H+; O2; Coumarin

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant C6V

substrate: NADPH; H+; O2; Coumarin


substrate_name: Deltamethrin

column_label: Table 1, deltamethrin/CYP2C19 row: Vmax 61.6 +/- 17.7; Km 9.0 +/- 5.6 uM; Vmax/Km column a 6.8.

row_label: Deltamethrin / CYP2C19

table_label: Table 1

substrate: Deltamethrin


substrate_name: Esfenvalerate

column_label: Table 1, esfenvalerate/CYP2C8 row: Vmax 59.2 +/- 21.6; Km 19.1 +/- 11.6 uM; Vmax/Km column a 3.1.

row_label: Esfenvalerate / CYP2C8

substrate: Esfenvalerate


column_label: Table 1, esfenvalerate/CYP2C9*1 row: Vmax 79.8 +/- 6.3; Km 24.3 +/- 5.6 uM; Vmax/Km column a 3.3.

row_label: Esfenvalerate / CYP2C9*1


substrate_name: NADPH; O2; Esfenvalerate; H+

substrate: NADPH; O2; Esfenvalerate; H+


column_label: Table 1, deltamethrin/CYP2C8 row: Vmax 42.7 +/- 16.6; Km 10.2 +/- 9.5 uM; Vmax/Km column a 4.2.

row_label: Deltamethrin / CYP2C8


column_label: Table 1, esfenvalerate/CYP2C19 row: Vmax 64.4 +/- 12.3; Km 4.1 +/- 2.2 uM; Vmax/Km column a 15.7.

row_label: Esfenvalerate / CYP2C19


substrate_name: Deltamethrin; NADPH; O2; H+

substrate: Deltamethrin; NADPH; O2; H+


substrate_name: O2; H+; NADPH; 7-Ethoxycoumarin

substrate: O2; H+; NADPH; 7-Ethoxycoumarin


substrate_name: NADPH; O2; 7-Ethoxycoumarin; H+

substrate: NADPH; O2; 7-Ethoxycoumarin; H+


substrate_name: O2; NADPH; H+; 7-Ethoxycoumarin

substrate: O2; NADPH; H+; 7-Ethoxycoumarin


substrate_name: O2; 7-Ethoxycoumarin; NADPH; H+

substrate: O2; 7-Ethoxycoumarin; NADPH; H+


organism: Rattus norvegicus


enzyme_display_name: beta-lactamase

organism: Stenotrophomonas maltophilia

substrate_name: Imipenem

enzyme: beta-lactamase

substrate: Imipenem


substrate_name: Epicillin

substrate: Epicillin


substrate_name: tazobactam

substrate: tazobactam


substrate_name: Temocillin

substrate: Temocillin


substrate_name: piperacillin

substrate: piperacillin


substrate_name: azlocillin

substrate: azlocillin


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: Meropenem

substrate: Meropenem


substrate_name: NADPH; H+; Phenacetin; O2

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2A13 A117V

substrate: NADPH; H+; Phenacetin; O2


substrate_name: H+; O2; NADPH; Phenacetin

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2A13 A213S

substrate: H+; O2; NADPH; Phenacetin


substrate_name: NADPH; Phenacetin; O2; H+

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2A6 I300F/G301A/S369G

substrate: NADPH; Phenacetin; O2; H+


substrate_name: NADPH; H+; O2; Phenacetin

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2A6 I208S/I300F/G301A

substrate: NADPH; H+; O2; Phenacetin


substrate_name: O2; H+; Phenacetin; NADPH

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2A13 L366I

substrate: O2; H+; Phenacetin; NADPH


substrate_name: NADPH; Phenacetin; H+; O2

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2A13 S208I

substrate: NADPH; Phenacetin; H+; O2


substrate_name: Phenacetin; H+; NADPH; O2

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2A6 I208S/I300G/G301A

substrate: Phenacetin; H+; NADPH; O2


substrate_name: H+; NADPH; O2; Phenacetin

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2A6 I208S/I300F/G301A/G369S

substrate: H+; NADPH; O2; Phenacetin


substrate_name: Deltamethrin

sequence_source: UniProtKB reviewed (Swiss-Prot)

substrate: Deltamethrin


substrate_name: Reduced flavoprotein; O2; 5-Methoxy-N,N-diisopropyltryptamine


substrate_name: 5-Methoxy-N,N-diisopropyltryptamine; Reduced flavoprotein; O2


substrate_name: 5-Methoxy-N,N-diisopropyltryptamine; O2; Reduced flavoprotein


substrate: 5-Methoxy-N,N-diisopropyltryptamine; Reduced flavoprotein; O2


substrate_name: O2; Reduced flavoprotein; 5-Methoxy-N,N-diisopropyltryptamine


substrate_name: Phenacetin

sequence_variant_note: Mutation signature P2A/I208S/I300F/G301A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: Phenacetin


sequence_variant_note: Mutation signature P2A/I300F/G301A/S369G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: O2; NADPH; Phenacetin; H+

sequence_variant_note: Mutation signature I300F/G301A/G369S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2A6 I300F/G301A/G369S

substrate: O2; NADPH; Phenacetin; H+


substrate_name: NADPH; O2; Phenacetin; H+

sequence_variant_note: Resolved canonical sequence from uniprot_fasta and applied mutation signature I300F/G301A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2A6 I300F/G301A

substrate: NADPH; O2; Phenacetin; H+


substrate_name: Phenacetin; O2; NADPH; H+

substrate: Phenacetin; O2; NADPH; H+


substrate_name: H+; Phenacetin; O2; NADPH

sequence_variant_note: Resolved canonical sequence from uniprot_fasta and applied mutation signature H372R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2A13 H372R

substrate: H+; Phenacetin; O2; NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_fasta and applied mutation signature M365V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2A13 M365V


substrate_name: O2; NADPH; H+; Phenacetin

sequence_variant_note: Resolved canonical sequence from uniprot_fasta and applied mutation signature G369S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant CYP2A13 G369S

substrate: O2; NADPH; H+; Phenacetin


substrate_name: cefpirome

assay_conditions_summary: pH 6.5; 303.15 K; buffer 30 mM sodium cacodylate

column_label: Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row Cefpirome / X. maltophilia ULA-511, column X. maltophilia ULA-511; Km uM, raw cell 320 +/- 20, normalized 0.32 mM; Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row Cefpirome / X. maltophilia ULA-511, column X. maltophilia ULA-511; kcat s^-1, raw cell 85.0, normalized 85 s^-1; Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row Cefpirome / X. maltophilia ULA-511, column X. maltophilia ULA-511; kcat/Km M^-1 s^-1, raw cell 2.65 x 10^5, normalized 265 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.32 normalized_unit=mM; kcat normalized_value=85 normalized_unit=s^-1; kcat/Km normalized_value=265 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=320 +/- 20 raw_unit=uM raw_cell=320 +/- 20; kcat raw_value=85.0 raw_unit=s^-1 raw_cell=85.0; kcat/Km raw_value=2.65 x 10^5 raw_unit=M^-1*s^-1 raw_cell=2.65 x 10^5

row_label: Cefpirome / X. maltophilia ULA-511

substrate: cefpirome


substrate_name: Cefsulodin

column_label: Table 5: Kinetic parameters of metallo-beta-lactamases with cephalosporins (Delta3-cephems); organism block X. maltophilia ULA-511 (now Stenotrophomonas maltophilia); row Cefsulodin; Km raw 5 uM normalized 0.005 mM; kcat raw 7.5 s^-1 normalized 7.5 s^-1; kcat/Km raw 1500000.0 M^-1 s^-1 normalized 1500 s^-1 mM^-1.

row_label: X. maltophilia ULA-511 (now Stenotrophomonas maltophilia) / Cefsulodin

substrate: Cefsulodin


substrate_name: Talampicillin

substrate: Talampicillin


column_label: Table 6: Kinetic parameters of metallo-beta-lactamases with penems, tazobactam (YTR-830), and carumonam; organism block X. maltophilia ULA-511 (now Stenotrophomonas maltophilia); row HRE-664; Km raw 20 uM normalized 0.02 mM; kcat raw 1.5 s^-1 normalized 1.5 s^-1; kcat/Km raw 75000.0 M^-1 s^-1 normalized 75 s^-1 mM^-1.

row_label: X. maltophilia ULA-511 (now Stenotrophomonas maltophilia) / HRE-664


column_label: Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row CGP-31523A / X. maltophilia ULA-511, column X. maltophilia ULA-511; Km uM, raw cell 27 +/- 2, normalized 0.027 mM; Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row CGP-31523A / X. maltophilia ULA-511, column X. maltophilia ULA-511; kcat s^-1, raw cell 38.0, normalized 38 s^-1; Table 5. Kinetic parameters of metallo-beta-lactamases with cephalosporins (D3-cephems) row CGP-31523A / X. maltophilia ULA-511, column X. maltophilia ULA-511; kcat/Km M^-1 s^-1, raw cell 1.40 x 10^6, normalized 1400 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.027 normalized_unit=mM; kcat normalized_value=38 normalized_unit=s^-1; kcat/Km normalized_value=1400 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=27 +/- 2 raw_unit=uM raw_cell=27 +/- 2; kcat raw_value=38.0 raw_unit=s^-1 raw_cell=38.0; kcat/Km raw_value=1.40 x 10^6 raw_unit=M^-1*s^-1 raw_cell=1.40 x 10^6

row_label: CGP-31523A / X. maltophilia ULA-511


substrate_name: Asparenomycin A

column_label: Table 7: Kinetic parameters of metallo-beta-lactamases with carbapenem antibiotics; organism block X. maltophilia ULA-511 (now Stenotrophomonas maltophilia); row Asparenomycin A; Km raw 2 uM normalized 0.002 mM; kcat raw 14 s^-1 normalized 14 s^-1; kcat/Km raw 7000000.0 M^-1 s^-1 normalized 7000 s^-1 mM^-1.

row_label: X. maltophilia ULA-511 (now Stenotrophomonas maltophilia) / Asparenomycin A

substrate: Asparenomycin A


substrate_name: Sulbenicillin

column_label: Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins row Sulbenicillin / X. maltophilia ULA-511, column X. maltophilia ULA-511; Km uM, raw cell 190 +/- 5, normalized 0.19 mM; Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins row Sulbenicillin / X. maltophilia ULA-511, column X. maltophilia ULA-511; kcat s^-1, raw cell 225, normalized 225 s^-1; Table 4. Kinetic parameters of metallo-beta-lactamases with penicillins row Sulbenicillin / X. maltophilia ULA-511, column X. maltophilia ULA-511; kcat/Km M^-1 s^-1, raw cell 1.20 x 10^6, normalized 1200 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.19 normalized_unit=mM; kcat normalized_value=225 normalized_unit=s^-1; kcat/Km normalized_value=1200 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=190 +/- 5 raw_unit=uM raw_cell=190 +/- 5; kcat raw_value=225 raw_unit=s^-1 raw_cell=225; kcat/Km raw_value=1.20 x 10^6 raw_unit=M^-1*s^-1 raw_cell=1.20 x 10^6

row_label: Sulbenicillin / X. maltophilia ULA-511

substrate: Sulbenicillin


substrate_name: Ticarcillin

assay_conditions_summary: pH 6.5; 303.15 K; buffer this record. Assay condition: 30 mM sodium cacodylate

column_label: Table 4 (PDF page 5 of 8, printed page 196), antibiotic row `Ticarcillin`, enzyme block `X. maltophilia ULA-511`: Km (uM) = 140 +/- 2; kcat (s-1) = 375; kcat/Km (M-1 s-1) = 2.70 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 375 s-1 -> 375 s^(-1) (the printed unit is already per second); the exported value is 440 s^(-1). Km: printed cell 140 +/- 2 uM -> 0.14 mM (divide by 1000); the exported value is 0.14 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.70 x 10^6 M-1 s-1 for this cell block -> 2700 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1; the per-second part is unchanged); the exported value is 3142.8571428571427 s^(-1)*mM^(-1).

row_label: Table 4, decoded plain-numeral transcription, antibiotic row `Ticarcillin`, enzyme block `X. maltophilia ULA-511`

table_label: Table 4 (PDF page 5 of 8, printed page 196) 'Kinetic parameters of metallo-b-lactamases with penicillins'

substrate: Ticarcillin


substrate_name: Imipenem

column_label: Table 3 scanned page 154; enzyme block Pseudomonas maltophilia ULA-511 L-1 enzyme; row label Imipenem; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; P. maltophilia experiments at 35 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: Imipenem

table_label: Table 3

substrate: Imipenem


substrate_name: Cephaloglycin

column_label: Table 3 scanned page 154; enzyme block Pseudomonas maltophilia ULA-511 L-1 enzyme; row label Cephaloglycin; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; P. maltophilia experiments at 35 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: Cephaloglycin

substrate: Cephaloglycin


substrate_name: cefoxitin

column_label: Table 3 scanned page 154; enzyme block Pseudomonas maltophilia ULA-511 L-1 enzyme; row label cefoxitin; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; P. maltophilia experiments at 35 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: cefoxitin

substrate: cefoxitin


substrate_name: cefotaxime

column_label: Table 3 scanned page 154; enzyme block Pseudomonas maltophilia ULA-511 L-1 enzyme; row label cefotaxime; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; P. maltophilia experiments at 35 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: cefotaxime

substrate: cefotaxime


substrate_name: Sulbactam

column_label: Table 3 scanned page 154; enzyme block Pseudomonas maltophilia ULA-511 L-1 enzyme; row label Sulbactam; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; P. maltophilia experiments at 35 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: Sulbactam

substrate: Sulbactam


substrate_name: carbenicillin

column_label: Table 3 scanned page 154; enzyme block Pseudomonas maltophilia ULA-511 L-1 enzyme; row label carbenicillin; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; P. maltophilia experiments at 35 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: carbenicillin

substrate: carbenicillin


substrate_name: moxalactam

column_label: Table 3 scanned page 154; enzyme block Pseudomonas maltophilia ULA-511 L-1 enzyme; row label moxalactam; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; P. maltophilia experiments at 35 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: moxalactam

substrate: moxalactam


substrate_name: Cefuroxime

column_label: Table 3 scanned page 154; enzyme block Pseudomonas maltophilia ULA-511 L-1 enzyme; row label Cefuroxime; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; P. maltophilia experiments at 35 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: Cefuroxime

substrate: Cefuroxime


substrate_name: cefprozil

substrate: cefprozil


substrate_name: biapenem

substrate: biapenem


substrate_name: Cephaloridine

substrate: Cephaloridine


substrate_name: cefadroxil

substrate: cefadroxil


enzyme_display_name: pyruvate kinase

organism: Bos taurus

substrate_name: ADP; Phosphoenolpyruvate

source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org)

ki_unit: mM

assay_conditions_summary: pH 7; 298.15 K; cofactor ADP

proof_lines:
cosubstrate ADP
L-type isozyme, 25°C, pH 7.0
M-type isozyme, 25°C, pH 7.0

enzyme: pyruvate kinase

substrate: ADP; Phosphoenolpyruvate


organism: Candida tropicalis

substrate_name: myristic acid

source_db: brenda

proof_lines:
isozyme CYP52A17, pH 7.4, 35°C
isozyme CYP52A13, pH 7.4, 35°C

substrate: myristic acid

source: brenda


substrate_name: Phosphoenolpyruvate; ADP

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ADP

proof_lines:
cosubstrate phosphoenolpyruvate
apparent value
L-type isozyme, pH 7.4, 37°C

substrate: Phosphoenolpyruvate; ADP


organism: Monoraphidium minutum

substrate_name: ADP

assay_conditions_summary: cofactor ADP

proof_lines:
PKc-isozyme
cosubstrate phosphoenolpyruvate
isozyme PKc

substrate: ADP


substrate_name: 5-Methoxy-N,N-diisopropyltryptamine; O2; Reduced flavoprotein


substrate_name: Bufuralol

substrate: Bufuralol


substrate_name: Bufuralol; NADP+

substrate: Bufuralol; NADP+


substrate_name: NADP+; Bufuralol

sequence_source: UniProtKB reviewed (Swiss-Prot); secondary accession P13108 -> primary Q64680

substrate: NADP+; Bufuralol


organism: Rattus rattus

substrate_name: [reduced NADPH-hemoprotein reductase]; O2; 1,4-Cineole


organism: Salmonella enterica subsp. enterica serovar Typhimurium

assay_conditions_summary: pH 6.8; 303.15 K; cofactor ADP

proof_lines:
isozyme II, 30°C, pH 6.8
enzyme form I
30°C, pH 6.8


organism: Ricinus communis

assay_conditions_summary: pH 7.9; 298.15 K; cofactor ADP

proof_lines:
25°C, pH 7.9
pH 7.5, 30°C
ADP in form of MgADP-


substrate_name: Cephalosporin C

assay_conditions_summary: pH 7; 298.15 K; buffer 50 mM phosphate

column_label: Table 1; row Cephalosporin C / Recombinant L1; column Km (uM) raw value 180; column kcat (s^-1) raw value 280; column kcat/Km (s^-1 uM^-1) raw value 1.6

normalized_value_unit_evidence: kcat normalized_value=280 normalized_unit=s^-1; Km normalized_value=0.18 normalized_unit=mM; kcat/Km normalized_value=1600 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=280 raw_unit=s^-1; Km raw_value=180 raw_unit=uM; kcat/Km raw_value=1.6 raw_unit=s^-1*uM^-1

row_label: Cephalosporin C / Recombinant L1

table_label: Table 1. Steady-state kinetic constants of recombinant L1 and metallo-beta-lactamase isolated from S. maltophilia ULA-511

substrate: Cephalosporin C


substrate_name: Cephalothin

substrate: Cephalothin


substrate_name: Cefaclor

substrate: Cefaclor


substrate_name: cefmetazole

column_label: Table 1; row cefmetazole / Recombinant L1; column Km (uM) raw value 4.1; column kcat (s^-1) raw value 4.7; column kcat/Km (s^-1 uM^-1) raw value 1.1

normalized_value_unit_evidence: kcat normalized_value=4.7 normalized_unit=s^-1; Km normalized_value=0.0041 normalized_unit=mM; kcat/Km normalized_value=1100 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=4.7 raw_unit=s^-1; Km raw_value=4.1 raw_unit=uM; kcat/Km raw_value=1.1 raw_unit=s^-1*uM^-1

row_label: cefmetazole / Recombinant L1

substrate: cefmetazole


substrate_name: cefepime

substrate: cefepime


substrate_name: Ampicillin

substrate: Ampicillin


substrate_name: moxalactam

column_label: Table 1; row moxalactam / Recombinant L1; column Km (uM) raw value 5; column kcat (s^-1) raw value 0.15; column kcat/Km (s^-1 uM^-1) raw value 0.030

normalized_value_unit_evidence: kcat normalized_value=0.15 normalized_unit=s^-1; Km normalized_value=0.005 normalized_unit=mM; kcat/Km normalized_value=30 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.15 raw_unit=s^-1; Km raw_value=5 raw_unit=uM; kcat/Km raw_value=0.030 raw_unit=s^-1*uM^-1

row_label: moxalactam / Recombinant L1

substrate: moxalactam


substrate_name: Nitrocefin

substrate: Nitrocefin


enzyme_display_name: glutathione transferase

organism: Drosophila melanogaster

enzyme: glutathione transferase


substrate_name: reduced glutathione

substrate: reduced glutathione


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant DmGSTE13 (R208W)


assay_conditions_summary: pH 6.5; buffer 0.1 M potassium phosphate

column_label: PMID 22082028 Table 2; row DmGSTS1-1; columns Vmax, kcat, GSH Km; ResearchGate public full-text lines 873-879.

raw_value_unit_evidence: Vmax 4.53 umol min^-1 mg^-1; kcat 1.81 s^-1; GSH Km 0.52 mM

row_label: DmGSTS1-1 / GSH

table_label: PMID 22082028 Table 2. Kinetic parameters of DmGSTs and purification schemes


assay_conditions_summary: pH 6.5; 298.15 K; buffer 0.1 M potassium phosphate

column_label: PMID 22082028 Table 2; row DmGSTE7-7; columns Vmax, kcat, GSH Km, GSH kcat/Km

raw_value_unit_evidence: Vmax 81.8 umol min^-1 mg^-1; kcat 34.7 s^-1; GSH Km 0.78 mM; GSH kcat/Km 45 s^-1 mM^-1

row_label: DmGSTE7-7 / GSH


proof_lines: PMID 22082028 Table 1 labels DmGSTT3b as WT.

proof_lines: PMID 22082028 Table 2 row DmGSTT3b-3b reports kcat 0.41 s^-1, GSH Km 6.84 mM, and GSH kcat/Km 0.06 s^-1*mM^-1.


column_label: PMID 22082028 Table 2; row DmGSTE3-3; columns Vmax, kcat, GSH Km; ResearchGate public full-text lines 714-720.

raw_value_unit_evidence: Vmax 63.9 umol min^-1 mg^-1; kcat 26.6 s^-1; GSH Km 0.46 mM

row_label: DmGSTE3-3 / GSH


proof_lines: PMID 22082028 Table 1 labels DmGSTE11 as WT.

proof_lines: PMID 22082028 Table 2 row DmGSTE11-11 reports kcat 60.2 s^-1, GSH Km 38.5 mM, and GSH kcat/Km 1.56 s^-1*mM^-1.


proof_lines: PMID 22082028 Table 1 labels DmGSTD9 as WT.

proof_lines: PMID 22082028 Table 2 row DmGSTD9-9 reports kcat 3.63 s^-1, GSH Km 0.30 mM, and GSH kcat/Km 12 s^-1*mM^-1.


proof_lines: PMID 22082028 Table 1 labels DmGSTE13 as R208W relative to the Drosophila database sequence.

proof_lines: PMID 22082028 Table 2 row DmGSTE13-13 reports kcat 204 s^-1, GSH Km 1.05 mM, and GSH kcat/Km 194 s^-1*mM^-1.


proof_lines: PMID 22082028 Table 1 labels DmGSTT2 as G61D/N93D/V194M relative to the Drosophila database sequence.

proof_lines: PMID 22082028 Table 2 row DmGSTT2-2 reports Vmax 107 umol*min^-1*mg^-1, kcat 47.6 s^-1, CDNB Km 1.05 mM, and GSH Km 10.7 mM.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E142V to reconstruct the assayed variant sequence.


column_label: PMID 22082028 Table 2; row DmGSTD8-8; columns Vmax, kcat, CDNB Km, CDNB kcat/Km

raw_value_unit_evidence: Vmax 11.2 umol min^-1 mg^-1; kcat 4.49 s^-1; CDNB Km 0.64 mM; CDNB kcat/Km 7 s^-1 mM^-1

row_label: DmGSTD8-8 / CDNB


column_label: PMID 22082028 Table 2; row DmGSTD11a-11a; columns Vmax, kcat, GSH Km, GSH kcat/Km

raw_value_unit_evidence: Vmax 848 umol min^-1 mg^-1; kcat 360 s^-1; GSH Km 0.99 mM; GSH kcat/Km 360 s^-1 mM^-1

row_label: DmGSTD11a-11a / GSH


column_label: PMID 22082028 Table 2; row DmGSTD1-1; columns Vmax, kcat, CDNB Km, CDNB kcat/Km

raw_value_unit_evidence: Vmax 84.2 umol min^-1 mg^-1; kcat 33.5 s^-1; CDNB Km 0.45 mM; CDNB kcat/Km 74 s^-1 mM^-1

row_label: DmGSTD1-1 / CDNB


column_label: PMID 22082028 Table 2; row DmGSTE6-6; columns Vmax, kcat, GSH Km, GSH kcat/Km

raw_value_unit_evidence: Vmax 208 umol min^-1 mg^-1; kcat 86.8 s^-1; GSH Km 1.71 mM; GSH kcat/Km 50.8 s^-1 mM^-1

row_label: DmGSTE6-6 / GSH


column_label: PMID 22082028 Table 2; row DmGSTE12-12; columns Vmax, kcat, CDNB Km; ResearchGate public full-text lines 777-782.

raw_value_unit_evidence: Vmax 43.8 umol min^-1 mg^-1; kcat 18.4 s^-1; CDNB Km 0.05 mM

row_label: DmGSTE12-12 / CDNB


column_label: PMID 22082028 Table 2; row DmGSTD2-2; columns Vmax, kcat, CDNB Km, CDNB kcat/Km

raw_value_unit_evidence: Vmax 0.53 umol min^-1 mg^-1; kcat 0.22 s^-1; CDNB Km 0.81 mM; CDNB kcat/Km 0.27 s^-1 mM^-1

row_label: DmGSTD2-2 / CDNB


organism: Arabidopsis thaliana

substrate_name: acrolein

smiles: C=CC=O

substrate: acrolein


organism: Bombyx mori

source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=6.5


organism: Caenorhabditis elegans


column_label: Table 2; row DmGSTE12-12; column kcat (s^-1) raw value 18.4; column Km (mM) GSH block raw value 2.44; column kcat/Km (s^-1 mM^-1) GSH block; printed cell 7.52.

normalized_value_unit_evidence: kcat 18.4 s^-1 = 18.4 s^-1. Km 2.44 mM = 2.44 mM (GSH column). kcat/Km reported in s^-1 mM^-1 needs no unit change.

raw_value_unit_evidence: DmGSTE12-12 row, GSH block: kcat 18.4 s^-1; GSH Km 2.44 mM; GSH kcat/Km 7.52 s^-1 mM^-1; Vmax 43.8 umol min^-1 mg^-1; purification An, HIC.

row_label: DmGSTE12-12 | GSH

table_label: Table 2 Kinetic parameters of DmGSTs and purification schemes


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant DmGSTD4 (E142V)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q7KK90 and applied mutation signature K25N/S117C/T145A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of DmGSTs and purification schemes), enzyme row 'DmGSTE1-1', GSH column group; column 'k cat (s-1)' = 35.1; column 'K m (mM)' under the GSH head = 1.43; column 'k cat /K m (s-1 mM-1)' under the GSH head = 24.6; the CDNB column group of the same enzyme row prints K m 0.15 mM and k cat /K m 230 s-1 mM-1; column 'V max (umol min-1 mg-1)' = 84.5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 35.1 s^-1; the printed turnover column is already per second, so no unit conversion applies and the exported value is 35.1 s^(-1). Km: printed Table 2 cell 1.43 mM; the printed constant is already in mM, so no unit conversion applies and the exported value is 1.43 mM. kcat/Km: printed Table 2 cell 24.6 s^-1 mM^-1; the printed efficiency column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell carries as 24.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row DmGSTE1-1, GSH column group: kcat = 35.1 s^-1; Km = 1.43 mM; printed kcat/Km = 24.6 s^-1 mM^-1.

table_label: Table 2: Kinetic parameters of DmGSTs and purification schemes (Biochem. J. 2012, 442:181-190)


column_label: Table 2; row DmGSTE4-4; column kcat (s^-1) raw value 83.7; column Km (mM) GSH block raw value 40.7; column kcat/Km (s^-1 mM^-1) GSH block; the printed cell is 2.06 and the value used here is the exact quotient of the same row kcat and Km cells, which agrees with the printed cell at its printed precision.

normalized_value_unit_evidence: kcat 83.7 s^-1 = 83.7 s^-1. Km 40.7 mM = 40.7 mM (GSH column). kcat/Km reported in s^-1 mM^-1 needs no unit change.

raw_value_unit_evidence: DmGSTE4-4 row, GSH block: kcat 83.7 s^-1; GSH Km 40.7 mM; GSH kcat/Km 2.06 s^-1 mM^-1; Vmax 198 umol min^-1 mg^-1; purification GSTrap.

row_label: DmGSTE4-4 | GSH


column_label: Table 2; row DmGSTO2b-2b; column kcat (s^-1) raw value 0.03; column Km (mM) CDNB block raw value 1.63; column kcat/Km (s^-1 mM^-1) CDNB block; the printed cell is 0.02 and the value used here is the exact quotient of the same row kcat and Km cells, which agrees with the printed cell at its printed precision.

normalized_value_unit_evidence: kcat 0.03 s^-1 = 0.03 s^-1. Km 1.63 mM = 1.63 mM (CDNB column). kcat/Km reported in s^-1 mM^-1 needs no unit change.

raw_value_unit_evidence: DmGSTO2b-2b row, CDNB block: kcat 0.03 s^-1; CDNB Km 1.63 mM; CDNB kcat/Km 0.02 s^-1 mM^-1; Vmax 0.05 umol min^-1 mg^-1; purification An.

row_label: DmGSTO2b-2b | CDNB


sequence_variant_note: Mutation signature K181E matches the mutant residue at offset +0 and the reference residue at offset +13; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


column_label: Table 2; row DmGSTD11a-11a; column kcat (s^-1) raw value 360; column Km (mM) CDNB block raw value 1.28; column kcat/Km (s^-1 mM^-1) CDNB block; the printed cell is 281.0 and the value used here is the exact quotient of the same row kcat and Km cells, which agrees with the printed cell at its printed precision.

normalized_value_unit_evidence: kcat 360 s^-1 = 360.0 s^-1. Km 1.28 mM = 1.28 mM (CDNB column). kcat/Km reported in s^-1 mM^-1 needs no unit change.

raw_value_unit_evidence: DmGSTD11a-11a row, CDNB block: kcat 360 s^-1; CDNB Km 1.28 mM; CDNB kcat/Km 281 s^-1 mM^-1; Vmax 848 umol min^-1 mg^-1; purification GSTrap.

row_label: DmGSTD11a-11a | CDNB


sequence_variant_note: Mutation signature S135A matches the mutant residue at offset +0 and the reference residue at offset +10; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


organism: Anopheles dirus


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant R66A


assay_conditions_summary: pH 6.5; 298.15 K; buffer 0.1 M phosphate

column_label: Table 1 wild-type row, columns kcat, Km GSH, and kcat/Km GSH.

normalized_value_unit_evidence: kcat=35.4 s^-1; Km GSH=0.27 mM; explicit paper kcat/Km GSH=130.69 s^-1 mM^-1.

raw_value_unit_evidence: Wild-type row reports kcat 35.4 s^-1; Km GSH 0.27 +/- 0.05 mM; kcat/Km GSH 130.69 s^-1/mM.

row_label: Wild-type adGSTD3-3

table_label: Table 1. Steady-state kinetic parameters and pKa values for wild-type and mutant adGSTD3-3


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant M101A


column_label: Table 2; row DmGSTD6-6; column kcat (s^-1) raw value 0.03; column Km (mM) CDNB block raw value 3.79; column kcat/Km (s^-1 mM^-1) CDNB block; the printed cell is 0.01 and the value used here is the exact quotient of the same row kcat and Km cells, which agrees with the printed cell at its printed precision.

normalized_value_unit_evidence: kcat 0.03 s^-1 = 0.03 s^-1. Km 3.79 mM = 3.79 mM (CDNB column). kcat/Km reported in s^-1 mM^-1 needs no unit change.

raw_value_unit_evidence: DmGSTD6-6 row, CDNB block: kcat 0.03 s^-1; CDNB Km 3.79 mM; CDNB kcat/Km 0.01 s^-1 mM^-1; Vmax 0.07 umol min^-1 mg^-1; purification An, HIC.

row_label: DmGSTD6-6 | CDNB


column_label: Table 2; row DmGSTD5-5; column kcat (s^-1) raw value 4.08; column Km (mM) CDNB block raw value 2.98; column kcat/Km (s^-1 mM^-1) CDNB block; the printed cell is 1.37 and the value used here is the exact quotient of the same row kcat and Km cells, which agrees with the printed cell at its printed precision.

normalized_value_unit_evidence: kcat 4.08 s^-1 = 4.08 s^-1. Km 2.98 mM = 2.98 mM (CDNB column). kcat/Km reported in s^-1 mM^-1 needs no unit change.

raw_value_unit_evidence: DmGSTD5-5 row, CDNB block: kcat 4.08 s^-1; CDNB Km 2.98 mM; CDNB kcat/Km 1.37 s^-1 mM^-1; Vmax 9.90 umol min^-1 mg^-1; purification An.

row_label: DmGSTD5-5 | CDNB


column_label: Table 2; row DmGSTE3-3; column kcat (s^-1) raw value 26.6; column Km (mM) CDNB block raw value 1.51; column kcat/Km (s^-1 mM^-1) CDNB block; the printed cell is 17.6 and the value used here is the exact quotient of the same row kcat and Km cells, which agrees with the printed cell at its printed precision.

normalized_value_unit_evidence: kcat 26.6 s^-1 = 26.6 s^-1. Km 1.51 mM = 1.51 mM (CDNB column). kcat/Km reported in s^-1 mM^-1 needs no unit change.

raw_value_unit_evidence: DmGSTE3-3 row, CDNB block: kcat 26.6 s^-1; CDNB Km 1.51 mM; CDNB kcat/Km 17.6 s^-1 mM^-1; Vmax 63.9 umol min^-1 mg^-1; purification GSTrap.

row_label: DmGSTE3-3 | CDNB


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant DmGSTE5 (K181E)


column_label: Table 2 (Kinetic parameters of DmGSTs and purification schemes), enzyme row 'DmGSTE1-1', CDNB column group; column 'k cat (s-1)' = 35.1; column 'K m (mM)' under the CDNB head = 0.15; column 'k cat /K m (s-1 mM-1)' under the CDNB head = 230; the GSH column group of the same enzyme row prints K m 1.43 mM and k cat /K m 24.6 s-1 mM-1; column 'V max (umol min-1 mg-1)' = 84.5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 35.1 s^-1; the printed turnover column is already per second, so no unit conversion applies and the exported value is 35.1 s^(-1). Km: printed Table 2 cell 0.15 mM; the printed constant is already in mM, so no unit conversion applies and the exported value is 0.15 mM. kcat/Km: printed Table 2 cell 230 s^-1 mM^-1; the printed efficiency column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell carries as 230.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row DmGSTE1-1, CDNB column group: kcat = 35.1 s^-1; Km = 0.15 mM; printed kcat/Km = 230 s^-1 mM^-1.


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant DmGSTT1 (S135A)


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant DmGSTE2 (N82K)


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant DmGSTO1 (C160G)


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) wildtype DmGSTE7 (M126T)


column_label: Table 2; row DmGSTD8-8; column kcat (s^-1) raw value 4.49; column Km (mM) GSH block raw value 1.10; column kcat/Km (s^-1 mM^-1) GSH block; the printed cell is 4.08 and the value used here is the exact quotient of the same row kcat and Km cells, which agrees with the printed cell at its printed precision.

normalized_value_unit_evidence: kcat 4.49 s^-1 = 4.49 s^-1. Km 1.10 mM = 1.1 mM (GSH column). kcat/Km reported in s^-1 mM^-1 needs no unit change.

raw_value_unit_evidence: DmGSTD8-8 row, GSH block: kcat 4.49 s^-1; GSH Km 1.10 mM; GSH kcat/Km 4.08 s^-1 mM^-1; Vmax 11.2 umol min^-1 mg^-1; purification An, HIC.

row_label: DmGSTD8-8 | GSH


column_label: Table 2 (Kinetic parameters of DmGSTs and purification schemes), enzyme row 'DmGSTE4-4', CDNB column group; column 'k cat (s-1)' = 83.7; column 'K m (mM)' under the CDNB head = 0.29; column 'k cat /K m (s-1 mM-1)' under the CDNB head = 280; the GSH column group of the same enzyme row prints K m 40.7 mM and k cat /K m 2.06 s-1 mM-1; column 'V max (umol min-1 mg-1)' = 198.

normalized_value_unit_evidence: kcat: printed Table 2 cell 83.7 s^-1; the printed turnover column is already per second, so no unit conversion applies and the exported value is 83.7 s^(-1). Km: printed Table 2 cell 0.29 mM; the printed constant is already in mM, so no unit conversion applies and the exported value is 0.29 mM. kcat/Km: printed Table 2 cell 280 s^-1 mM^-1; the printed efficiency column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell carries as 280.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row DmGSTE4-4, CDNB column group: kcat = 83.7 s^-1; Km = 0.29 mM; printed kcat/Km = 280 s^-1 mM^-1.


column_label: Table 2 Kinetic parameters of DmGSTs and purification schemes; row DmGSTD10-10; purification column An, HIC; column kcat (s^-1) raw value 6.5; column Km (mM) of the GSH substrate block raw value 5.44; column kcat/Km (s^-1 mM^-1) of the GSH substrate block printed cell 1.2. The PDF text layer splits every plus/minus S.D. across two lines, so the row reads as the plus sign, then the Unicode minus and the S.D., then the next cell.

normalized_value_unit_evidence: metric: kcat; raw value: 6.5 s^-1; raw unit: s^-1; normalized value: 6.5 s^(-1); metric: Km; raw value: 5.44 mM; raw unit: mM; normalized value: 5.44 mM; metric: kcat/Km; normalized value: 1.1948529411764706 s^(-1)*mM^(-1); assay condition: GST activity assay at 25 C in 0.1 M potassium phosphate buffer, pH 6.5; steady-state kinetics with the CDNB concentration varied at a saturating GSH concentration and vice versa; Michaelis-Menten fit in GraphPad Prism 5; wild-type DmGST enzyme. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 6.5 s^-1 is already in s^-1, no conversion. Km 5.44 mM is already in mM, no conversion. kcat/Km is recorded as the quotient of this row's own two printed cells: paper kcat / paper Km = 6.5 / 5.44 = 1.1948529411764706 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 Kinetic parameters of DmGSTs and purification schemes; row DmGSTD10-10; GSH substrate block; metric: kcat; raw value: 6.5; raw unit: s^-1; metric: Km; raw value: 5.44; raw unit: mM; metric: kcat/Km; raw value: null (not taken from a printed cell); normalized value: 1.1948529411764706 s^-1 mM^-1; assay condition: GST activity assay at 25 C in 0.1 M potassium phosphate buffer, pH 6.5; steady-state kinetics with the CDNB concentration varied at a saturating GSH concentration and vice versa; Michaelis-Menten fit in GraphPad Prism 5; wild-type DmGST enzyme.


column_label: Table 2 (Kinetic parameters of DmGSTs and purification schemes), enzyme row 'DmGSTE11-11', CDNB column group; column 'k cat (s-1)' = 60.2; column 'K m (mM)' under the CDNB head = 0.01; column 'k cat /K m (s-1 mM-1)' under the CDNB head = 4600; the GSH column group of the same enzyme row prints K m 38.5 mM and k cat /K m 1.56 s-1 mM-1; column 'V max (umol min-1 mg-1)' = 144.

normalized_value_unit_evidence: kcat: printed Table 2 cell 60.2 s^-1; the printed turnover column is already per second, so no unit conversion applies and the exported value is 60.2 s^(-1). Km: printed Table 2 cell 0.01 mM; the printed constant is already in mM, so no unit conversion applies and the exported value is 0.01 mM. kcat/Km: printed Table 2 cell 4600 s^-1 mM^-1; the printed efficiency column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell carries as 4600.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row DmGSTE11-11, CDNB column group: kcat = 60.2 s^-1; Km = 0.01 mM; printed kcat/Km = 4600 s^-1 mM^-1.


column_label: Table 2 Kinetic parameters of DmGSTs and purification schemes; row DmGSTE14-14; purification column GSTrap; column kcat (s^-1) raw value 59.2; column Km (mM) of the GSH substrate block raw value 3.84; column kcat/Km (s^-1 mM^-1) of the GSH substrate block printed cell 15.4. The PDF text layer splits every plus/minus S.D. across two lines, so the row reads as the plus sign, then the Unicode minus and the S.D., then the next cell.

normalized_value_unit_evidence: metric: kcat; raw value: 59.2 s^-1; raw unit: s^-1; normalized value: 59.2 s^(-1); metric: Km; raw value: 3.84 mM; raw unit: mM; normalized value: 3.84 mM; metric: kcat/Km; normalized value: 15.416666666666668 s^(-1)*mM^(-1); assay condition: GST activity assay at 25 C in 0.1 M potassium phosphate buffer, pH 6.5; steady-state kinetics with the CDNB concentration varied at a saturating GSH concentration and vice versa; Michaelis-Menten fit in GraphPad Prism 5; wild-type DmGST enzyme. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 59.2 s^-1 is already in s^-1, no conversion. Km 3.84 mM is already in mM, no conversion. kcat/Km is recorded as the quotient of this row's own two printed cells: paper kcat / paper Km = 59.2 / 3.84 = 15.416666666666668 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 Kinetic parameters of DmGSTs and purification schemes; row DmGSTE14-14; GSH substrate block; metric: kcat; raw value: 59.2; raw unit: s^-1; metric: Km; raw value: 3.84; raw unit: mM; metric: kcat/Km; raw value: null (not taken from a printed cell); normalized value: 15.416666666666668 s^-1 mM^-1; assay condition: GST activity assay at 25 C in 0.1 M potassium phosphate buffer, pH 6.5; steady-state kinetics with the CDNB concentration varied at a saturating GSH concentration and vice versa; Michaelis-Menten fit in GraphPad Prism 5; wild-type DmGST enzyme.


column_label: Table 2 Kinetic parameters of DmGSTs and purification schemes; row DmGSTD5-5; purification column An; column kcat (s^-1) raw value 4.08; column Km (mM) of the GSH substrate block raw value 1.43; column kcat/Km (s^-1 mM^-1) of the GSH substrate block printed cell 2.85. The PDF text layer splits every plus/minus S.D. across two lines, so the row reads as the plus sign, then the Unicode minus and the S.D., then the next cell.

normalized_value_unit_evidence: metric: kcat; raw value: 4.08 s^-1; raw unit: s^-1; normalized value: 4.08 s^(-1); metric: Km; raw value: 1.43 mM; raw unit: mM; normalized value: 1.43 mM; metric: kcat/Km; normalized value: 2.8531468531468533 s^(-1)*mM^(-1); assay condition: GST activity assay at 25 C in 0.1 M potassium phosphate buffer, pH 6.5; steady-state kinetics with the CDNB concentration varied at a saturating GSH concentration and vice versa; Michaelis-Menten fit in GraphPad Prism 5; wild-type DmGST enzyme. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 4.08 s^-1 is already in s^-1, no conversion. Km 1.43 mM is already in mM, no conversion. kcat/Km is recorded as the quotient of this row's own two printed cells: paper kcat / paper Km = 4.08 / 1.43 = 2.8531468531468533 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 Kinetic parameters of DmGSTs and purification schemes; row DmGSTD5-5; GSH substrate block; metric: kcat; raw value: 4.08; raw unit: s^-1; metric: Km; raw value: 1.43; raw unit: mM; metric: kcat/Km; raw value: null (not taken from a printed cell); normalized value: 2.8531468531468533 s^-1 mM^-1; assay condition: GST activity assay at 25 C in 0.1 M potassium phosphate buffer, pH 6.5; steady-state kinetics with the CDNB concentration varied at a saturating GSH concentration and vice versa; Michaelis-Menten fit in GraphPad Prism 5; wild-type DmGST enzyme.


column_label: Table 2 Kinetic parameters of DmGSTs and purification schemes; row DmGSTE9-9; purification column GSTrap; column kcat (s^-1) raw value 42.7; column Km (mM) of the CDNB substrate block raw value 0.01; column kcat/Km (s^-1 mM^-1) of the CDNB substrate block printed cell 4300. The PDF text layer splits every plus/minus S.D. across two lines, so the row reads as the plus sign, then the Unicode minus and the S.D., then the next cell.

normalized_value_unit_evidence: metric: kcat; raw value: 42.7 s^-1; raw unit: s^-1; normalized value: 42.7 s^(-1); metric: Km; raw value: 0.01 mM; raw unit: mM; normalized value: 0.01 mM; metric: kcat/Km; normalized value: 4270.0 s^(-1)*mM^(-1); assay condition: GST activity assay at 25 C in 0.1 M potassium phosphate buffer, pH 6.5; steady-state kinetics with the CDNB concentration varied at a saturating GSH concentration and vice versa; Michaelis-Menten fit in GraphPad Prism 5; wild-type DmGST enzyme. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 42.7 s^-1 is already in s^-1, no conversion. Km 0.01 mM is already in mM, no conversion. kcat/Km is recorded as the quotient of this row's own two printed cells: paper kcat / paper Km = 42.7 / 0.01 = 4270.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 Kinetic parameters of DmGSTs and purification schemes; row DmGSTE9-9; CDNB substrate block; metric: kcat; raw value: 42.7; raw unit: s^-1; metric: Km; raw value: 0.01; raw unit: mM; metric: kcat/Km; raw value: null (not taken from a printed cell); normalized value: 4270.0 s^-1 mM^-1; assay condition: GST activity assay at 25 C in 0.1 M potassium phosphate buffer, pH 6.5; steady-state kinetics with the CDNB concentration varied at a saturating GSH concentration and vice versa; Michaelis-Menten fit in GraphPad Prism 5; wild-type DmGST enzyme.


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant I52A


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant S65A


column_label: Table 1 wild-type row, columns kcat, Km CDNB, and kcat/Km CDNB.

normalized_value_unit_evidence: kcat=35.4 s^-1; Km CDNB=0.14 mM; explicit paper kcat/Km CDNB=245.95 s^-1 mM^-1.

raw_value_unit_evidence: Wild-type row reports kcat 35.4 s^-1; Km CDNB 0.14 +/- 0.01 mM; kcat/Km CDNB 245.95 s^-1/mM.


mutation_type: truncation

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant DmGSTD7 Stop172W


column_label: PMID 22082028 Table 2; row DmGSTD11b-11b; columns Vmax, kcat, CDNB Km, CDNB kcat/Km

raw_value_unit_evidence: Vmax 239 umol min^-1 mg^-1; kcat 111 s^-1; CDNB Km 2.52 mM; CDNB kcat/Km 44.1 s^-1 mM^-1

row_label: DmGSTD11b-11b / CDNB


column_label: PMID 22082028 Table 2; row DmGSTD9-9; columns Vmax, kcat, CDNB Km, CDNB kcat/Km

raw_value_unit_evidence: Vmax 8.54 umol min^-1 mg^-1; kcat 3.63 s^-1; CDNB Km 0.36 mM; CDNB kcat/Km 10 s^-1 mM^-1

row_label: DmGSTD9-9 / CDNB


column_label: PMID 22082028 Table 2; row DmGSTD9-9; columns Vmax, kcat, GSH Km; ResearchGate public full-text lines 665-671.

raw_value_unit_evidence: Vmax 8.54 umol min^-1 mg^-1; kcat 3.63 s^-1; GSH Km 0.3 mM

row_label: DmGSTD9-9 / GSH


column_label: PMID 22082028 Table 2; row DmGSTD2-2; columns Vmax, kcat, GSH Km, GSH kcat/Km

raw_value_unit_evidence: Vmax 0.53 umol min^-1 mg^-1; kcat 0.22 s^-1; GSH Km 1.84 mM; GSH kcat/Km 0.12 s^-1 mM^-1

row_label: DmGSTD2-2 / GSH


column_label: PMID 22082028 Table 2; row DmGSTT3b-3b; columns Vmax, kcat, CDNB Km, CDNB kcat/Km

raw_value_unit_evidence: Vmax 0.77 umol min^-1 mg^-1; kcat 0.41 s^-1; CDNB Km 0.74 mM; CDNB kcat/Km 0.55 s^-1 mM^-1

row_label: DmGSTT3b-3b / CDNB


column_label: PMID 22082028 Table 2; row DmGSTD10-10; columns Vmax, kcat, CDNB Km; ResearchGate public full-text lines 673-678.

raw_value_unit_evidence: Vmax 15.9 umol min^-1 mg^-1; kcat 6.5 s^-1; CDNB Km 2.78 mM

row_label: DmGSTD10-10 / CDNB


column_label: PMID 22082028 Table 2; row DmGSTE10-10; columns Vmax, kcat, CDNB Km, CDNB kcat/Km

raw_value_unit_evidence: Vmax 13.4 umol min^-1 mg^-1; kcat 6.06 s^-1; CDNB Km 2.44 mM; CDNB kcat/Km 2.48 s^-1 mM^-1

row_label: DmGSTE10-10 / CDNB


sequence_source: UniProtKB REST JSON A1ZB68

column_label: Table 2 (Kinetic parameters of DmGSTs and purification schemes), enzyme row 'DmGSTE3-3', GSH column group; column 'k cat (s-1)' = 26.6; column 'K m (mM)' under the GSH head = 0.46; column 'k cat /K m (s-1 mM-1)' under the GSH head = 57; the CDNB column group of the same enzyme row prints K m 1.51 mM and k cat /K m 17.6 s-1 mM-1; column 'V max (umol min-1 mg-1)' = 63.9.

normalized_value_unit_evidence: kcat: printed Table 2 cell 26.6 s^-1; the printed turnover column is already per second, so no unit conversion applies and the exported value is 26.6 s^(-1). Km: printed Table 2 cell 0.46 mM; the printed constant is already in mM, so no unit conversion applies and the exported value is 0.46 mM. kcat/Km: printed Table 2 cell 57 s^-1 mM^-1; the printed efficiency column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell carries as 57.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row DmGSTE3-3, GSH column group: kcat = 26.6 s^-1; Km = 0.46 mM; printed kcat/Km = 57 s^-1 mM^-1.


sequence_source: UniProtKB REST JSON P41043

column_label: Table 2 Kinetic parameters of DmGSTs and purification schemes; row DmGSTS1-1; purification column GSTrap; column kcat (s^-1) raw value 1.81; column Km (mM) of the CDNB substrate block raw value 1.24; column kcat/Km (s^-1 mM^-1) of the CDNB substrate block printed cell 1.46. The PDF text layer splits every plus/minus S.D. across two lines, so the row reads as the plus sign, then the Unicode minus and the S.D., then the next cell.

normalized_value_unit_evidence: metric: kcat; raw value: 1.81 s^-1; raw unit: s^-1; normalized value: 1.81 s^(-1); metric: Km; raw value: 1.24 mM; raw unit: mM; normalized value: 1.24 mM; metric: kcat/Km; normalized value: 1.4596774193548387 s^(-1)*mM^(-1); assay condition: GST activity assay at 25 C in 0.1 M potassium phosphate buffer, pH 6.5; steady-state kinetics with the CDNB concentration varied at a saturating GSH concentration and vice versa; Michaelis-Menten fit in GraphPad Prism 5; wild-type DmGST enzyme. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 1.81 s^-1 is already in s^-1, no conversion. Km 1.24 mM is already in mM, no conversion. kcat/Km is recorded as the quotient of this row's own two printed cells: paper kcat / paper Km = 1.81 / 1.24 = 1.4596774193548387 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 Kinetic parameters of DmGSTs and purification schemes; row DmGSTS1-1; CDNB substrate block; metric: kcat; raw value: 1.81; raw unit: s^-1; metric: Km; raw value: 1.24; raw unit: mM; metric: kcat/Km; raw value: null (not taken from a printed cell); normalized value: 1.4596774193548387 s^-1 mM^-1; assay condition: GST activity assay at 25 C in 0.1 M potassium phosphate buffer, pH 6.5; steady-state kinetics with the CDNB concentration varied at a saturating GSH concentration and vice versa; Michaelis-Menten fit in GraphPad Prism 5; wild-type DmGST enzyme.


sequence_source: UniProtKB REST JSON Q4V6J1


sequence_source: UniProtKB REST JSON Q7K8X7


sequence_source: UniProtKB REST JSON Q9XYZ9

column_label: Table 2 (Kinetic parameters of DmGSTs and purification schemes), enzyme row 'DmGSTE12-12', CDNB column group; column 'k cat (s-1)' = 18.4; column 'K m (mM)' under the CDNB head = 0.05; column 'k cat /K m (s-1 mM-1)' under the CDNB head = 390; the GSH column group of the same enzyme row prints K m 2.44 mM and k cat /K m 7.52 s-1 mM-1; column 'V max (umol min-1 mg-1)' = 43.8.

normalized_value_unit_evidence: kcat: printed Table 2 cell 18.4 s^-1; the printed turnover column is already per second, so no unit conversion applies and the exported value is 18.4 s^(-1). Km: printed Table 2 cell 0.05 mM; the printed constant is already in mM, so no unit conversion applies and the exported value is 0.05 mM. kcat/Km: printed Table 2 cell 390 s^-1 mM^-1; the printed efficiency column is already in s^-1 mM^-1, so no unit conversion applies and the printed cell carries as 390.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row DmGSTE12-12, CDNB column group: kcat = 18.4 s^-1; Km = 0.05 mM; printed kcat/Km = 390 s^-1 mM^-1.


sequence_source: UniProtKB REST JSON Q9VSL2

column_label: Table 2 Kinetic parameters of DmGSTs and purification schemes; row DmGSTO3-3; purification column An; column kcat (s^-1) raw value 0.05; column Km (mM) of the GSH substrate block raw value 0.11; column kcat/Km (s^-1 mM^-1) of the GSH substrate block printed cell 0.45. The PDF text layer splits every plus/minus S.D. across two lines, so the row reads as the plus sign, then the Unicode minus and the S.D., then the next cell.

normalized_value_unit_evidence: metric: kcat; raw value: 0.05 s^-1; raw unit: s^-1; normalized value: 0.05 s^(-1); metric: Km; raw value: 0.11 mM; raw unit: mM; normalized value: 0.11 mM; metric: kcat/Km; normalized value: 0.4545454545454546 s^(-1)*mM^(-1); assay condition: GST activity assay at 25 C in 0.1 M potassium phosphate buffer, pH 6.5; steady-state kinetics with the CDNB concentration varied at a saturating GSH concentration and vice versa; Michaelis-Menten fit in GraphPad Prism 5; wild-type DmGST enzyme. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 0.05 s^-1 is already in s^-1, no conversion. Km 0.11 mM is already in mM, no conversion. kcat/Km is recorded as the quotient of this row's own two printed cells: paper kcat / paper Km = 0.05 / 0.11 = 0.4545454545454546 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 Kinetic parameters of DmGSTs and purification schemes; row DmGSTO3-3; GSH substrate block; metric: kcat; raw value: 0.05; raw unit: s^-1; metric: Km; raw value: 0.11; raw unit: mM; metric: kcat/Km; raw value: null (not taken from a printed cell); normalized value: 0.4545454545454546 s^-1 mM^-1; assay condition: GST activity assay at 25 C in 0.1 M potassium phosphate buffer, pH 6.5; steady-state kinetics with the CDNB concentration varied at a saturating GSH concentration and vice versa; Michaelis-Menten fit in GraphPad Prism 5; wild-type DmGST enzyme.


column_label: PMID 22082028 Table 2; row DmGSTT3a-3a; columns Vmax, kcat, CDNB Km, CDNB kcat/Km

raw_value_unit_evidence: Vmax 0.93 umol min^-1 mg^-1; kcat 0.39 s^-1; CDNB Km 1.61 mM; CDNB kcat/Km 0.24 s^-1 mM^-1

row_label: DmGSTT3a-3a / CDNB


column_label: PMID 22082028 Table 2; row DmGSTE9-9; columns Vmax, kcat, GSH Km, GSH kcat/Km

raw_value_unit_evidence: Vmax 103 umol min^-1 mg^-1; kcat 42.7 s^-1; GSH Km 7.13 mM; GSH kcat/Km 6 s^-1 mM^-1

row_label: DmGSTE9-9 / GSH


column_label: PMID 22082028 Table 2; row DmGSTE7-7; columns Vmax, kcat, CDNB Km, CDNB kcat/Km

raw_value_unit_evidence: Vmax 81.8 umol min^-1 mg^-1; kcat 34.7 s^-1; CDNB Km 0.2 mM; CDNB kcat/Km 170 s^-1 mM^-1

row_label: DmGSTE7-7 / CDNB


column_label: PMID 22082028 Table 2; row DmGSTD11b-11b; columns Vmax, kcat, GSH Km, GSH kcat/Km

raw_value_unit_evidence: Vmax 239 umol min^-1 mg^-1; kcat 111 s^-1; GSH Km 0.99 mM; GSH kcat/Km 110 s^-1 mM^-1

row_label: DmGSTD11b-11b / GSH


column_label: PMID 22082028 Table 2; row DmGSTT3a-3a; columns Vmax, kcat, GSH Km; ResearchGate public full-text lines 853-859.

raw_value_unit_evidence: Vmax 0.93 umol min^-1 mg^-1; kcat 0.39 s^-1; GSH Km 1.31 mM

row_label: DmGSTT3a-3a / GSH


column_label: PMID 22082028 Table 2; row DmGSTE10-10; columns Vmax, kcat, GSH Km, GSH kcat/Km

raw_value_unit_evidence: Vmax 13.4 umol min^-1 mg^-1; kcat 6.06 s^-1; GSH Km 2.25 mM; GSH kcat/Km 2.69 s^-1 mM^-1

row_label: DmGSTE10-10 / GSH


column_label: PMID 22082028 Table 2; row DmGSTT3a-3a; columns Vmax, kcat, GSH Km, GSH kcat/Km

raw_value_unit_evidence: Vmax 0.93 umol min^-1 mg^-1; kcat 0.39 s^-1; GSH Km 1.31 mM; GSH kcat/Km 0.3 s^-1 mM^-1


sequence_variant_note: Mutation signature K25N/S117C/T145A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant DmGSTE1 (K25N/S117C/T145A)


organism: Homo sapiens

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant (Y119A/N212F/N213G) hGSTM3


column_label: PMID 22082028 Table 2; row DmGSTD10-10; columns Vmax, kcat, CDNB Km, CDNB kcat/Km

raw_value_unit_evidence: Vmax 15.9 umol min^-1 mg^-1; kcat 6.5 s^-1; CDNB Km 2.78 mM; CDNB kcat/Km 2.34 s^-1 mM^-1


column_label: PMID 22082028 Table 2; row DmGSTD5-5; columns Vmax, kcat, GSH Km; ResearchGate public full-text lines 633-639.

raw_value_unit_evidence: Vmax 9.9 umol min^-1 mg^-1; kcat 4.08 s^-1; GSH Km 1.43 mM

row_label: DmGSTD5-5 / GSH


column_label: PMID 22082028 Table 2; row DmGSTO2a-2a; columns Vmax, kcat, CDNB Km, CDNB kcat/Km

raw_value_unit_evidence: Vmax 0.05 umol min^-1 mg^-1; kcat 0.02 s^-1; CDNB Km 2.41 mM; CDNB kcat/Km 0.01 s^-1 mM^-1

row_label: DmGSTO2a-2a / CDNB


column_label: PMID 22082028 Table 2; row DmGSTE6-6; columns Vmax, kcat, CDNB Km, CDNB kcat/Km

raw_value_unit_evidence: Vmax 208 umol min^-1 mg^-1; kcat 86.8 s^-1; CDNB Km 0.13 mM; CDNB kcat/Km 660 s^-1 mM^-1

row_label: DmGSTE6-6 / CDNB


column_label: PMID 22082028 Table 2; row DmGSTE14-14; columns Vmax, kcat, CDNB Km, CDNB kcat/Km

raw_value_unit_evidence: Vmax 133 umol min^-1 mg^-1; kcat 59.2 s^-1; CDNB Km 0.28 mM; CDNB kcat/Km 210 s^-1 mM^-1

row_label: DmGSTE14-14 / CDNB


substrate_name: glutathione

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.

substrate: glutathione


substrate_name: dehydroascorbate

substrate: dehydroascorbate


organism: Gallus gallus

sequence_variant_note: Mutation signature F111A/S208M matches the mutant residue at offset +0 and the reference residue at offset -6; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


substrate_name: Ethacrynic acid

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

substrate: Ethacrynic acid


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant F111A/K15L


organism: Gelatoporia subvermispora

substrate_name: cumene hydroperoxide

substrate: cumene hydroperoxide


organism: Escherichia coli

substrate_name: Bromoacetate; Reduced glutathione

substrate: Bromoacetate; Reduced glutathione


substrate_name: Bromoacetate

smiles: O=C([O-])CBr

substrate: Bromoacetate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F111A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant (N212G) hGSTM3


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant (Y119F) hGSTM3


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant F111A/S208M


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant E104G / L208S


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant F111A


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant R15K / E104G


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant (delPVC) hGSTM3


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant (N212F) hGSTM3


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant GSTM4-4 S107R


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant GSTM1a-1a H107R


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) wildtype variant Val 105/ Phe 151

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) wildtype variant Val 105/ Leu 151

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) wildtype variant Ile 105/ Leu 151


substrate_name: Dichloromethane; Reduced glutathione

substrate: Dichloromethane; Reduced glutathione


organism: Glycine max

substrate_name: RX; Reduced glutathione

substrate: RX; Reduced glutathione


sequence_variant_note: Mutation signature S13A matches the mutant residue at offset +0 and the reference residue at offset -11; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant chimeric: aa 1-196 from P46439, aa 201-224 from P21266


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant (N212G/N213G) hGSTM3


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant (N212F/N213G) hGSTM3


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant (Y119F/N212F) hGSTM3


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant chimeric: 1-197 from P21266, 194-217 from P46439


column_label: Table 2 row M3-3 columns KmGSH (mM), kcat (s^-1), and kcat/KmGSH (s^-1 mM^-1).

table_label: Table 2. Limiting Values of Kinetic Parameters of Recombinant Wild-Type, Chimeric, and Mutant Mu Class GSTs with the CDNB Substrate


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant (N213G) hGSTM3


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant (Y119A/N212F) hGSTM3


column_label: Table 2 row M3-3 columns KmCDNB (mM), kcat (s^-1), and kcat/KmCDNB (s^-1 mM^-1).

raw_value_unit_evidence: M3-3 row: KmCDNB 1.10 mM; kcat 5.43 s^-1; kcat/KmCDNB 4.9 s^-1 mM^-1.


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant (Y119A) hGSTM3


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant (Y119F/N212F/N213G) hGSTM3


column_label: Table 2 row M5-5 columns KmCDNB (mM) and kcat (s^-1).

normalized_value_unit_evidence: KmCDNB 0.10 mM; kcat 59.7 s^-1.

raw_value_unit_evidence: M5-5 row: KmCDNB 0.10 mM; kcat 59.7 s^-1.


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant GSTM2-2 Y6F


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant GSTM2-2 Y6F/R107H


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant GSTM2-2 R107H


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant GSTM2-2 R107N


substrate_name: (+)-anti-BPDE; Reduced glutathione

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant hGSTA2/S215A

substrate: (+)-anti-BPDE; Reduced glutathione


substrate_name: Reduced glutathione; (+)-anti-BPDE

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant hGSTA2/S9F

substrate: Reduced glutathione; (+)-anti-BPDE


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant hGSTA2/F110V


substrate_name: (+)-anti-BPDE

substrate: (+)-anti-BPDE


substrate_name: S-Glutathionyl benzoate

substrate: S-Glutathionyl benzoate


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant hGSTA2/I11A


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant hGSTA2/SIFS


organism: Nilaparvata lugens


substrate_name: S-Glutathionyl benzoate; H2O

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant A216H

substrate: S-Glutathionyl benzoate; H2O


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant GSTA3(G12A)


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant GSTA3(A208M)


substrate_name: Hyp-Cys-Gly

column_label: [{'metric': 'km', 'table_label': 'Table IV', 'row_label': 'IV', 'column_label': 'hGSTP1-1A', 'raw_value': '3.22 +/- 0.46', 'raw_unit': 'mM', 'normalized_value': 3.22, 'normalized_unit': 'mM'}, {'metric': 'kcat', 'table_label': 'Table IV', 'row_label': 'IV', 'column_label': 'hGSTP1-1A', 'raw_value': '62.50 +/- 4.55', 'raw_unit': 'min^-1', 'normalized_value': 1.0416666666666667, 'normalized_unit': 's^-1'}, {'metric': 'kcat_over_km', 'table_label': 'Table IV', 'row_label': 'IV', 'column_label': 'hGSTP1-1A', 'raw_value': '19.41 +/- 4.88', 'raw_unit': 'min^-1 mM^-1', 'normalized_value': 0.3235, 'normalized_unit': 's^-1 mM^-1'}]

row_label: Analogue IV; hGSTP1-1A

table_label: Table IV

substrate: Hyp-Cys-Gly


substrate_name: gamma-Glu-Cys-Sar

column_label: [{'metric': 'km', 'table_label': 'Table IV', 'row_label': 'XV', 'column_label': 'hGSTP1-1A', 'raw_value': '3.18 +/- 0.28', 'raw_unit': 'mM', 'normalized_value': 3.18, 'normalized_unit': 'mM'}, {'metric': 'kcat', 'table_label': 'Table IV', 'row_label': 'XV', 'column_label': 'hGSTP1-1A', 'raw_value': '23.30 +/- 0.97', 'raw_unit': 'min^-1', 'normalized_value': 0.38833333333333336, 'normalized_unit': 's^-1'}, {'metric': 'kcat_over_km', 'table_label': 'Table IV', 'row_label': 'XV', 'column_label': 'hGSTP1-1A', 'raw_value': '7.33 +/- 1.04', 'raw_unit': 'min^-1 mM^-1', 'normalized_value': 0.12216666666666667, 'normalized_unit': 's^-1 mM^-1'}]

row_label: Analogue XV; hGSTP1-1A

substrate: gamma-Glu-Cys-Sar


substrate_name: acetyl-gamma-Glu-Cys-Gly

sequence_variant_note: Resolved canonical sequence from uniprotkb:P09211;rcsb:11GS,1PGT,3CSI and applied mutation signature I104V/A113V with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: [{'metric': 'km', 'table_label': 'Table IV', 'row_label': 'V', 'column_label': 'hGSTP1-1C', 'raw_value': '2.24 +/- 0.17', 'raw_unit': 'mM', 'normalized_value': 2.24, 'normalized_unit': 'mM'}, {'metric': 'kcat', 'table_label': 'Table IV', 'row_label': 'V', 'column_label': 'hGSTP1-1C', 'raw_value': '61.67 +/- 1.66', 'raw_unit': 'min^-1', 'normalized_value': 1.0278333333333334, 'normalized_unit': 's^-1'}, {'metric': 'kcat_over_km', 'table_label': 'Table IV', 'row_label': 'V', 'column_label': 'hGSTP1-1C', 'raw_value': '27.53 +/- 3.06', 'raw_unit': 'min^-1 mM^-1', 'normalized_value': 0.4588333333333333, 'normalized_unit': 's^-1 mM^-1'}]

row_label: Analogue V; hGSTP1-1C

substrate: acetyl-gamma-Glu-Cys-Gly


substrate_name: Tic-Cys-Gly

column_label: [{'metric': 'km', 'table_label': 'Table IV', 'row_label': 'II', 'column_label': 'hGSTP1-1A', 'raw_value': '1.25 +/- 0.07', 'raw_unit': 'mM', 'normalized_value': 1.25, 'normalized_unit': 'mM'}, {'metric': 'kcat', 'table_label': 'Table IV', 'row_label': 'II', 'column_label': 'hGSTP1-1A', 'raw_value': '18.56 +/- 1.03', 'raw_unit': 'min^-1', 'normalized_value': 0.30933333333333335, 'normalized_unit': 's^-1'}, {'metric': 'kcat_over_km', 'table_label': 'Table IV', 'row_label': 'II', 'column_label': 'hGSTP1-1A', 'raw_value': '14.85 +/- 1.75', 'raw_unit': 'min^-1 mM^-1', 'normalized_value': 0.2475, 'normalized_unit': 's^-1 mM^-1'}]

row_label: Analogue II; hGSTP1-1A

substrate: Tic-Cys-Gly


substrate_name: glutathione

sequence_variant_note: Resolved canonical sequence from uniprotkb:P09211;rcsb:11GS,1PGT,3CSI and applied mutation signature I104V with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: [{'metric': 'km', 'table_label': 'Table IV', 'row_label': 'GSH', 'column_label': 'hGSTP1-1B', 'raw_value': '0.074 +/- 0.008', 'raw_unit': 'mM', 'normalized_value': 0.074, 'normalized_unit': 'mM'}, {'metric': 'kcat', 'table_label': 'Table IV', 'row_label': 'GSH', 'column_label': 'hGSTP1-1B', 'raw_value': '150.9 +/- 5.7', 'raw_unit': 'min^-1', 'normalized_value': 2.515, 'normalized_unit': 's^-1'}, {'metric': 'kcat_over_km', 'table_label': 'Table IV', 'row_label': 'GSH', 'column_label': 'hGSTP1-1B', 'raw_value': '2040 +/- 333', 'raw_unit': 'min^-1 mM^-1', 'normalized_value': 34.0, 'normalized_unit': 's^-1 mM^-1'}]

row_label: Analogue GSH; hGSTP1-1B

substrate: glutathione


column_label: [{'metric': 'km', 'table_label': 'Table IV', 'row_label': 'GSH', 'column_label': 'hGSTP1-1C', 'raw_value': '0.15 +/- 0.01', 'raw_unit': 'mM', 'normalized_value': 0.15, 'normalized_unit': 'mM'}, {'metric': 'kcat', 'table_label': 'Table IV', 'row_label': 'GSH', 'column_label': 'hGSTP1-1C', 'raw_value': '137.4 +/- 3.8', 'raw_unit': 'min^-1', 'normalized_value': 2.29, 'normalized_unit': 's^-1'}, {'metric': 'kcat_over_km', 'table_label': 'Table IV', 'row_label': 'GSH', 'column_label': 'hGSTP1-1C', 'raw_value': '916 +/- 93', 'raw_unit': 'min^-1 mM^-1', 'normalized_value': 15.266666666666667, 'normalized_unit': 's^-1 mM^-1'}]

row_label: Analogue GSH; hGSTP1-1C


column_label: [{'metric': 'km', 'table_label': 'Table IV', 'row_label': 'XV', 'column_label': 'hGSTP1-1B', 'raw_value': '0.033 +/- 0.003', 'raw_unit': 'mM', 'normalized_value': 0.033, 'normalized_unit': 'mM'}, {'metric': 'kcat', 'table_label': 'Table IV', 'row_label': 'XV', 'column_label': 'hGSTP1-1B', 'raw_value': '31.82 +/- 0.00', 'raw_unit': 'min^-1', 'normalized_value': 0.5303333333333333, 'normalized_unit': 's^-1'}, {'metric': 'kcat_over_km', 'table_label': 'Table IV', 'row_label': 'XV', 'column_label': 'hGSTP1-1B', 'raw_value': '964 +/- 96', 'raw_unit': 'min^-1 mM^-1', 'normalized_value': 16.066666666666666, 'normalized_unit': 's^-1 mM^-1'}]

row_label: Analogue XV; hGSTP1-1B


substrate_name: (beta-(13-Hydroperoxy-cis-9, trans-11-octadecadienoyl)-gamma-palmitoyl)-L-alpha-phosphatidylcholine; Reduced glutathione

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R15K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant isoenzyme GST A1-1 R15K


organism: Novosphingobium aromaticivorans


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant isoenzyme GST A1-1 M208A

substrate: (beta-(13-Hydroperoxy-cis-9, trans-11-octadecadienoyl)-gamma-palmitoyl)-L-alpha-phosphatidylcholine; Reduced glutathione


substrate_name: reduced glutathione

substrate: reduced glutathione


organism: Lucilia cuprina

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S9A to reconstruct the assayed variant sequence.

column_label: Table 1 columns VGSH, KGSH, KCDNB; row S9A; expected Km matches KCDNB.

raw_value_unit_evidence: Table 1 row S9A reports VGSH = 0.07 +/- 0.021 umol/min per mg and KCDNB = 1.22 +/- 1.033 mM.

table_label: Table 1: Kinetic parameters for normal and mutant recombinant L. cuprina GST


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S9T to reconstruct the assayed variant sequence.

column_label: Table 1 columns VGSH, KGSH, KCDNB; row S9T; expected Km matches KGSH.

raw_value_unit_evidence: Table 1 row S9T reports VGSH = 0.48 +/- 0.155 umol/min per mg and KGSH = 1.16 +/- 0.635 mM.


column_label: Table 1 columns VGSH, KGSH, KCDNB; row Normal; expected Km matches KGSH.

raw_value_unit_evidence: Table 1 row Normal reports VGSH = 20.1 +/- 1.72 umol/min per mg and KGSH = 0.51 +/- 0.093 mM.

row_label: Normal enzyme


organism: Mus musculus


organism: Plasmodium falciparum

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant Y9F


organism: Rattus norvegicus

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant C156L


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant L199F


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant K198E


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant K112E


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant Y152F


proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=25°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=6.5


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant Y8F


substrate_name: iodomethane

smiles: CI

substrate: iodomethane


substrate_name: iodohexane

smiles: CCCCCCI

substrate: iodohexane


substrate_name: iodobutane

substrate: iodobutane


column_label: [{'metric': 'km', 'table_label': 'Table IV', 'row_label': 'GSH', 'column_label': 'hGSTP1-1A', 'raw_value': '0.30 +/- 0.02', 'raw_unit': 'mM', 'normalized_value': 0.3, 'normalized_unit': 'mM'}, {'metric': 'kcat', 'table_label': 'Table IV', 'row_label': 'GSH', 'column_label': 'hGSTP1-1A', 'raw_value': '101.9 +/- 2.8', 'raw_unit': 'min^-1', 'normalized_value': 1.6983333333333333, 'normalized_unit': 's^-1'}, {'metric': 'kcat_over_km', 'table_label': 'Table IV', 'row_label': 'GSH', 'column_label': 'hGSTP1-1A', 'raw_value': '340 +/- 34', 'raw_unit': 'min^-1 mM^-1', 'normalized_value': 5.666666666666667, 'normalized_unit': 's^-1 mM^-1'}]

row_label: Analogue GSH; hGSTP1-1A


organism: Ochrobactrum anthropi

column_label: Table II; row OaGST; columns GSH Km (mM), GSH kcat (s^-1), GSH kcat/Km (mM^-1 s^-1).

raw_value_unit_evidence: Table II Table II row OaGST; GSH column group reports GSH Km 0.132 +/- 0.02 mM; GSH kcat 2.35 +/- 0.15 s^-1; GSH kcat/Km 17.80 mM^-1 s^-1.

row_label: Table II row OaGST; GSH column group

table_label: Table II


organism: Oryza sativa


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C86A to reconstruct the assayed variant sequence.

column_label: PMC Table 1, row C86A, columns kcat^GSH (min^-1); Km^GSH (uM); cells kcat = 5.6 +/- 0.2 min^-1; Km = 123 +/- 3 uM. Footnote: mean of two independent determinations; CDNB conjugation assay.

table_label: PMC Table 1: Kinetic parameters of wild-type PfGST and G-site mutants


column_label: PMC Table 1, row C86A, columns kcat^GSH (min^-1); Km^GSH (uM); kcat^GSH/Km^GSH (M^-1 sec^-1); cells kcat = 5.6 +/- 0.2 min^-1; Km = 123 +/- 3 uM; kcat/Km = 756 +/- 48 M^-1 sec^-1. Footnote: mean of two independent determinations; CDNB conjugation assay.


column_label: Table 1. Kinetic parameters of wild-type PfGST and G-site mutants of PfGST determined using the CDNB conjugation assay (columns 2-4) and the peroxidase assay (column 5); row Wild-type; columns kcat^GSH (min^-1); Km^GSH (uM); kcat^GSH/Km^GSH (M^-1 sec^-1); cells 6.3 +/- 0.01 min^-1; 108 +/- 4 uM; 978 +/- 34 M^-1 sec^-1

normalized_value_unit_evidence: kcat normalized_value=0.105 normalized_unit=s^-1; Km normalized_value=0.108 normalized_unit=mM; kcat/Km central_normalized_value=0.9722222222222222 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=0.978 s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=6.3 +/- 0.01 min^-1; Km raw_value=108 +/- 4 uM; kcat/Km raw_value=978 +/- 34 M^-1 sec^-1

row_label: Wild-type


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y211F to reconstruct the assayed variant sequence.

column_label: PMC Table 1, row Y211F, columns kcat^GSH (min^-1); Km^GSH (uM); kcat^GSH/Km^GSH (M^-1 sec^-1); cells kcat = 7.6 +/- 0.4 min^-1; Km = 128 +/- 2 uM; kcat/Km = 985 +/- 42 M^-1 sec^-1. Footnote: mean of two independent determinations; CDNB conjugation assay.


organism: Serratia marcescens

substrate_name: Phosphonomycin

substrate: Phosphonomycin


substrate_name: Phosphonomycin; Reduced glutathione

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant E113A

substrate: Phosphonomycin; Reduced glutathione


substrate_name: Reduced glutathione; Phosphonomycin

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant E113Q

substrate: Reduced glutathione; Phosphonomycin


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant H67Q


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant H67A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C10A to reconstruct the assayed variant sequence.


column_label: Retained PDF Table II, OaGST row, CDNB Km, kcat, and kcat/Km columns.

normalized_value_unit_evidence: KM 3.095 mM; kcat 16.51 s^-1; independently printed kcat/KM 5.33 s^-1 mM^-1.

raw_value_unit_evidence: Table II OaGST row, CDNB block: KM 3.095 +/- 0.22 mM; kcat 16.51 +/- 0.83 s^-1; independently printed kcat/KM 5.33 mM^-1 s^-1.

row_label: OaGST / CDNB block

table_label: Table II. Specific Activity and Kinetic Constants for OaGST and C10A and C10A/S11A Mutants with CDNB as Second Substrate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C10A/S11A to reconstruct the assayed variant sequence.

column_label: Table II; row C10A/S11A; columns CDNB Km (mM), CDNB kcat (s^-1), CDNB kcat/Km (mM^-1 s^-1).

raw_value_unit_evidence: Table II Table II row C10A/S11A; CDNB column group reports CDNB Km 0.46 +/- 0.031 mM; CDNB kcat 0.45 +/- 0.03 s^-1; CDNB kcat/Km 0.98 mM^-1 s^-1.


column_label: Table II; row C10A; columns CDNB Km (mM), CDNB kcat (s^-1), CDNB kcat/Km (mM^-1 s^-1).

raw_value_unit_evidence: Table II Table II row C10A; CDNB column group reports CDNB Km 3.933 +/- 0.64 mM; CDNB kcat 11.79 +/- 0.55 s^-1; CDNB kcat/Km 2.99 mM^-1 s^-1.

row_label: Table II row C10A; CDNB column group


column_label: Table II; row C10A; columns CDNB Km (mM), CDNB kcat (s^-1).

raw_value_unit_evidence: Table II Table II row C10A; CDNB column group reports CDNB Km 3.933 +/- 0.64 mM; CDNB kcat 11.79 +/- 0.55 s^-1.


column_label: Table II; row C10A/S11A; columns GSH Km (mM), GSH kcat (s^-1), GSH kcat/Km (mM^-1 s^-1).

raw_value_unit_evidence: Table II Table II row C10A/S11A; GSH column group reports GSH Km 13.93 +/- 0.94 mM; GSH kcat 0.85 +/- 0.09 s^-1; GSH kcat/Km 0.06 mM^-1 s^-1.


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant C10A/S11A


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant C156Y


substrate_name: Dichloromethane; Reduced glutathione

substrate: Dichloromethane; Reduced glutathione


organism: Saccharomyces cerevisiae


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q71E to reconstruct the assayed variant sequence.

column_label: PMC Table 1, row Q71E, columns kcat^GSH (min^-1); Km^GSH (uM); cells kcat = 3.4 +/- 0.04 min^-1; Km = 281 +/- 27 uM. Footnote: mean of two independent determinations; CDNB conjugation assay.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C101A to reconstruct the assayed variant sequence.

column_label: PMC Table 1, row C101A, columns kcat^GSH (min^-1); Km^GSH (uM); kcat^GSH/Km^GSH (M^-1 sec^-1); cells kcat = 4.5 +/- 0.2 min^-1; Km = 246 +/- 6 uM; kcat/Km = 305 +/- 3 M^-1 sec^-1. Footnote: mean of two independent determinations; CDNB conjugation assay.

normalized_value_unit_evidence: kcat 0.075 s^-1; Km 0.246 mM; printed kcat/Km 0.305 s^-1*mM^-1 after dividing the Table 1 M^-1 sec^-1 cell by 1000


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y9F to reconstruct the assayed variant sequence.

column_label: PMC Table 1, row Y9F, columns kcat^GSH (min^-1); Km^GSH (uM); kcat^GSH/Km^GSH (M^-1 sec^-1); cells kcat = 0.2 +/- 0.01 min^-1; Km = 101 +/- 12 uM; kcat/Km = 32.4 +/- 1.5 M^-1 sec^-1. Footnote: mean of two independent determinations; CDNB conjugation assay.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K15E to reconstruct the assayed variant sequence.

column_label: PMC Table 1, row K15E, columns kcat^GSH (min^-1); Km^GSH (uM); kcat^GSH/Km^GSH (M^-1 sec^-1); cells kcat = 0.1 +/- 0.00 min^-1; Km = 994 +/- 150 uM; kcat/Km = 2.0 +/- 0.3 M^-1 sec^-1. Footnote: mean of two independent determinations; CDNB conjugation assay.


column_label: PMC Table 1, row Y211F, columns kcat^GSH (min^-1); Km^GSH (uM); cells kcat = 7.6 +/- 0.4 min^-1; Km = 128 +/- 2 uM. Footnote: mean of two independent determinations; CDNB conjugation assay.


column_label: PMC Table 1, row K15E, columns kcat^GSH (min^-1); Km^GSH (uM); cells kcat = 0.1 +/- 0.00 min^-1; Km = 994 +/- 150 uM. Footnote: mean of two independent determinations; CDNB conjugation assay.


column_label: PMC Table 1, row Q71E, columns kcat^GSH (min^-1); Km^GSH (uM); kcat^GSH/Km^GSH (M^-1 sec^-1); cells kcat = 3.4 +/- 0.04 min^-1; Km = 281 +/- 27 uM; kcat/Km = 203 +/- 18 M^-1 sec^-1. Footnote: mean of two independent determinations; CDNB conjugation assay.


column_label: PMC Table 1, row C101A, columns kcat^GSH (min^-1); Km^GSH (uM); cells kcat = 4.5 +/- 0.2 min^-1; Km = 246 +/- 6 uM. Footnote: mean of two independent determinations; CDNB conjugation assay.