substrate_name: ertapenem

column_label: Table 1 'Table 1: Kinetic parameters of IMP-13, IMP-1, and IMP-2'; row Ertapenem; IMP-13 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 1 row Ertapenem, IMP-13 normalized: kcat 1.8 s^-1; Km 0.0008 mM; kcat/Km 2200 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row Ertapenem, IMP-13 columns: kcat 1.8 ± 0.1 s^-1; Km 0.8 ± 0.1 uM; kcat/Km 2.2 uM^-1 s^-1.

row_label: Ertapenem

substrate: ertapenem


enzyme_display_name: beta-lactamase

organism: Pseudomonas aeruginosa

substrate_name: ticarcillin

source_db: oed

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

column_label: Table 1 'Table 1: Kinetic parameters of IMP-13, IMP-1, and IMP-2'; row Ticarcillin; IMP-13 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 1 row Ticarcillin, IMP-13 normalized: kcat 220 s^-1; Km 0.13 mM; kcat/Km 1800 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row Ticarcillin, IMP-13 columns: kcat 220 ± 30 s^-1; Km 130 ± 20 uM; kcat/Km 1.8 uM^-1 s^-1.

row_label: Ticarcillin

data_origin: experimental

enzyme: beta-lactamase

substrate: ticarcillin

status: corrected

source: oed


substrate_name: cefotaxime

column_label: Table 1 'Table 1: Kinetic parameters of IMP-13, IMP-1, and IMP-2'; row Cefotaxime; IMP-13 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 1 row Cefotaxime, IMP-13 normalized: kcat 33 s^-1; Km 0.021 mM; kcat/Km 1600 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row Cefotaxime, IMP-13 columns: kcat 33 ± 2 s^-1; Km 21 ± 2 uM; kcat/Km 1.6 uM^-1 s^-1.

row_label: Cefotaxime

substrate: cefotaxime


substrate_name: cefepime

verification_status: verified

column_label: Table 1 'Table 1: Kinetic parameters of IMP-13, IMP-1, and IMP-2'; row Cefepime; IMP-13 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 1 row Cefepime, IMP-13 normalized: kcat 12 s^-1; Km 0.008 mM; kcat/Km 1500 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row Cefepime, IMP-13 columns: kcat 12 ± 1 s^-1; Km 8 ± 1 uM; kcat/Km 1.5 uM^-1 s^-1.

row_label: Cefepime

substrate: cefepime

status: verified


assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM HEPES

column_label: Table 4; row Cefepime; enzyme column VIM-13; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 61 +/- 21, Km 1,870 +/- 569, kcat/Km 3.3E4

normalized_value_unit_evidence: kcat=61 s^-1; Km=1.87 mM; kcat/Km=33 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-13 / Cefepime

table_label: Table 4. Kinetic parameters for VIM-13 enzyme with various beta-lactams in comparison with those for VIM-1


substrate_name: Penicillin G

column_label: Table 4; row Penicillin G; enzyme column VIM-13; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 757 +/- 146, Km 1,127 +/- 172, kcat/Km 6.7E5

normalized_value_unit_evidence: kcat=757 s^-1; Km=1.127 mM; kcat/Km=670 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-13 / Penicillin G

substrate: Penicillin G


substrate_name: piperacillin

column_label: Table 4; row Piperacillin; enzyme column VIM-1; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 374 +/- 107, Km 1,377 +/- 340, kcat/Km 2.7E5

normalized_value_unit_evidence: kcat=374 s^-1; Km=1.377 mM; kcat/Km=270 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-1 / Piperacillin

substrate: piperacillin


substrate_name: Cephalothin

column_label: Table 4; row Cephalothin; enzyme column VIM-1; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 449 +/- 133, Km 135 +/- 29, kcat/Km 3.3E6

normalized_value_unit_evidence: kcat=449 s^-1; Km=0.135 mM; kcat/Km=3300 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-1 / Cephalothin

substrate: Cephalothin


substrate_name: Ceftazidime

column_label: Table 4; row Ceftazidime; enzyme column VIM-13; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 10 +/- 1, Km 509 +/- 120, kcat/Km 1.9E4

normalized_value_unit_evidence: kcat=10 s^-1; Km=0.509 mM; kcat/Km=19 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-13 / Ceftazidime

substrate: Ceftazidime


substrate_name: Ampicillin

column_label: Table 4; row Ampicillin; enzyme column VIM-1; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 307 +/- 67, Km 1,737 +/- 376, kcat/Km 1.8E5

normalized_value_unit_evidence: kcat=307 s^-1; Km=1.737 mM; kcat/Km=180 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-1 / Ampicillin

substrate: Ampicillin


column_label: Table 4; row Ceftazidime; enzyme column VIM-1; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 42 +/- 9.6, Km 1,132 +/- 320, kcat/Km 3.7E4

normalized_value_unit_evidence: kcat=42 s^-1; Km=1.132 mM; kcat/Km=37 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-1 / Ceftazidime


substrate_name: H2O; Penicillin G

kcat_over_km_display: Not reported

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

substrate: H2O; Penicillin G


organism: Proteus mirabilis

kcat_over_km_origin: calculated

sequence_source: UniProt REST

column_label: Table 2, TEM-89 enzyme block; row Cephalothin; column k cat (s^-1) cell 5; column K m (uM) cell 79; column k cat / K m (uM^-1 s^-1) cell 0.06.

normalized_value_unit_evidence: kcat 5 s^-1 = 5.0 s^(-1). Km 79 uM = 79 / 1000 = 0.079 mM. kcat/Km is recorded as the quotient of this row's own two printed cells: 5 s^-1 / 0.079 mM = 63.291139240506325 s^-1 mM^-1. Table 2 prints the ratio cell only to two significant figures (0.06 uM^-1 s^-1); that printed cell is the rounding of the same quotient and does not contradict it.

raw_value_unit_evidence: Table 2 of the PMC HTML asset, row Cephalothin, TEM-89 enzyme block: kcat column cell 5 s^-1; Km column cell 79 uM; kcat/Km column cell 0.06 uM^-1 s^-1.

row_label: Cephalothin

table_label: TABLE 2. Kinetics parameters of TEM-89 beta-lactamase compared with those of TEM-2, TEM-3, and TEM-59 beta-lactamases


substrate_name: amoxicillin

column_label: Table 2, TEM-89 enzyme block; row Amoxicillin; column k cat (s^-1) cell 50; column K m (uM) cell 28; column k cat / K m (uM^-1 s^-1) cell 1.79.

normalized_value_unit_evidence: kcat 50 s^-1 = 50.0 s^(-1). Km 28 uM = 28 / 1000 = 0.028 mM. kcat/Km is recorded as the quotient of this row's own two printed cells: 50 s^-1 / 0.028 mM = 1785.7142857142858 s^-1 mM^-1. Table 2 prints the ratio cell only to two significant figures (1.79 uM^-1 s^-1); that printed cell is the rounding of the same quotient and does not contradict it.

raw_value_unit_evidence: Table 2 of the PMC HTML asset, row Amoxicillin, TEM-89 enzyme block: kcat column cell 50 s^-1; Km column cell 28 uM; kcat/Km column cell 1.79 uM^-1 s^-1.

row_label: Amoxicillin

substrate: amoxicillin


substrate_name: Cephaloridine

column_label: Table 2, TEM-89 enzyme block; row Cephaloridine; column k cat (s^-1) cell 5; column K m (uM) cell 160; column k cat / K m (uM^-1 s^-1) cell 0.03.

normalized_value_unit_evidence: kcat 5 s^-1 = 5.0 s^(-1). Km 160 uM = 160 / 1000 = 0.16 mM. kcat/Km is recorded as the quotient of this row's own two printed cells: 5 s^-1 / 0.16 mM = 31.25 s^-1 mM^-1. Table 2 prints the ratio cell only to two significant figures (0.03 uM^-1 s^-1); that printed cell is the rounding of the same quotient and does not contradict it.

raw_value_unit_evidence: Table 2 of the PMC HTML asset, row Cephaloridine, TEM-89 enzyme block: kcat column cell 5 s^-1; Km column cell 160 uM; kcat/Km column cell 0.03 uM^-1 s^-1.

row_label: Cephaloridine

substrate: Cephaloridine


column_label: PMC Table 2, Cefepime: Km 23 uM = 0.023 mM; kcat 4.4 s^-1; printed kcat/Km 1.9 × 10^5 M^-1 s^-1 = 190 s^-1 mM^-1. Current 191.30434782608697 is the exact quotient of the same row's printed kcat and Km cells; the separately printed efficiency is retained without forcing literal equality.

normalized_value_unit_evidence: The same Table 2 row normalizes to kcat=4.4 s^-1 and Km=0.023 mM. Their stored-precision quotient is 4.4 / 0.023 = 191.30434782608697 s^-1 mM^-1. The independently printed efficiency 1.9 × 10^5 M^-1 s^-1 normalizes separately to 190 s^-1 mM^-1 and is preserved as printed precision.

raw_value_unit_evidence: Km raw_value=23 raw_unit=uM; kcat raw_value=4.4 raw_unit=s^-1; printed kcat/Km raw_value=1.9 × 10^5 raw_unit=M^-1 s^-1

table_label: Table 2: Kinetic parameters for TEM-87 beta-lactamase


substrate_name: cefazolin

column_label: PMC Table 2, Cefazolin: Km 54 uM = 0.054 mM; kcat 13 s^-1; printed kcat/Km 2.4 × 10^5 M^-1 s^-1 = 240 s^-1 mM^-1. Current 240.74074074074073 is the exact quotient of the same row's printed kcat and Km cells; the separately printed efficiency is retained without forcing literal equality.

normalized_value_unit_evidence: The same Table 2 row normalizes to kcat=13 s^-1 and Km=0.054 mM. Their stored-precision quotient is 13 / 0.054 = 240.74074074074073 s^-1 mM^-1. The independently printed efficiency 2.4 × 10^5 M^-1 s^-1 normalizes separately to 240 s^-1 mM^-1 and is preserved as printed precision.

raw_value_unit_evidence: Km raw_value=54 raw_unit=uM; kcat raw_value=13 raw_unit=s^-1; printed kcat/Km raw_value=2.4 × 10^5 raw_unit=M^-1 s^-1

row_label: Cefazolin

substrate: cefazolin


column_label: PMC Table 2, Cefotaxime: Km 53 uM = 0.053 mM; kcat 2.2 s^-1; printed kcat/Km 4.1 × 10^4 M^-1 s^-1 = 41 s^-1 mM^-1. Current 41.509433962264154 is the exact quotient of the same row's printed kcat and Km cells; the separately printed efficiency is retained without forcing literal equality.

normalized_value_unit_evidence: The same Table 2 row normalizes to kcat=2.2 s^-1 and Km=0.053 mM. Their stored-precision quotient is 2.2 / 0.053 = 41.509433962264154 s^-1 mM^-1. The independently printed efficiency 4.1 × 10^4 M^-1 s^-1 normalizes separately to 41 s^-1 mM^-1 and is preserved as printed precision.

raw_value_unit_evidence: Km raw_value=53 raw_unit=uM; kcat raw_value=2.2 raw_unit=s^-1; printed kcat/Km raw_value=4.1 × 10^4 raw_unit=M^-1 s^-1


substrate_name: H2O; Nitrocefin

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

substrate: H2O; Nitrocefin


column_label: PMC Table 2, Ceftazidime: Km 94 uM = 0.094 mM; kcat 23 s^-1; printed kcat/Km 2.4 × 10^5 M^-1 s^-1 = 240 s^-1 mM^-1. Current 244.68085106382978 is the exact quotient of the same row's printed kcat and Km cells; the separately printed efficiency is retained without forcing literal equality.

normalized_value_unit_evidence: The same Table 2 row normalizes to kcat=23 s^-1 and Km=0.094 mM. Their stored-precision quotient is 23 / 0.094 = 244.68085106382978 s^-1 mM^-1. The independently printed efficiency 2.4 × 10^5 M^-1 s^-1 normalizes separately to 240 s^-1 mM^-1 and is preserved as printed precision.

raw_value_unit_evidence: Km raw_value=94 raw_unit=uM; kcat raw_value=23 raw_unit=s^-1; printed kcat/Km raw_value=2.4 × 10^5 raw_unit=M^-1 s^-1

row_label: Ceftazidime


column_label: Table 2 'Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates'; row Cefotaxime; IMP-18 kcat/Km/Km cells.

normalized_value_unit_evidence: Table 2 row Cefotaxime, IMP-18 normalized: kcat 0.7 s^-1; Km 0.003 mM; kcat/Km 230 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Cefotaxime, IMP-18 columns: kcat 0.7 s^-1; Km 3 uM; kcat/Km 2.3 x 10^5 M^-1 s^-1.

table_label: Table 2: Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates


column_label: Table 2 'Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates'; row Ertapenem; IMP-18 kcat/Km/Km cells.

normalized_value_unit_evidence: Table 2 row Ertapenem, IMP-18 normalized: kcat 0.03 s^-1; Km 0.0026 mM; kcat/Km 12 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Ertapenem, IMP-18 columns: kcat 0.03 s^-1; Km 2.6 uM; kcat/Km 1.2 x 10^4 M^-1 s^-1.


substrate_name: meropenem

column_label: Table 2 Meropenem row, IMP-18 columns report kcat 0.05 s^-1, Km 8.4 uM, and kcat/Km 6.0 x 10^3 M^-1*s^-1; expected row appears off by factor 10 for Km and kcat/Km

normalized_value_unit_evidence: kcat normalized_value=0.05 normalized_unit=s^-1 matches; paper Km normalized_value=0.0084 normalized_unit=mM does not match expected 0.00084 mM; paper kcat/Km normalized_value=6 normalized_unit=s^-1*mM^-1 does not match expected 59.523809523809526

raw_value_unit_evidence: kcat raw_value=0.05 raw_unit=s^-1; Km raw_value=8.4 raw_unit=uM; kcat/Km raw_value=6.0 x 10^3 raw_unit=M^-1*s^-1

row_label: Meropenem row; IMP-18 columns for kcat, Km, and kcat/Km

table_label: PMID 21041509 Table 2

substrate: meropenem


substrate_name: Imipenem

column_label: Table 2 'Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates'; row Imipenem; IMP-18 kcat/Km/Km cells.

normalized_value_unit_evidence: Table 2 row Imipenem, IMP-18 normalized: kcat 17 s^-1; Km 0.007 mM; kcat/Km 2400 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Imipenem, IMP-18 columns: kcat 17 s^-1; Km 7 uM; kcat/Km 2.4 x 10^6 M^-1 s^-1.

row_label: Imipenem

substrate: Imipenem


substrate_name: ceftazidime

column_label: Table 2 'Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates'; row Ceftazidime; IMP-18 kcat/Km/Km cells.

normalized_value_unit_evidence: Table 2 row Ceftazidime, IMP-18 normalized: kcat 1 s^-1; Km 0.0013 mM; kcat/Km 770 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Ceftazidime, IMP-18 columns: kcat 1 s^-1; Km 1.3 uM; kcat/Km 7.7 x 10^5 M^-1 s^-1.

substrate: ceftazidime


substrate_name: cephalotin

column_label: Table 2 'Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates'; row Cephalothin; IMP-18 kcat/Km/Km cells.

normalized_value_unit_evidence: Table 2 row Cephalothin, IMP-18 normalized: kcat 0.4 s^-1; Km 0.0001 mM; kcat/Km 4000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Cephalothin, IMP-18 columns: kcat 0.4 s^-1; Km 0.1 uM; kcat/Km 4.0 x 10^6 M^-1 s^-1.

substrate: cephalotin


substrate_name: cefuroxime

column_label: Table 2 'Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates'; row Cefuroxime; IMP-18 kcat/Km/Km cells.

normalized_value_unit_evidence: Table 2 row Cefuroxime, IMP-18 normalized: kcat 0.9 s^-1; Km 0.007 mM; kcat/Km 130 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Cefuroxime, IMP-18 columns: kcat 0.9 s^-1; Km 7 uM; kcat/Km 1.3 x 10^5 M^-1 s^-1.

row_label: Cefuroxime

substrate: cefuroxime


substrate_name: benzylpenicillin

column_label: Table 2 'Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates'; row Benzylpenicillin; IMP-18 kcat/Km/Km cells.

normalized_value_unit_evidence: Table 2 row Benzylpenicillin, IMP-18 normalized: kcat 54 s^-1; Km 0.09 mM; kcat/Km 620 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Benzylpenicillin, IMP-18 columns: kcat 54 s^-1; Km 90 uM; kcat/Km 6.2 x 10^5 M^-1 s^-1.

row_label: Benzylpenicillin

substrate: benzylpenicillin


verification_status: unverified

status: unverified


assay_conditions_summary: pH 7.5; 310.15 K; buffer HB (50 mM HEPES

column_label: TABLE 1. Kinetic parameters of purified IMP-13 and comparison with the kinetic parameters of other IMP-type enzymesa; substrate row Ceftazidime; IMP-13 column block; column "kcat (s−1)" = 9 ± 1; column "Km (μM)" = 15 ± 3; column "kcat/Km (μM−1·s−1)" = 0.60.

normalized_value_unit_evidence: kcat: printed cell 9 ± 1 s−1; unit is already s^-1, so 9.0 s^-1. Km: printed cell 15 ± 3 μM; 15.0 μM / 1000 = 0.015 mM. kcat/Km: printed cell 0.60 μM−1·s−1; μM−1·s−1 × 1000 = mM−1·s−1, so 600.0 s^-1 mM^-1. The exact quotient of the paper's own two printed cells is 9.0 s^-1 / 0.015 mM = 600.0 s^-1 mM^-1 = 0.6 μM−1·s−1, which the paper prints as 0.60.

raw_value_unit_evidence: TABLE 1, IMP-13 columns, substrate row Ceftazidime: kcat = 9 ± 1 s−1; Km = 15 ± 3 μM; printed kcat/Km = 0.60 μM−1·s−1.

row_label: TABLE 1, substrate row Ceftazidime, IMP-13 columns


substrate_name: ampicillin

column_label: Table 1 (Kinetic parameters of purified IMP-13 and comparison with the kinetic parameters of other IMP-type enzymes), substrate row 'Ampicillin', IMP-13 column group; column 'kcat (s^-1)' = 82; column 'Km (uM)' = 210; column 'kcat/Km (uM^-1 s^-1)' = 0.38. The three IMP-1 columns and the three IMP-2 columns further along the same printed line belong to the two comparison enzymes and were not read.

normalized_value_unit_evidence: kcat: printed Table 1 cell 82 s^-1; the cell is already per second, so no unit conversion applies and the canonical value is 82.0 s^(-1). Km: printed Table 1 cell 210 uM; 210 / 1000 = 0.21 mM. kcat/Km: printed Table 1 cell 0.38 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.38 x 1000 = 380.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, IMP-13 column group, substrate row 'Ampicillin': kcat = 82 s^-1; Km = 210 uM; printed kcat/Km = 0.38 uM^-1 s^-1.

table_label: Table 1: Kinetic parameters of purified IMP-13 and comparison with the kinetic parameters of other IMP-type enzymes (Antimicrob. Agents Chemother. 2011, 55(1):399-401)

substrate: ampicillin


column_label: Table 1 (Kinetic parameters of purified IMP-13 and comparison with the kinetic parameters of other IMP-type enzymes), substrate row 'Imipenem', IMP-13 column group; column 'kcat (s^-1)' = 120; column 'Km (uM)' = 49; column 'kcat/Km (uM^-1 s^-1)' = 2.5. The three IMP-1 columns and the three IMP-2 columns further along the same printed line belong to the two comparison enzymes and were not read.

normalized_value_unit_evidence: kcat: printed Table 1 cell 120 s^-1; the cell is already per second, so no unit conversion applies and the canonical value is 120.0 s^(-1). Km: printed Table 1 cell 49 uM; 49 / 1000 = 0.049 mM. kcat/Km: printed Table 1 cell 2.5 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 2.5 x 1000 = 2500.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, IMP-13 column group, substrate row 'Imipenem': kcat = 120 s^-1; Km = 49 uM; printed kcat/Km = 2.5 uM^-1 s^-1.


substrate_name: nitrocefin

assay_conditions_summary: pH 7.5; 303.15 K; buffer 10 mM HEPES

column_label: table label: TABLE 2. Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates^d; row label: Nitrocefin; column label: the IMP-18 kcat (s^-1) and IMP-18 Km (uM) cells of this one TABLE 2 row only; no cell is taken from the IMP-1 column group, from another TABLE 2 row, or from any other table; raw value: kcat 55 s^-1, Km 9 uM; raw unit: s^-1 for kcat, uM for Km; normalized value: kcat 55.0 s^-1, Km 0.009 mM, kcat/Km 6111.111111111111 s^-1 mM^-1; normalized unit: s^-1, mM, s^-1 mM^-1; condition label: All measurements were performed on a Cary 100 UV-Vis spectrophotometer (Varian, Walnut Creek, CA) at 30 C in 10 mM HEPES buffer (pH 7.5) containing 50 uM ZnSO4, using a reaction volume of 500 ul. The purified IMP-18 was diluted in the same buffer supplemented with 20 ug/ml bovine serum albumin (BSA) to prevent enzyme denaturation. The steady-state kinetic parameters (kcat and Km) were calculated after direct fit of the initial rates to the Henri-Michaelis-Menten equation or using the Hanes-Woolf linearization. Exported assay conditions: pH 7.5; 303.15 K, which is the 30 C of this Methods paragraph. Table 2 Km cells below 10 uM were measured as inhibition constants: the Methods paragraph states that Km values lower than 10 uM were measured as inhibition constants by using a competitive inhibition model and 100 uM nitrocefin as the reporter substrate.

normalized_value_unit_evidence: kcat 55 s^-1 is already s^-1, giving 55.0 s^-1 at the export's stored precision; exported kcat 55.0 s^(-1). Km 9 uM divided by 1000 gives 0.009 mM at the export's stored precision; exported Km 0.009 mM. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 55.0 s^-1 divided by 0.009 mM giving 6111.111111111111 s^-1 mM^-1, and of nothing else; exported kcat/Km 6111.111111111111 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 2. Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates^d, row Nitrocefin, IMP-18 column group: kcat 55 s^-1; Km 9 uM; printed kcat/Km 6.1 x 10^6 M^-1 s^-1.

row_label: Nitrocefin

substrate: nitrocefin


substrate_name: ticarcillin

substrate: ticarcillin


substrate_name: cefoxitin

column_label: table label: TABLE 2. Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates^d; row label: Cefoxitin; column label: the IMP-18 kcat (s^-1) and IMP-18 Km (uM) cells of this one TABLE 2 row only; no cell is taken from the IMP-1 column group, from another TABLE 2 row, or from any other table; raw value: kcat 2 s^-1, Km 11 uM; raw unit: s^-1 for kcat, uM for Km; normalized value: kcat 2.0 s^-1, Km 0.011 mM, kcat/Km 181.81818181818184 s^-1 mM^-1; normalized unit: s^-1, mM, s^-1 mM^-1; condition label: All measurements were performed on a Cary 100 UV-Vis spectrophotometer (Varian, Walnut Creek, CA) at 30 C in 10 mM HEPES buffer (pH 7.5) containing 50 uM ZnSO4, using a reaction volume of 500 ul. The purified IMP-18 was diluted in the same buffer supplemented with 20 ug/ml bovine serum albumin (BSA) to prevent enzyme denaturation. The steady-state kinetic parameters (kcat and Km) were calculated after direct fit of the initial rates to the Henri-Michaelis-Menten equation or using the Hanes-Woolf linearization. Exported assay conditions: pH 7.5; 303.15 K, which is the 30 C of this Methods paragraph.

normalized_value_unit_evidence: kcat 2 s^-1 is already s^-1, giving 2.0 s^-1 at the export's stored precision; exported kcat 2.0 s^(-1). Km 11 uM divided by 1000 gives 0.011 mM at the export's stored precision; exported Km 0.011 mM. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 2.0 s^-1 divided by 0.011 mM giving 181.81818181818184 s^-1 mM^-1, and of nothing else; exported kcat/Km 181.81818181818184 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 2. Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates^d, row Cefoxitin, IMP-18 column group: kcat 2 s^-1; Km 11 uM; printed kcat/Km 1.8 x 10^5 M^-1 s^-1.

row_label: Cefoxitin

substrate: cefoxitin


column_label: table label: TABLE 2. Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates^d; row label: Ampicillin; column label: the IMP-18 kcat (s^-1) and IMP-18 Km (uM) cells of this one TABLE 2 row only; no cell is taken from the IMP-1 column group, from another TABLE 2 row, or from any other table; raw value: kcat 65 s^-1, Km 103 uM; raw unit: s^-1 for kcat, uM for Km; normalized value: kcat 65.0 s^-1, Km 0.103 mM, kcat/Km 631.0679611650486 s^-1 mM^-1; normalized unit: s^-1, mM, s^-1 mM^-1; condition label: All measurements were performed on a Cary 100 UV-Vis spectrophotometer (Varian, Walnut Creek, CA) at 30 C in 10 mM HEPES buffer (pH 7.5) containing 50 uM ZnSO4, using a reaction volume of 500 ul. The purified IMP-18 was diluted in the same buffer supplemented with 20 ug/ml bovine serum albumin (BSA) to prevent enzyme denaturation. The steady-state kinetic parameters (kcat and Km) were calculated after direct fit of the initial rates to the Henri-Michaelis-Menten equation or using the Hanes-Woolf linearization. Exported assay conditions: pH 7.5; 303.15 K, which is the 30 C of this Methods paragraph.

normalized_value_unit_evidence: kcat 65 s^-1 is already s^-1, giving 65.0 s^-1 at the export's stored precision; exported kcat 65.0 s^(-1). Km 103 uM divided by 1000 gives 0.103 mM at the export's stored precision; exported Km 0.103 mM. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 65.0 s^-1 divided by 0.103 mM giving 631.0679611650486 s^-1 mM^-1, and of nothing else; exported kcat/Km 631.0679611650486 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 2. Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates^d, row Ampicillin, IMP-18 column group: kcat 65 s^-1; Km 103 uM; printed kcat/Km 6.3 x 10^5 M^-1 s^-1.

row_label: Ampicillin


substrate_name: cefepime

column_label: Table 2 'Kinetic parameters of selected IMP-type MBLs for the hydrolysis of various beta-lactam substrates'; row Cefepime; IMP-18 kcat/Km/Km cells.

normalized_value_unit_evidence: Table 2 row Cefepime, IMP-18 normalized: kcat 0.35 s^-1; Km 0.0008 mM; kcat/Km 440 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Cefepime, IMP-18 columns: kcat 0.35 s^-1; Km 0.8 uM; kcat/Km 4.4 x 10^5 M^-1 s^-1.

row_label: Cefepime

substrate: cefepime


column_label: Table 4 'Table 4: Kinetic parameters of VIM enzymes'; row Nitrocefin; VIM-4 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 4 row Nitrocefin, VIM-4 normalized: kcat 690 s^-1; Km 0.022 mM; kcat/Km 31000 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row Nitrocefin, VIM-4 columns: kcat 690 s^-1; Km 22 uM; kcat/Km 31,000 mM^-1 s^-1.


substrate_name: carbenicillin

column_label: Table 4 'Table 4: Kinetic parameters of VIM enzymes'; row Carbenicillin; VIM-4 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 4 row Carbenicillin, VIM-4 normalized: kcat 100 s^-1; Km 0.031 mM; kcat/Km 3300 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row Carbenicillin, VIM-4 columns: kcat 100 s^-1; Km 31 uM; kcat/Km 3,300 mM^-1 s^-1.

row_label: Carbenicillin

substrate: carbenicillin


column_label: Table 4 'Table 4: Kinetic parameters of VIM enzymes'; row Meropenem; VIM-4 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 4 row Meropenem, VIM-4 normalized: kcat 7 s^-1; Km 0.008 mM; kcat/Km 875 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row Meropenem, VIM-4 columns: kcat 7 s^-1; Km 8 uM; kcat/Km 875 mM^-1 s^-1.

row_label: Meropenem


column_label: Table 4 'Table 4: Kinetic parameters of VIM enzymes'; row Cephalothin; VIM-4 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 4 row Cephalothin, VIM-4 normalized: kcat 500 s^-1; Km 0.014 mM; kcat/Km 36000 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row Cephalothin, VIM-4 columns: kcat 500 s^-1; Km 14 uM; kcat/Km 36,000 mM^-1 s^-1.


column_label: Table 4 'Table 4: Kinetic parameters of VIM enzymes'; row Imipenem; VIM-4 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 4 row Imipenem, VIM-4 normalized: kcat 70 s^-1; Km 0.003 mM; kcat/Km 23000 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row Imipenem, VIM-4 columns: kcat 70 s^-1; Km 3 uM; kcat/Km 23,000 mM^-1 s^-1.


column_label: Table 4 'Table 4: Kinetic parameters of VIM enzymes'; row Ampicillin; VIM-4 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 4 row Ampicillin, VIM-4 normalized: kcat 210 s^-1; Km 3 mM; kcat/Km 71 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row Ampicillin, VIM-4 columns: kcat >210 s^-1; Km >3,000 uM; kcat/Km 71 mM^-1 s^-1.


substrate_name: Penicillin G

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

mutation_type: substitution

substrate: Penicillin G


substrate_name: Cephalothin

substrate: Cephalothin


substrate_name: Cephaloridine

substrate: Cephaloridine


substrate_name: aztreonam

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

substrate: aztreonam


substrate_name: Penicillin G; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N104G

substrate: Penicillin G; H2O


substrate_name: Ceftazidime

substrate: Ceftazidime


substrate_name: cefotaxime

substrate: cefotaxime


column_label: Table 2, Cefepime row, kcat column 1 s^-1, Km column 150 uM, kcat/Km column 7 mM^-1 s^-1.

normalized_value_unit_evidence: kcat=1 s^-1; Km=0.15 mM; printed kcat/Km=7 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 Cefepime row: kcat 1 s^-1; Km 150 uM; kcat/Km 7 mM^-1 s^-1.

table_label: Table 2. Kinetic parameters of BEL-1


substrate_name: H2O; Cefotaxime

substrate: H2O; Cefotaxime


substrate_name: Meropenem

column_label: Table 4; row Meropenem; enzyme column VIM-1; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 20 +/- 0.2, Km 72 +/- 7.7, kcat/Km 2.8E5

normalized_value_unit_evidence: kcat=20 s^-1; Km=0.072 mM; kcat/Km=280 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-1 / Meropenem

substrate: Meropenem


column_label: Table 4; row Meropenem; enzyme column VIM-13; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 9 +/- 1.5, Km 15.5 +/- 2.3, kcat/Km 5.92E5

normalized_value_unit_evidence: kcat=9 s^-1; Km=0.0155 mM; kcat/Km=592 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-13 / Meropenem


column_label: Table 4; row Cefepime; enzyme column VIM-1; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 119 +/- 17, Km 337 +/- 110, kcat/Km 3.5E5

normalized_value_unit_evidence: kcat=119 s^-1; Km=0.337 mM; kcat/Km=350 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-1 / Cefepime


substrate_name: Cefuroxime

column_label: Table 4; row Cefuroxime; enzyme column VIM-1; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 239 +/- 22, Km 148 +/- 36, kcat/Km 1.6E6

normalized_value_unit_evidence: kcat=239 s^-1; Km=0.148 mM; kcat/Km=1600 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-1 / Cefuroxime

substrate: Cefuroxime


substrate_name: Imipenem

column_label: Table 4; row Imipenem; enzyme column VIM-1; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 3.4 +/- 1.2, Km 4 +/- 1.9, kcat/Km 8.38E5

normalized_value_unit_evidence: kcat=3.4 s^-1; Km=0.004 mM; kcat/Km=838 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-1 / Imipenem

substrate: Imipenem


column_label: Table 4; row Cephalothin; enzyme column VIM-13; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); raw cells kcat 656 +/- 143, Km 76 +/- 16, kcat/Km 8.6E6

normalized_value_unit_evidence: kcat=656 s^-1; Km=0.076 mM; kcat/Km=8600 s^-1 mM^-1 (explicit Table 4 ratio normalized from M^-1 s^-1)

row_label: VIM-13 / Cephalothin


assay_conditions_summary: pH 7; 303.15 K; buffer 0.1 M phosphate

column_label: Table 2 PER-1 row under Ceftazidime reports Km=3519 uM, kcat=70 s^-1, and kcat/Km=19.9 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=3.519 normalized_unit=mM; kcat normalized_value=70 normalized_unit=s^-1; kcat_over_km normalized_value=19.89201477692526 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=3519 raw_unit=uM; kcat raw_value=70 raw_unit=s^-1; kcat/Km raw_value=19.9 raw_unit=s^-1*mM^-1

row_label: PER-1 row; Ceftazidime columns Km, kcat, kcat/Km

table_label: Biochemical Journal PDF page 5 / journal page 1447, Table 2: Kinetic parameters for hydrolysis of beta-lactams by PER-1 and mutant enzymes


substrate_name: H2O; Penicillin G

substrate: H2O; Penicillin G


substrate_name: H2O; Cephaloridine

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant E166A

substrate: H2O; Cephaloridine


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant A164S


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Q104G


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant S238G


substrate_name: biapenem

column_label: Table 4 'Table 4: Kinetic parameters of VIM enzymes'; row Biapenem; VIM-4 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 4 row Biapenem, VIM-4 normalized: kcat 15 s^-1; Km 0.066 mM; kcat/Km 230 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row Biapenem, VIM-4 columns: kcat 15 s^-1; Km 66 uM; kcat/Km 230 mM^-1 s^-1.

row_label: Biapenem

substrate: biapenem


substrate_name: benzylpenicillin

column_label: Table 4 'Table 4: Kinetic parameters of VIM enzymes'; row Benzylpenicillin; VIM-4 kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 4 row Benzylpenicillin, VIM-4 normalized: kcat 650 s^-1; Km 0.18 mM; kcat/Km 3100 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row Benzylpenicillin, VIM-4 columns: kcat 650 s^-1; Km 180 uM; kcat/Km 3,100 mM^-1 s^-1.

substrate: benzylpenicillin


substrate_name: Nitrocefin; H2O

substrate: Nitrocefin; H2O


substrate_name: Cephaloridine; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant T104E

substrate: Cephaloridine; H2O


substrate_name: Penicillin G

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant G240E

substrate: Penicillin G


substrate_name: Cephalothin

column_label: Table 2 PER-1 row under Cephalothin reports Km=46 uM, kcat=12.4 s^-1, and kcat/Km=269 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.046 normalized_unit=mM; kcat normalized_value=12.4 normalized_unit=s^-1; kcat_over_km normalized_value=269.5652173913044 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=46 raw_unit=uM; kcat raw_value=12.4 raw_unit=s^-1; kcat/Km raw_value=269 raw_unit=s^-1*mM^-1

row_label: PER-1 row; Cephalothin columns Km, kcat, kcat/Km

substrate: Cephalothin


organism: Serratia fonticola

column_label: Official ScienceDirect HTML Table 2 row Cefotaxime gives columns kcat 920 s^-1, Km 80 uM, and kcat/Km 11500 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=920 normalized_unit=s^-1; Km normalized_value=0.08 normalized_unit=mM; kcat/Km normalized_value=11500 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=920 raw_unit=s^-1; Km raw_value=80 raw_unit=uM; kcat/Km raw_value=11500 raw_unit=mM^-1 s^-1

row_label: Cefotaxime

table_label: Table 2. Kinetic parameters of beta-lactamase of Serratia fonticola CUV


substrate_name: ceftriaxone

column_label: Official ScienceDirect HTML Table 2 row Ceftriaxone gives columns kcat 620 s^-1, Km 28 uM, and kcat/Km 22150 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=620 normalized_unit=s^-1; Km normalized_value=0.028 normalized_unit=mM; kcat/Km normalized_value=22150 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=620 raw_unit=s^-1; Km raw_value=28 raw_unit=uM; kcat/Km raw_value=22150 raw_unit=mM^-1 s^-1

row_label: Ceftriaxone

substrate: ceftriaxone


substrate_name: Cloxacillin

column_label: Official ScienceDirect HTML Table 2 row Cloxacillin gives columns kcat 90 s^-1, Km 43 uM, and kcat/Km 2100 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=90 normalized_unit=s^-1; Km normalized_value=0.043 normalized_unit=mM; kcat/Km normalized_value=2100 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=90 raw_unit=s^-1; Km raw_value=43 raw_unit=uM; kcat/Km raw_value=2100 raw_unit=mM^-1 s^-1

row_label: Cloxacillin

substrate: Cloxacillin


substrate_name: Cefoperazone

column_label: Official ScienceDirect HTML Table 2 row Cefoperazone gives columns kcat 70 s^-1, Km 10 uM, and kcat/Km 7000 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=70 normalized_unit=s^-1; Km normalized_value=0.01 normalized_unit=mM; kcat/Km normalized_value=7000 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=70 raw_unit=s^-1; Km raw_value=10 raw_unit=uM; kcat/Km raw_value=7000 raw_unit=mM^-1 s^-1

row_label: Cefoperazone

substrate: Cefoperazone


substrate_name: Mezlocillin sodium

column_label: Official ScienceDirect HTML Table 2 row Mezlocillin gives columns kcat 255 s^-1, Km 15 uM, and kcat/Km 17000 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=255 normalized_unit=s^-1; Km normalized_value=0.015 normalized_unit=mM; kcat/Km normalized_value=17000 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=255 raw_unit=s^-1; Km raw_value=15 raw_unit=uM; kcat/Km raw_value=17000 raw_unit=mM^-1 s^-1

row_label: Mezlocillin

substrate: Mezlocillin sodium


substrate_name: cefepime

column_label: Official ScienceDirect HTML Table 2 row Cefepime gives columns kcat 225 s^-1, Km 430 uM, and kcat/Km 525 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=225 normalized_unit=s^-1; Km normalized_value=0.43 normalized_unit=mM; kcat/Km normalized_value=525 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=225 raw_unit=s^-1; Km raw_value=430 raw_unit=uM; kcat/Km raw_value=525 raw_unit=mM^-1 s^-1

row_label: Cefepime

substrate: cefepime


substrate_name: Amoxycillin

column_label: Official ScienceDirect HTML Table 2 row Amoxycillin gives columns kcat 460 s^-1, Km 35 uM, and kcat/Km 13150 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=460 normalized_unit=s^-1; Km normalized_value=0.035 normalized_unit=mM; kcat/Km normalized_value=13150 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=460 raw_unit=s^-1; Km raw_value=35 raw_unit=uM; kcat/Km raw_value=13150 raw_unit=mM^-1 s^-1

row_label: Amoxycillin

substrate: Amoxycillin


column_label: Official ScienceDirect HTML Table 2 row Cephalothin gives columns kcat 7150 s^-1, Km 175 uM, and kcat/Km 40900 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=7150 normalized_unit=s^-1; Km normalized_value=0.175 normalized_unit=mM; kcat/Km normalized_value=40900 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=7150 raw_unit=s^-1; Km raw_value=175 raw_unit=uM; kcat/Km raw_value=40900 raw_unit=mM^-1 s^-1

row_label: Cephalothin


enzyme_display_name: pyruvate kinase

organism: Amycolatopsis methanolica

substrate_name: Phosphoenolpyruvate; ADP

kcat_display: Not reported

enzyme: pyruvate kinase

substrate: Phosphoenolpyruvate; ADP


organism: Arabidopsis thaliana

km_display: Not reported


substrate_name: ADP

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ADP

substrate: ADP


substrate_name: phosphoenolpyruvate

substrate: phosphoenolpyruvate


organism: Bos taurus


organism: Chlamydia trachomatis


substrate_name: Ceftazidime

column_label: Official ScienceDirect HTML Table 2 row Ceftazidime gives columns kcat 30 s^-1, Km 500 uM, and kcat/Km 60 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=30 normalized_unit=s^-1; Km normalized_value=0.5 normalized_unit=mM; kcat/Km normalized_value=60 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=30 raw_unit=s^-1; Km raw_value=500 raw_unit=uM; kcat/Km raw_value=60 raw_unit=mM^-1 s^-1

row_label: Ceftazidime

substrate: Ceftazidime


substrate_name: Cefuroxime

column_label: Official ScienceDirect HTML Table 2 row Cefuroxime gives columns kcat 540 s^-1, Km 20 uM, and kcat/Km 27000 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=540 normalized_unit=s^-1; Km normalized_value=0.02 normalized_unit=mM; kcat/Km normalized_value=27000 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=540 raw_unit=s^-1; Km raw_value=20 raw_unit=uM; kcat/Km raw_value=27000 raw_unit=mM^-1 s^-1

row_label: Cefuroxime

substrate: Cefuroxime


substrate_name: cefpirome

column_label: Official ScienceDirect HTML Table 2 row Cefpirome gives columns kcat 745 s^-1, Km 440 uM, and kcat/Km 1690 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=745 normalized_unit=s^-1; Km normalized_value=0.44 normalized_unit=mM; kcat/Km normalized_value=1690 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=745 raw_unit=s^-1; Km raw_value=440 raw_unit=uM; kcat/Km raw_value=1690 raw_unit=mM^-1 s^-1

row_label: Cefpirome

substrate: cefpirome


substrate_name: cefotiam

column_label: Official ScienceDirect HTML Table 2 row Cefotiam gives columns kcat 945 s^-1, Km 55 uM, and kcat/Km 17200 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=945 normalized_unit=s^-1; Km normalized_value=0.055 normalized_unit=mM; kcat/Km normalized_value=17200 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=945 raw_unit=s^-1; Km raw_value=55 raw_unit=uM; kcat/Km raw_value=17200 raw_unit=mM^-1 s^-1

row_label: Cefotiam

substrate: cefotiam


substrate_name: Penicillin G; H2O

substrate: Penicillin G; H2O


substrate_name: Ticarcillin

column_label: Official ScienceDirect HTML Table 2 row Ticarcillin gives columns kcat 115 s^-1, Km 31 uM, and kcat/Km 3700 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=115 normalized_unit=s^-1; Km normalized_value=0.031 normalized_unit=mM; kcat/Km normalized_value=3700 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=115 raw_unit=s^-1; Km raw_value=31 raw_unit=uM; kcat/Km raw_value=3700 raw_unit=mM^-1 s^-1

row_label: Ticarcillin

substrate: Ticarcillin


substrate_name: carbenicillin

column_label: Official ScienceDirect HTML Table 2 row Carbenicillin gives columns kcat 100 s^-1, Km 40 uM, and kcat/Km 2500 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=100 normalized_unit=s^-1; Km normalized_value=0.04 normalized_unit=mM; kcat/Km normalized_value=2500 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=100 raw_unit=s^-1; Km raw_value=40 raw_unit=uM; kcat/Km raw_value=2500 raw_unit=mM^-1 s^-1

row_label: Carbenicillin

substrate: carbenicillin


substrate_name: moxalactam

source_db: skid

source_license: CC BY-NC-ND 4.0

substrate: moxalactam

source: skid


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: Cephalothin

substrate: Cephalothin


substrate_name: Cephaloridine

column_label: Table 2 PER-1 row under Cephaloridine reports Km=237 uM, kcat=13 s^-1, and kcat/Km=55 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.237 normalized_unit=mM; kcat normalized_value=13 normalized_unit=s^-1; kcat_over_km normalized_value=54.85232067510549 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=237 raw_unit=uM; kcat raw_value=13 raw_unit=s^-1; kcat/Km raw_value=55 raw_unit=s^-1*mM^-1

row_label: PER-1 row; Cephaloridine columns Km, kcat, kcat/Km

substrate: Cephaloridine


substrate_name: cefotaxime

substrate: cefotaxime


substrate_name: ceftazidime; ampicillin; cephalotin; cefotaxime; cefepime; ertapenem; cefoxitin; cefuroxime; ticarcillin; piperacillin; Imipenem; meropenem

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----


organism: Pseudomonas fluorescens


organism: Pseudomonas putida

substrate_name: Ampicillin; H2O

substrate: Ampicillin; H2O


column_label: Official PMC Table 1 row Carbenicillin Sfh-I columns: kcat=9.15 +/- 1.58 s^-1, Km=1,280 +/- 363 uM, kcat/Km=7.18 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat 9.15 s^-1; Km 1.28 mM; primary table kcat/Km 7.18 s^-1 mM^-1. Exported kcat/Km 7.1484375 s^-1 mM^-1 is consistent with table significant-figure rounding/computation from displayed kcat and Km.

table_label: Table 1. Kinetic parameters of purified Sfh-I beta-lactamase and comparison with other B2 metallo-beta-lactamases.


column_label: Official PMC Table 1 row Moxalactam Sfh-I columns: kcat=0.017 +/- 0.0012 s^-1, Km=91 +/- 14 uM, kcat/Km=1.87 x 10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat 0.017 s^-1; Km 0.091 mM; primary table kcat/Km 0.187 s^-1 mM^-1. Exported kcat/Km 0.18681318681318684 s^-1 mM^-1 is consistent with table significant-figure rounding/computation from displayed kcat and Km.

row_label: Moxalactam


substrate_name: cefepime

column_label: Official PMC Table 1 row Cefepime Sfh-I columns: kcat=0.64 +/- 0.073 s^-1, Km=202 +/- 43.7 uM, kcat/Km=3.16 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat 0.64 s^-1; Km 0.202 mM; primary table kcat/Km 3.16 s^-1 mM^-1. Exported kcat/Km 3.168316831683168 s^-1 mM^-1 is consistent with table significant-figure rounding/computation from displayed kcat and Km.

substrate: cefepime


substrate_name: cefoxitin

column_label: Official PMC Table 1 row Cefoxitin Sfh-I columns: kcat=0.032 +/- 0.00094 s^-1, Km=99 +/- 7 uM, kcat/Km=3.23 x 10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat 0.032 s^-1; Km 0.099 mM; primary table kcat/Km 0.323 s^-1 mM^-1. Exported kcat/Km 0.3232323232323232 s^-1 mM^-1 is consistent with table significant-figure rounding/computation from displayed kcat and Km.

row_label: Cefoxitin

substrate: cefoxitin


substrate_name: meropenem

column_label: Official PMC Table 1 row Meropenem Sfh-I columns: kcat=109 +/- 9.5 s^-1, Km=215 +/- 47.0 uM, kcat/Km=5.05 x 10^5 M^-1 s^-1.

normalized_value_unit_evidence: kcat 109.0 s^-1; Km 0.215 mM; primary table kcat/Km 505.0 s^-1 mM^-1. Exported kcat/Km 506.9767441860465 s^-1 mM^-1 is consistent with table significant-figure rounding/computation from displayed kcat and Km.

row_label: Meropenem

substrate: meropenem


substrate_name: ampicillin

column_label: Official PMC Table 1 row Ampicillin Sfh-I columns: kcat=9.5 +/- 1.11 s^-1, Km=676 +/- 187 uM, kcat/Km=1.41 x 10^4 M^-1 s^-1.

normalized_value_unit_evidence: kcat 9.5 s^-1; Km 0.676 mM; primary table kcat/Km 14.1 s^-1 mM^-1. Exported kcat/Km 14.053254437869821 s^-1 mM^-1 is consistent with table significant-figure rounding/computation from displayed kcat and Km.

row_label: Ampicillin

substrate: ampicillin


organism: Homo sapiens

substrate_name: ADP

assay_conditions_summary: pH 8; 310.15 K; cofactor ADP

substrate: ADP


substrate_name: Phosphoenolpyruvate

substrate: Phosphoenolpyruvate


substrate_name: Fructose 1,6-bisphosphate

substrate: Fructose 1,6-bisphosphate


substrate_name: phosphoenolpyruvate

substrate: phosphoenolpyruvate


substrate_name: Pyruvate; ATP

ki_unit: mM

assay_conditions_summary: 303.15 K; cofactor ATP

substrate: Pyruvate; ATP


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=32°C, pH=8
Raw SKiD Env: Temp=25°C, pH=6


organism: Lactococcus lactis subsp. cremoris

substrate_name: ADP; Phosphoenolpyruvate

assay_conditions_summary: cofactor ADP

substrate: ADP; Phosphoenolpyruvate


substrate_name: Imipenem

column_label: Table 1, substrate Imipenem, Sfh-I kcat cell 51, Sfh-I Km cell 79.2 uM, and Sfh-I kcat/Km cell 6.42 x 10^5 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=51.0 normalized_unit=s^-1; Km normalized_value=0.0792 normalized_unit=mM; kcat/Km normalized_value=643.9393939393939 normalized_unit=s^-1 mM^-1 from 51.0 / 0.0792.

raw_value_unit_evidence: Table 1 Sfh-I imipenem cells: kcat raw_value=51 s^-1 raw_unit=s^-1; Km raw_value=79.2 uM raw_unit=uM; kcat/Km raw_value=6.42 x 10^5 M^-1 s^-1 raw_unit=M^-1 s^-1.

row_label: Sfh-I beta-lactamase row: Imipenem

table_label: PMC3195014 Table 1

substrate: Imipenem


substrate_name: nitrocefin

column_label: Table 1, substrate Nitrocefin, Sfh-I kcat cell 0.06, Sfh-I Km cell 106 uM, and Sfh-I kcat/Km cell 5.7 x 10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=0.06 normalized_unit=s^-1; Km normalized_value=0.106 normalized_unit=mM; kcat/Km normalized_value=0.5660377358490566 normalized_unit=s^-1 mM^-1 from 0.06 / 0.106.

raw_value_unit_evidence: Table 1 Sfh-I nitrocefin cells: kcat raw_value=0.06 s^-1 raw_unit=s^-1; Km raw_value=106 uM raw_unit=uM; kcat/Km raw_value=5.7 x 10^2 M^-1 s^-1 raw_unit=M^-1 s^-1.

row_label: Sfh-I beta-lactamase row: Nitrocefin

substrate: nitrocefin


substrate_name: piperacillin

column_label: Official ScienceDirect HTML Table 2 row Piperacillin gives columns kcat 255 s^-1, Km 23 uM, and kcat/Km 11000 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=255 normalized_unit=s^-1; Km normalized_value=0.023 normalized_unit=mM; kcat/Km normalized_value=11000 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=255 raw_unit=s^-1; Km raw_value=23 raw_unit=uM; kcat/Km raw_value=11000 raw_unit=mM^-1 s^-1

row_label: Piperacillin

substrate: piperacillin


substrate_name: Cephaloridine

column_label: Official ScienceDirect HTML Table 2 row Cephaloridine gives columns kcat 2530 s^-1, Km 175 uM, and kcat/Km 14500 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=2530 normalized_unit=s^-1; Km normalized_value=0.175 normalized_unit=mM; kcat/Km normalized_value=14500 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=2530 raw_unit=s^-1; Km raw_value=175 raw_unit=uM; kcat/Km raw_value=14500 raw_unit=mM^-1 s^-1

row_label: Cephaloridine


substrate_name: Cefamandole

column_label: Official ScienceDirect HTML Table 2 row Cefamandole gives columns kcat 6105 s^-1, Km 200 uM, and kcat/Km 30500 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=6105 normalized_unit=s^-1; Km normalized_value=0.2 normalized_unit=mM; kcat/Km normalized_value=30500 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=6105 raw_unit=s^-1; Km raw_value=200 raw_unit=uM; kcat/Km raw_value=30500 raw_unit=mM^-1 s^-1

row_label: Cefamandole

substrate: Cefamandole


substrate_name: Penicillin G

column_label: Official ScienceDirect HTML Table 2 row Benzylpenicillin gives columns kcat 770 s^-1, Km 23 uM, and kcat/Km 33500 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=770 normalized_unit=s^-1; Km normalized_value=0.023 normalized_unit=mM; kcat/Km normalized_value=33500 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=770 raw_unit=s^-1; Km raw_value=23 raw_unit=uM; kcat/Km raw_value=33500 raw_unit=mM^-1 s^-1

row_label: Benzylpenicillin

substrate: Penicillin G


substrate_name: Oxacillin

column_label: Official ScienceDirect HTML Table 2 row Oxacillin gives columns kcat 105 s^-1, Km 42 uM, and kcat/Km 2500 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=105 normalized_unit=s^-1; Km normalized_value=0.042 normalized_unit=mM; kcat/Km normalized_value=2500 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=105 raw_unit=s^-1; Km raw_value=42 raw_unit=uM; kcat/Km raw_value=2500 raw_unit=mM^-1 s^-1

row_label: Oxacillin

substrate: Oxacillin


substrate_name: aztreonam

column_label: Official ScienceDirect HTML Table 2 row Aztreonam gives columns kcat 38 s^-1, Km 41 uM, and kcat/Km 930 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=38 normalized_unit=s^-1; Km normalized_value=0.041 normalized_unit=mM; kcat/Km normalized_value=930 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=38 raw_unit=s^-1; Km raw_value=41 raw_unit=uM; kcat/Km raw_value=930 raw_unit=mM^-1 s^-1

row_label: Aztreonam

substrate: aztreonam


organism: Saccharomyces cerevisiae

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant Y436F


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant Q299N


substrate_name: Phosphoenolpyruvate; ADP

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant A458K

substrate: Phosphoenolpyruvate; ADP


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant K236Q


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant Y436S


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant T406R


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R409Q


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R369A


organism: Corynebacterium glutamicum

assay_conditions_summary: pH 7; 308.15 K; cofactor ADP


organism: Entamoeba histolytica


organism: Escherichia coli

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant K382Q


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R431E


organism: Rattus norvegicus


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 A398R/E432A


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 A398R/E432K


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 E432A


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 E432D


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 E432K


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 A398R


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant M1 A398R/E432D


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R271L


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant K413Q


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R510Q


sequence_source: UniProtKB REST API


organism: Ricinus communis


sequence_source: UniProtKB REST API; reconstructed from canonical sequence and mutation signature T403E

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: pyruvate kinase(Enzyme) mutant T403E


assay_conditions_summary: cofactor ATP

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R336K


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R336Q


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant T403K


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R459Q


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant K292Q


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant T311M


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant E392A


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R77Q


assay_conditions_summary: pH 6.8; cofactor ADP

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant isoenzyme Pyk1 T298S


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant isoenzyme Pyk1 T298A


organism: Lactococcus lactis subsp. lactis


organism: Leishmania mexicana

assay_conditions_summary: pH 7.5; cofactor ADP


organism: Mus musculus

substrate_name: ATP; Pyruvate

substrate: ATP; Pyruvate


organism: Oncorhynchus mykiss

substrate_name: AMP; Phosphate; Phosphoenolpyruvate

substrate: AMP; Phosphate; Phosphoenolpyruvate


organism: Oryctolagus cuniculus


organism: Plasmodium falciparum

substrate_name: ADP


organism: Serratia marcescens

substrate_name: Ampicillin; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H105Y

substrate: Ampicillin; H2O


substrate_name: H2O; Ampicillin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H105W

substrate: H2O; Ampicillin


substrate_name: Nitrocefin

substrate: Nitrocefin


substrate_name: Cephazoline

substrate: Cephazoline


substrate_name: Cefuroxime

substrate: Cefuroxime


substrate_name: cefotaxime

substrate: cefotaxime


substrate_name: H2O; Cephaloridine

substrate: H2O; Cephaloridine


substrate_name: moxalactam

substrate: moxalactam


organism: Trypanosoma brucei

substrate_name: ADP; Phosphoenolpyruvate

substrate: ADP; Phosphoenolpyruvate


organism: Trypanosoma brucei brucei

substrate_name: phosphoenolpyruvate

substrate: phosphoenolpyruvate


organism: Trypanosoma congolense


organism: Ustilago maydis


organism: Zymomonas mobilis


organism: Saccharomyces cerevisiae

substrate_name: Phosphoenolpyruvate

sequence_source: UniProtKB accession lookup: P00549

substrate: Phosphoenolpyruvate


assay_conditions_summary: pH 6.5; 303.15 K; cofactor ADP

substrate: ADP


sequence_source: reconstructed_variant_sequence from UniProtKB P00549

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant isoenzyme PYK1 S384P


sequence_source: UniProtKB accession lookup: P52489


organism: Trichomonas vaginalis


substrate_name: Cephaloridine; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120(81)A

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120(81)E

substrate: Cephaloridine; H2O


substrate_name: Cephaloridine

substrate: Cephaloridine


substrate_name: Imipenem

substrate: Imipenem


substrate_name: Penicillin G

substrate: Penicillin G


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H105R


organism: Stenotrophomonas maltophilia


substrate_name: Cefaclor

substrate: Cefaclor


substrate_name: Ampicillin

substrate: Ampicillin


substrate_name: Cephalothin

column_label: Table 2 Cephalothin row; kcat column 1100 +/- 50 s-1; Km column 67 +/- 4 uM; kcat/Km column 16 x 10^6 M-1 s-1.

row_label: Cephalothin row; kcat, Km, kcat/Km columns

table_label: PMID 3548700 Table 2: Kinetic parameters of Serratia marcescens beta-lactamase at pH 8.2

substrate: Cephalothin


column_label: Table 2 Benzylpenicillin row; kcat column 75 +/- 3 s-1; Km column 1.7 +/- 0.2 uM; kcat/Km column 44 x 10^6 M-1 s-1.

raw_value_unit_evidence: Benzylpenicillin row: kcat = 75 +/- 3 s-1; Km = 1.7 +/- 0.2 uM; kcat/Km = 44 x 10^6 M-1 s-1.

row_label: Benzylpenicillin row; kcat, Km, kcat/Km columns


substrate_name: cefoxitin

column_label: Table 2 Cefoxitin row; kcat column 0.014 +/- 0.002 s-1; Km column 0.3 +/- 0.03 uM; kcat/Km column 47000 M-1 s-1.

row_label: Cefoxitin row; kcat, Km, kcat/Km columns

substrate: cefoxitin


substrate_name: Ampicillin; H2O

substrate: Ampicillin; H2O


organism: Shewanella algae

substrate_name: Oxacillin

column_label: Table 2. Kinetic parameters and relative kcat/Km values of purified beta-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1.; row OXA-55 / Oxacillin; columns OXA-55 kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1); cells kcat 5, Km 390, kcat/Km 10.

normalized_value_unit_evidence: kcat normalized_value=5 normalized_unit=s^-1; Km normalized_value=0.39 normalized_unit=mM; kcat/Km normalized_value=10 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row OXA-55 / Oxacillin: kcat 5 s^-1; Km 390 uM; kcat/Km 10 mM^-1 s^-1; relative kcat/Km 6.

row_label: OXA-55 / Oxacillin

substrate: Oxacillin


substrate_name: Ceftazidime

column_label: Table 2. Kinetic parameters and relative kcat/Km values of purified beta-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1.; row OXA-55 / Ceftazidime; columns OXA-55 kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1); cells kcat 2, Km 4,700, kcat/Km 0.5.

normalized_value_unit_evidence: kcat normalized_value=2 normalized_unit=s^-1; Km normalized_value=4.7 normalized_unit=mM; kcat/Km normalized_value=0.5 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row OXA-55 / Ceftazidime: kcat 2 s^-1; Km 4,700 uM; kcat/Km 0.5 mM^-1 s^-1; relative kcat/Km 0.25.

row_label: OXA-55 / Ceftazidime

substrate: Ceftazidime


column_label: Table 2. Kinetic parameters and relative kcat/Km values of purified beta-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1.; row OXA-55 / Cephalothin; columns OXA-55 kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1); cells kcat 0.6, Km 70, kcat/Km 10.

normalized_value_unit_evidence: kcat normalized_value=0.6 normalized_unit=s^-1; Km normalized_value=0.07 normalized_unit=mM; kcat/Km normalized_value=10 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row OXA-55 / Cephalothin: kcat 0.6 s^-1; Km 70 uM; kcat/Km 10 mM^-1 s^-1; relative kcat/Km 5.

row_label: OXA-55 / Cephalothin


column_label: Table 2. Kinetic parameters and relative kcat/Km values of purified beta-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1.; row OXA-55 / Ampicillin; columns OXA-55 kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1); cells kcat 8, Km 500, kcat/Km 15.

normalized_value_unit_evidence: kcat normalized_value=8 normalized_unit=s^-1; Km normalized_value=0.5 normalized_unit=mM; kcat/Km normalized_value=15 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row OXA-55 / Ampicillin: kcat 8 s^-1; Km 500 uM; kcat/Km 15 mM^-1 s^-1; relative kcat/Km 10.

row_label: OXA-55 / Ampicillin


substrate_name: Meropenem

column_label: Table 2. Kinetic parameters and relative kcat/Km values of purified beta-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1.; row OXA-55 / Meropenem; columns OXA-55 kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1); cells kcat 0.05, Km 500, kcat/Km 0.1.

normalized_value_unit_evidence: kcat normalized_value=0.05 normalized_unit=s^-1; Km normalized_value=0.5 normalized_unit=mM; kcat/Km normalized_value=0.1 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row OXA-55 / Meropenem: kcat 0.05 s^-1; Km 500 uM; kcat/Km 0.1 mM^-1 s^-1; relative kcat/Km 0.06.

row_label: OXA-55 / Meropenem

substrate: Meropenem


column_label: Table 2. Kinetic parameters and relative kcat/Km values of purified beta-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1.; row OXA-55 / Cephaloridine; columns OXA-55 kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1); cells kcat 10, Km 750, kcat/Km 15.

normalized_value_unit_evidence: kcat normalized_value=10 normalized_unit=s^-1; Km normalized_value=0.75 normalized_unit=mM; kcat/Km normalized_value=15 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row OXA-55 / Cephaloridine: kcat 10 s^-1; Km 750 uM; kcat/Km 15 mM^-1 s^-1; relative kcat/Km 9.

row_label: OXA-55 / Cephaloridine


column_label: Table 2. Kinetic parameters and relative kcat/Km values of purified beta-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1.; row OXA-55 / Imipenem; columns OXA-55 kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1); cells kcat 0.1, Km 20, kcat/Km 5.

normalized_value_unit_evidence: kcat normalized_value=0.1 normalized_unit=s^-1; Km normalized_value=0.02 normalized_unit=mM; kcat/Km normalized_value=5 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row OXA-55 / Imipenem: kcat 0.1 s^-1; Km 20 uM; kcat/Km 5 mM^-1 s^-1; relative kcat/Km 3.

row_label: OXA-55 / Imipenem


substrate_name: piperacillin

column_label: Table 2. Kinetic parameters and relative kcat/Km values of purified beta-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1.; row OXA-55 / Piperacillin; columns OXA-55 kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1); cells kcat 3, Km 110, kcat/Km 30.

normalized_value_unit_evidence: kcat normalized_value=3 normalized_unit=s^-1; Km normalized_value=0.11 normalized_unit=mM; kcat/Km normalized_value=30 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row OXA-55 / Piperacillin: kcat 3 s^-1; Km 110 uM; kcat/Km 30 mM^-1 s^-1; relative kcat/Km 17.

row_label: OXA-55 / Piperacillin

substrate: piperacillin


column_label: Table 2. Kinetic parameters and relative kcat/Km values of purified beta-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1.; row OXA-55 / Benzylpenicillin; columns OXA-55 kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1); cells kcat 4, Km 25, kcat/Km 160.

normalized_value_unit_evidence: kcat normalized_value=4 normalized_unit=s^-1; Km normalized_value=0.025 normalized_unit=mM; kcat/Km normalized_value=160 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row OXA-55 / Benzylpenicillin: kcat 4 s^-1; Km 25 uM; kcat/Km 160 mM^-1 s^-1; relative kcat/Km 100.

row_label: OXA-55 / Benzylpenicillin


substrate_name: H2O; Penicillin G

substrate: H2O; Penicillin G


substrate_name: Ticarcillin

column_label: Table 2. Kinetic parameters and relative kcat/Km values of purified beta-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1.; row OXA-55 / Ticarcillin; columns OXA-55 kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1); cells kcat 1, Km 20, kcat/Km 50.

normalized_value_unit_evidence: kcat normalized_value=1 normalized_unit=s^-1; Km normalized_value=0.02 normalized_unit=mM; kcat/Km normalized_value=50 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row OXA-55 / Ticarcillin: kcat 1 s^-1; Km 20 uM; kcat/Km 50 mM^-1 s^-1; relative kcat/Km 31.

row_label: OXA-55 / Ticarcillin

substrate: Ticarcillin


substrate_name: H2O; Nitrocefin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N233L

substrate: H2O; Nitrocefin


substrate_name: biapenem

substrate: biapenem


substrate_name: Nitrocefin; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant S224A

substrate: Nitrocefin; H2O


substrate_name: Nitrocefin

substrate: Nitrocefin


substrate_name: Imipenem

substrate: Imipenem


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant F158A


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: Cefaclor

substrate: Cefaclor


substrate_name: Ampicillin

substrate: Ampicillin


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant S224D


substrate_name: cefpirome

sequence_source: UniProtKB REST API canonical sequence

column_label: Table 2. Kinetic parameters and relative kcat/Km values of purified beta-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1.; row OXA-55 / Cefpirome; columns OXA-55 kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1); cells kcat 0.1, Km 670, kcat/Km 0.1.

normalized_value_unit_evidence: kcat normalized_value=0.1 normalized_unit=s^-1; Km normalized_value=0.67 normalized_unit=mM; kcat/Km normalized_value=0.1 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row OXA-55 / Cefpirome: kcat 0.1 s^-1; Km 670 uM; kcat/Km 0.1 mM^-1 s^-1; relative kcat/Km 0.06.

row_label: OXA-55 / Cefpirome

substrate: cefpirome


substrate_name: Cloxacillin

column_label: Table 2. Kinetic parameters and relative kcat/Km values of purified beta-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1.; row OXA-55 / Cloxacillin; columns OXA-55 kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1); cells kcat 0.5, Km 190, kcat/Km 3.

normalized_value_unit_evidence: kcat normalized_value=0.5 normalized_unit=s^-1; Km normalized_value=0.19 normalized_unit=mM; kcat/Km normalized_value=3 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row OXA-55 / Cloxacillin: kcat 0.5 s^-1; Km 190 uM; kcat/Km 3 mM^-1 s^-1; relative kcat/Km 1.5.

row_label: OXA-55 / Cloxacillin

substrate: Cloxacillin


organism: Shewanella frigidimarina

substrate_name: H2O; Amoxicillin

substrate: H2O; Amoxicillin


organism: Shewanella livingstonensis

substrate_name: Amoxicillin; H2O

substrate: Amoxicillin; H2O


organism: Staphylococcus aureus

substrate_name: Cefuroxime

assay_conditions_summary: pH 6; 310.15 K; buffer pH 6

column_label: Same-row type A Cefuroxime cells match exported kcat 0.009 s^-1, Km 0.378 mM, and kcat/Km 0.023809523809523808 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 reports Cefuroxime Km 378 uM for type A; Table 2 reports Cefuroxime kcat 0.009 s^-1 for type A; Table 4 identifies Cefuroxime REH for type A.

row_label: Cefuroxime; beta-lactamase type A (PC1)

table_label: Tables 1, 2, and 4 kinetic constants/REH, PDF pp. 2-3

substrate: Cefuroxime


substrate_name: cefazolin

substrate: cefazolin


substrate_name: Cephapirin

column_label: The same-type paper cells do not exactly equal the exported kcat/Km value.

raw_value_unit_evidence: Table 2 reports Cephapirin kcat 1.82 s^-1 for type B; Table 1 reports Cephapirin Km 79.5 uM for type B.

row_label: Cephapirin; beta-lactamase type B (22260)

substrate: Cephapirin


substrate_name: Meropenem

substrate: Meropenem


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y228F


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant I164A


substrate_name: Cephalothin

substrate: Cephalothin


substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: Cephaloridine

column_label: The same-type paper cells do not exactly equal the exported Km and kcat/Km values under the strict equality rule.

raw_value_unit_evidence: Table 2 reports Cephaloridine kcat 6.65 s^-1 for type B; Table 1 reports Cephaloridine Km 19.4 uM for type B.

row_label: Cephaloridine; beta-lactamase type B (22260)

substrate: Cephaloridine


substrate_name: Cefamandole

column_label: Same-row type B Cefamandole cells match exported kcat 0.357 s^-1, Km 0.006 mM, and kcat/Km 59.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 reports Cefamandole Km 6.0 uM for type B; Table 2 reports Cefamandole kcat 0.357 s^-1 for type B; Table 4 reports Cefamandole REH for type B.

row_label: Cefamandole; beta-lactamase type B (22260)

substrate: Cefamandole


substrate_name: H2O; Cephaloridine

substrate: H2O; Cephaloridine


column_label: The same-type paper cells do not exactly equal the exported Km and kcat/Km values.

raw_value_unit_evidence: Table 2 reports Cephalothin kcat 0.096 s^-1 for type B; Table 1 reports Cephalothin Km 6.2 uM for type B.

row_label: Cephalothin; beta-lactamase type B (22260)


substrate_name: Nitrocefin

substrate: Nitrocefin


substrate_name: H2O; Biapenem

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120N

substrate: H2O; Biapenem


substrate_name: Cefaclor

substrate: Cefaclor


substrate_name: Imipenem

substrate: Imipenem


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: biapenem

substrate: biapenem


substrate_name: Nitrocefin; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y228A

substrate: Nitrocefin; H2O


substrate_name: H2O; Nitrocefin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N233D

substrate: H2O; Nitrocefin


substrate_name: Ampicillin

substrate: Ampicillin


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant S224K


enzyme_display_name: glucan 1,4-alpha-glucosidase

organism: Bacteroides thetaiotaomicron

substrate_name: H2O; p-Nitrophenyl-alpha-D-glucoside

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E532A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucan 1,4-alpha-glucosidase(Enzyme) mutant E532A His-tagged

enzyme: glucan 1,4-alpha-glucosidase

substrate: H2O; p-Nitrophenyl-alpha-D-glucoside


substrate_name: Maltohexaose

substrate: Maltohexaose


substrate_name: maltoheptaose

substrate: maltoheptaose


substrate_name: Maltotriose

substrate: Maltotriose


substrate_name: Amylose

substrate: Amylose


substrate_name: Nigerose

substrate: Nigerose


substrate_name: Maltose

substrate: Maltose


substrate_name: Panose

substrate: Panose


substrate_name: maltotetraose

assay_conditions_summary: pH 6.5; 310.15 K; buffer 40 mM sodium acetate

column_label: Table 4 row Maltotetraose lists Km 0.64 +/- 0.07 mM, kcat 321 +/- 15 s^-1, and kcat/Km 504 s^-1 mM^-1.

normalized_value_unit_evidence: Km normalized=0.64 mM; kcat normalized=321 s^-1; kcat/Km normalized=501.5625 s^-1 mM^-1 from same-row kcat/Km quotient

row_label: Maltotetraose

table_label: Table 4. Kinetic constants for hydrolysis of various substrates by SusB

substrate: maltotetraose


substrate_name: Isomaltose

column_label: Table 4 row Isomaltose (alpha-1,6) lists Km 6.34 +/- 0.35 mM, kcat 105 +/- 4.6 s^-1, and kcat/Km 16.6 s^-1 mM^-1.

normalized_value_unit_evidence: Km normalized=6.34 mM; kcat normalized=105 s^-1; kcat/Km normalized=16.561514195583598 s^-1 mM^-1 from same-row kcat/Km quotient

row_label: Isomaltose (alpha-1,6)

substrate: Isomaltose


substrate_name: p-Nitrophenyl-alpha-D-glucoside

substrate: p-Nitrophenyl-alpha-D-glucoside


substrate_name: Kojibiose

column_label: Table 4 row Kojibiose (alpha-1,2) lists Km 2.39 +/- 0.21 mM, kcat 141 +/- 7.6 s^-1, and kcat/Km 58.9 s^-1 mM^-1.

normalized_value_unit_evidence: Km normalized=2.39 mM; kcat normalized=141 s^-1; kcat/Km normalized=58.99581589958159 s^-1 mM^-1 from same-row kcat/Km quotient

row_label: Kojibiose (alpha-1,2)

substrate: Kojibiose


substrate_name: maltopentaose

column_label: Table 4 row Maltopentaose lists Km 1.29 +/- 0.07 mM, kcat 434 +/- 4.9 s^-1, and kcat/Km 337 s^-1 mM^-1.

normalized_value_unit_evidence: Km normalized=1.29 mM; kcat normalized=434 s^-1; kcat/Km normalized=336.4341085271318 s^-1 mM^-1 from same-row kcat/Km quotient

row_label: Maltopentaose

substrate: maltopentaose


organism: Caulobacter vibrioides

substrate_name: maltohexaose

column_label: Table 2 row Maltohexaose; columns kcat (s^-1), Km (mM), kcat/Km (s^-1 mM^-1).

row_label: Maltohexaose

table_label: Table 2

substrate: maltohexaose


column_label: Table 2 row Maltopentaose; columns kcat (s^-1), Km (mM), kcat/Km (s^-1 mM^-1).


substrate_name: maltose

column_label: Table 2 row Maltose; columns kcat (s^-1), Km (mM), kcat/Km (s^-1 mM^-1).

row_label: Maltose

substrate: maltose


organism: Clostridium sp.


substrate_name: Maltopentaose; H2O

proof_lines: SABIO-RK modifier species: glucan 1,4-alpha-glucosidase(Enzyme) mutant W433F

substrate: Maltopentaose; H2O


substrate_name: H2O; Maltotriose

proof_lines: SABIO-RK modifier species: glucan 1,4-alpha-glucosidase(Enzyme) mutant E632Q

substrate: H2O; Maltotriose


organism: Aspergillus awamori


organism: Athelia rolfsii

substrate_name: H2O; Maltose

substrate: H2O; Maltose


substrate_name: H2O; p-Nitrophenyl-alpha-D-glucoside

proof_lines: SABIO-RK modifier species: glucan 1,4-alpha-glucosidase(Enzyme) mutant E194A His-tagged

substrate: H2O; p-Nitrophenyl-alpha-D-glucoside


proof_lines: SABIO-RK modifier species: glucan 1,4-alpha-glucosidase(Enzyme) mutant E439A His-tagged


substrate_name: p-Nitrophenyl-alpha-D-glucoside; H2O

substrate: p-Nitrophenyl-alpha-D-glucoside; H2O


proof_lines: SABIO-RK modifier species: glucan 1,4-alpha-glucosidase(Enzyme) mutant E526A His-tagged


substrate_name: maltotriose

column_label: Table 2 row Maltotriose; columns kcat (s^-1), Km (mM), kcat/Km (s^-1 mM^-1).

row_label: Maltotriose

substrate: maltotriose


column_label: Table 2 row Maltotetraose; columns kcat (s^-1), Km (mM), kcat/Km (s^-1 mM^-1).


substrate_name: maltoheptaose

column_label: Table 2 row Maltoheptaose; columns kcat (s^-1), Km (mM), kcat/Km (s^-1 mM^-1).

row_label: Maltoheptaose

substrate: maltoheptaose


column_label: Table I. Kinetic parameters for wild-type and mutant CGAs with malto-oligosaccharides; row Maltose; column group Wild-type; raw cells: Km 2.46 +/- 0.30 mM | kcat 6.92 +/- 0.32 s^-1; kcat/Km computed from matched row cells 6.92/2.46 = 2.813008130081301 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=6.92 normalized_unit=s^-1; Km normalized_value=2.46 normalized_unit=mM; kcat/Km normalized_value=2.813008130081301 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=2.46 +/- 0.30 raw_unit=mM; kcat raw_value=6.92 +/- 0.32 raw_unit=s^-1; kcat/Km computed_from=6.92/2.46 raw_unit=s^-1*mM^-1

row_label: Maltose / Wild-type


column_label: Table I. Kinetic parameters for wild-type and mutant CGAs with malto-oligosaccharides; row maltopentaose; column group Wild-type; raw cells: Km 0.21 +/- 0.02 mM | kcat 59.24 +/- 1.66 s^-1; kcat/Km computed from matched row cells 59.24/0.21 = 282.09523809523813 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=59.24 normalized_unit=s^-1; Km normalized_value=0.21 normalized_unit=mM; kcat/Km normalized_value=282.09523809523813 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.21 +/- 0.02 raw_unit=mM; kcat raw_value=59.24 +/- 1.66 raw_unit=s^-1; kcat/Km computed_from=59.24/0.21 raw_unit=s^-1*mM^-1

row_label: maltopentaose / Wild-type


substrate_name: Maltohexaose

substrate: Maltohexaose


substrate_name: biapenem

substrate: biapenem


substrate_name: Imipenem

substrate: Imipenem


substrate_name: Nitrocefin

substrate: Nitrocefin


substrate_name: Cephalothin

substrate: Cephalothin


substrate_name: Meropenem

substrate: Meropenem


substrate_name: H2O; Biapenem

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120C

substrate: H2O; Biapenem


substrate_name: cefoxitin

substrate: cefoxitin


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120S


substrate_name: Cefaclor

substrate: Cefaclor


substrate_name: Maltotriose

substrate: Maltotriose


substrate_name: Maltopentaose; H2O

proof_lines: SABIO-RK modifier species: glucan 1,4-alpha-glucosidase(Enzyme) mutant W321F

substrate: Maltopentaose; H2O


substrate_name: maltotetraose

substrate: maltotetraose


substrate_name: maltopentaose

substrate: maltopentaose


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: H2O; Nitrocefin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant W204F

substrate: H2O; Nitrocefin


substrate_name: Nitrocefin; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant W39F/ D160W

substrate: Nitrocefin; H2O


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W337F with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

column_label: Table I. Kinetic parameters for wild-type and mutant CGAs with malto-oligosaccharides; row maltopentaose; column group W337F; raw cells: Km 0.09 +/- 0.001 mM | kcat 0.052 +/- 0.0002 s^-1; kcat/Km computed from matched row cells 0.052/0.09 = 0.5777777777777777 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.052 normalized_unit=s^-1; Km normalized_value=0.09 normalized_unit=mM; kcat/Km normalized_value=0.5777777777777777 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.09 +/- 0.001 raw_unit=mM; kcat raw_value=0.052 +/- 0.0002 raw_unit=s^-1; kcat/Km computed_from=0.052/0.09 raw_unit=s^-1*mM^-1

row_label: maltopentaose / W337F


sequence_variant_note: Mutation signature W569F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -14, so it is treated as a source-provided variant sequence.


substrate_name: Maltose

substrate: Maltose


substrate_name: maltoheptaose

column_label: Table I. Kinetic parameters for wild-type and mutant CGAs with malto-oligosaccharides; row maltoheptaose; column group Wild-type; raw cells: Km 0.24 +/- 0.01 mM | kcat 60.52 +/- 1.34 s^-1; kcat/Km computed from matched row cells 60.52/0.24 = 252.16666666666669 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=60.52 normalized_unit=s^-1; Km normalized_value=0.24 normalized_unit=mM; kcat/Km normalized_value=252.16666666666669 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.24 +/- 0.01 raw_unit=mM; kcat raw_value=60.52 +/- 1.34 raw_unit=s^-1; kcat/Km computed_from=60.52/0.24 raw_unit=s^-1*mM^-1

row_label: maltoheptaose / Wild-type

substrate: maltoheptaose


column_label: Table I. Kinetic parameters for wild-type and mutant CGAs with malto-oligosaccharides; row Maltotriose; column group W337F; raw cells: Km 0.18 +/- 0.01 mM | kcat 0.032 +/- 0.001 s^-1; kcat/Km computed from matched row cells 0.032/0.18 = 0.17777777777777778 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.032 normalized_unit=s^-1; Km normalized_value=0.18 normalized_unit=mM; kcat/Km normalized_value=0.17777777777777778 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.18 +/- 0.01 raw_unit=mM; kcat raw_value=0.032 +/- 0.001 raw_unit=s^-1; kcat/Km computed_from=0.032/0.18 raw_unit=s^-1*mM^-1

row_label: Maltotriose / W337F


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +8, so it is treated as a source-provided variant sequence.


column_label: Table I. Kinetic parameters for wild-type and mutant CGAs with malto-oligosaccharides; row maltotetraose; column group Wild-type; raw cells: Km 0.27 +/- 0.02 mM | kcat 59.47 +/- 1.64 s^-1; kcat/Km computed from matched row cells 59.47/0.27 = 220.25925925925924 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=59.47 normalized_unit=s^-1; Km normalized_value=0.27 normalized_unit=mM; kcat/Km normalized_value=220.25925925925924 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.27 +/- 0.02 raw_unit=mM; kcat raw_value=59.47 +/- 1.64 raw_unit=s^-1; kcat/Km computed_from=59.47/0.27 raw_unit=s^-1*mM^-1

row_label: maltotetraose / Wild-type


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W569F with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.

column_label: Table I. Kinetic parameters for wild-type and mutant CGAs with malto-oligosaccharides; row maltopentaose; column group W569F; raw cells: Km 0.24 +/- 0.03 mM | kcat 60.17 +/- 2.55 s^-1; kcat/Km computed from matched row cells 60.17/0.24 = 250.70833333333334 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=60.17 normalized_unit=s^-1; Km normalized_value=0.24 normalized_unit=mM; kcat/Km normalized_value=250.70833333333334 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.24 +/- 0.03 raw_unit=mM; kcat raw_value=60.17 +/- 2.55 raw_unit=s^-1; kcat/Km computed_from=60.17/0.24 raw_unit=s^-1*mM^-1

row_label: maltopentaose / W569F


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P29761 and applied mutation signature W337F with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.

column_label: Table I. Kinetic parameters for wild-type and mutant CGAs with malto-oligosaccharides; row maltotetraose; column group W337F; raw cells: Km 0.13 +/- 0.004 mM | kcat 0.052 +/- 0.001 s^-1; kcat/Km computed from matched row cells 0.052/0.13 = 0.39999999999999997 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.052 normalized_unit=s^-1; Km normalized_value=0.13 normalized_unit=mM; kcat/Km normalized_value=0.39999999999999997 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.13 +/- 0.004 raw_unit=mM; kcat raw_value=0.052 +/- 0.001 raw_unit=s^-1; kcat/Km computed_from=0.052/0.13 raw_unit=s^-1*mM^-1

row_label: maltotetraose / W337F


column_label: Table I. Kinetic parameters for wild-type and mutant CGAs with malto-oligosaccharides; row maltoheptaose; column group W337F; raw cells: Km 0.04 +/- 0.003 mM | kcat 0.044 +/- 0.001 s^-1; kcat/Km computed from matched row cells 0.044/0.04 = 1.0999999999999999 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.044 normalized_unit=s^-1; Km normalized_value=0.04 normalized_unit=mM; kcat/Km normalized_value=1.0999999999999999 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.04 +/- 0.003 raw_unit=mM; kcat raw_value=0.044 +/- 0.001 raw_unit=s^-1; kcat/Km computed_from=0.044/0.04 raw_unit=s^-1*mM^-1

row_label: maltoheptaose / W337F


substrate_name: H2O; Maltopentaose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W337F with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucan 1,4-alpha-glucosidase(Enzyme) mutant W337F

substrate: H2O; Maltopentaose


substrate_name: Maltohexaose

column_label: Table I. Kinetic parameters for wild-type and mutant CGAs with malto-oligosaccharides; row Maltohexaose; column group Wild-type; raw cells: Km 0.18 +/- 0.02 mM | kcat 53.98 +/- 1.84 s^-1; kcat/Km computed from matched row cells 53.98/0.18 = 299.88888888888886 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=53.98 normalized_unit=s^-1; Km normalized_value=0.18 normalized_unit=mM; kcat/Km normalized_value=299.88888888888886 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.18 +/- 0.02 raw_unit=mM; kcat raw_value=53.98 +/- 1.84 raw_unit=s^-1; kcat/Km computed_from=53.98/0.18 raw_unit=s^-1*mM^-1

row_label: Maltohexaose / Wild-type

substrate: Maltohexaose


proof_lines: SABIO-RK modifier species: glucan 1,4-alpha-glucosidase(Enzyme) mutant W569F


column_label: Table I. Kinetic parameters for wild-type and mutant CGAs with malto-oligosaccharides; row Maltose; column group W337F; raw cells: Km 0.50 +/- 0.10 mM | kcat 0.006 +/- 0.0003 s^-1; kcat/Km computed from matched row cells 0.006/0.5 = 0.012 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.006 normalized_unit=s^-1; Km normalized_value=0.5 normalized_unit=mM; kcat/Km normalized_value=0.012 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.50 +/- 0.10 raw_unit=mM; kcat raw_value=0.006 +/- 0.0003 raw_unit=s^-1; kcat/Km computed_from=0.006/0.5 raw_unit=s^-1*mM^-1

row_label: Maltose / W337F


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant W53F


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant W39F


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant W269F


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant W206F


substrate_name: Nitrocefin

substrate: Nitrocefin


substrate_name: Cephalothin

substrate: Cephalothin


substrate_name: Meropenem

substrate: Meropenem


substrate_name: Cephradine

substrate: Cephradine


enzyme_display_name: unspecific monooxygenase

organism: Bacillus subtilis

substrate_name: Hexacyanoferrate(III)

enzyme: unspecific monooxygenase

substrate: Hexacyanoferrate(III)


substrate_name: Myristic acid

smiles: CCCCCCCCCCCCCC(=O)O

substrate: Myristic acid


substrate_name: NADPH

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADPH

substrate: NADPH


substrate_name: 15-Methyl-palmitic acid

smiles: CC(C)CCCCCCCCCCCCCC(=O)O

substrate: 15-Methyl-palmitic acid


substrate_name: Stearate

smiles: CCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: Stearate


substrate_name: Phytanate

smiles: CC(C)CCCC(C)CCCC(C)CCCC(C)CC(=O)O

assay_conditions_summary: pH 7.4; 303.15 K; buffer B; cofactor NADPH

raw_value_unit_evidence: kcat raw_value=794 +/- 74.8 raw_unit=min^-1; KM raw_value=28.7 +/- 6.0 raw_unit=uM; kcat/KM derived_from=Table 2 kcat and KM cells raw_unit=min^-1 per uM

row_label: CYP102A3 / phytanic acid

table_label: Table 2. Kinetic and binding parameters for the interaction of CYP102A2 and CYP102A3 with fatty acids, pyridine nucleotides, and electron acceptors

substrate: Phytanate


substrate_name: NADPH; Dodecanoate; H+; O2

assay_conditions_summary: cofactor NADPH

substrate: NADPH; Dodecanoate; H+; O2


raw_value_unit_evidence: kcat raw_value=3845 +/- 415 raw_unit=min^-1; KM raw_value=68.3 +/- 15.9 raw_unit=uM; kcat/KM derived_from=Table 2 kcat and KM cells raw_unit=min^-1 per uM

row_label: CYP102A3 / 15-methylpalmitic acid


raw_value_unit_evidence: kcat raw_value=430 +/- 81.7 raw_unit=min^-1; KM raw_value=38.8 +/- 17.5 raw_unit=uM; kcat/KM derived_from=Table 2 kcat and KM cells raw_unit=min^-1 per uM

row_label: CYP102A2 / stearic acid


substrate_name: palmitate

smiles: CCCCCCCCCCCCCCCC(=O)O

raw_value_unit_evidence: kcat raw_value=676 +/- 112 raw_unit=min^-1; KM raw_value=337 +/- 67.6 raw_unit=uM; kcat/KM derived_from=Table 2 kcat and KM cells raw_unit=min^-1 per uM

row_label: CYP102A3 / palmitic acid

substrate: palmitate


organism: Canis familiaris


substrate_name: Cyclophosphamide

substrate: Cyclophosphamide


organism: Homo sapiens


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


substrate_name: O2; H+; NADPH; Benzo[a]pyrene-7,8-diol

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) wildtype allelic variant RAVN

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) wildtype allelic variant RAVS

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) wildtype allelic variant RALN

substrate: O2; H+; NADPH; Benzo[a]pyrene-7,8-diol


substrate_name: O2; Reduced flavoprotein; 1-(3-Trifluoromethylphenyl)piperazine


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

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant D348N


organism: Bacillus cereus

substrate_name: Palmitate; NADPH; O2; H+

substrate: Palmitate; NADPH; O2; H+


organism: Bacillus licheniformis

substrate_name: NADPH; O2; H+; Dodecanoate

substrate: NADPH; O2; H+; Dodecanoate


organism: Bacillus megaterium

substrate_name: O2; NADPH; H+; Linoleate

assay_conditions_summary: pH 7.4; cofactor NADPH

column_label: Table 2; row Linoleic acid (CYP102A1); column Turnover (umol/min/umol).

raw_value_unit_evidence: Table 2 Turnover: 4101 +/- 410 umol min^-1 umol P450^-1 (equivalent to min^-1).

row_label: Linoleic acid (CYP102A1)

substrate: O2; NADPH; H+; Linoleate


substrate_name: arachidonate

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

raw_value_unit_evidence: kcat raw_value=1690 +/- 200 raw_unit=min^-1; KM raw_value=79.0 +/- 15.9 raw_unit=uM; kcat/KM derived_from=Table 2 kcat and KM cells raw_unit=min^-1 per uM

row_label: CYP102A3 / arachidonic acid

substrate: arachidonate


raw_value_unit_evidence: kcat raw_value=11560 +/- 200 raw_unit=min^-1; KM raw_value=3.6 +/- 0.3 raw_unit=uM; kcat/KM derived_from=Table 2 kcat and KM cells raw_unit=min^-1 per uM

row_label: CYP102A2 / NADPH


column_label: Table 2 CYP102A2 row phytanic acid; columns kcat/kmax min^-1 and KM/KH uM; raw cells 5430 +/- 1810 and 150 +/- 37.6; normalized cells 90.5 s^-1 and 0.15 mM; kcat/KM calculated from normalized cells as 603.3333333333333333333333333333333333333 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=90.5 normalized_unit=s^-1; KM normalized_value=0.15 normalized_unit=mM; kcat/KM normalized_value=603.3333333333333333333333333333333333333 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=5430 +/- 1810 raw_unit=min^-1; KM raw_value=150 +/- 37.6 raw_unit=uM; kcat/KM derived_from=Table 2 kcat and KM cells raw_unit=min^-1 per uM

row_label: CYP102A2 / phytanic acid


substrate_name: NADH

assay_conditions_summary: pH 7.4; 303.15 K; buffer B; cofactor NADH

raw_value_unit_evidence: kcat raw_value=1850 +/- 100 raw_unit=min^-1; KM raw_value=17900 +/- 2050 raw_unit=uM; kcat/KM derived_from=Table 2 kcat and KM cells raw_unit=min^-1 per uM

row_label: CYP102A2 / NADH

substrate: NADH


substrate_name: dodecanoate

smiles: CCCCCCCCCCCC(=O)O

raw_value_unit_evidence: kcat raw_value=104 +/- 7.7 raw_unit=min^-1; KM raw_value=165 +/- 29.0 raw_unit=uM; kcat/KM derived_from=Table 2 kcat and KM cells raw_unit=min^-1 per uM

row_label: CYP102A3 / lauric acid

substrate: dodecanoate


substrate_name: NADPH; H+; Cyclophosphamide; O2

substrate: NADPH; H+; Cyclophosphamide; O2


organism: Gallus gallus

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

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


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

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


enzyme_display_name: Cytochrome P450 3A

substrate_name: O2; T-2 Toxin; NADPH

enzyme: Cytochrome P450 3A

substrate: O2; T-2 Toxin; NADPH


enzyme_display_name: Cytochrome P450 2F1

substrate_name: Skatole

enzyme: Cytochrome P450 2F1

substrate: Skatole


enzyme_display_name: Cytochrome P450 4F8

substrate_name: NADPH; O2; H+; 9,11-Epoxymethano-prostaglandin H2

enzyme: Cytochrome P450 4F8


enzyme_display_name: Cytochrome P450 4A11

substrate_name: O2; NADPH; H+; Retinoate

enzyme: Cytochrome P450 4A11

substrate: O2; NADPH; H+; Retinoate


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

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) mutant I386F


substrate_name: Phenacetin

substrate: Phenacetin


substrate_name: Estradiol-17beta; NADPH; H+; O2

sequence_variant_note: Resolved canonical sequence from uniprot_reviewed_accession:Q16678 and applied mutation signature R48G/A119S/L432V/A443G to reconstruct the assayed variant sequence.

column_label: Complete article PDF, Table 5, CYP1B1.7 row (R48G/A119S/L432V/A443G), apparent Km for 2-hydroxyestradiol and Vmax for 2-hydroxyestradiol columns.

raw_value_unit_evidence: Table 5: apparent Km 39.1 +/- 2.4 uM; Vmax 0.7 +/- 0.08 pmol 2-hydroxyestradiol/pmol P450/min.

table_label: PMID 11854439 Table 5. Kinetic parameters for E2 hydroxylation of polymorphic CYP1B1 variants

substrate: Estradiol-17beta; NADPH; H+; O2


substrate_name: O2; H+; NADPH; Estradiol-17beta

sequence_variant_note: Resolved canonical sequence from uniprot_reviewed_accession:Q16678 and applied mutation signature R48G/A119S to reconstruct the assayed variant sequence.

column_label: Complete article PDF, Table 5, CYP1B1.2 row (R48G/A119S), apparent Km for 2-hydroxyestradiol and Vmax for 2-hydroxyestradiol columns.

raw_value_unit_evidence: Table 5: apparent Km 7.7 +/- 0.1 uM; Vmax 0.5 +/- 0.10 pmol 2-hydroxyestradiol/pmol P450/min.

substrate: O2; H+; NADPH; Estradiol-17beta


substrate_name: Estradiol-17beta; NADPH; O2; H+

sequence_variant_note: Resolved canonical sequence from uniprot_reviewed_accession:Q16678 and applied mutation signature L432V to reconstruct the assayed variant sequence.

column_label: Complete article PDF, Table 5, CYP1B1.3 row (L432V), apparent Km for 2-hydroxyestradiol and Vmax for 2-hydroxyestradiol columns.

raw_value_unit_evidence: Table 5: apparent Km 8.7 +/- 2.4 uM; Vmax 0.65 +/- 0.10 pmol 2-hydroxyestradiol/pmol P450/min.

row_label: CYP1B1.3, L432V, 2-hydroxyestradiol

substrate: Estradiol-17beta; NADPH; O2; H+


substrate_name: H+; O2; NADPH; Estradiol-17beta

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R48G/A119S/L432V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: unspecific monooxygenase(Enzyme) wildtype allele CYP1B1.6 (R48G, A119S, L432V)

substrate: H+; O2; NADPH; Estradiol-17beta


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed_accession:Q16678 and applied mutation signature L432V/A443G to reconstruct the assayed variant sequence.

column_label: Complete article PDF, Table 5, L432V/A443G row, apparent Km for 2-hydroxyestradiol and Vmax for 2-hydroxyestradiol columns.

raw_value_unit_evidence: Table 5: apparent Km 9.7 +/- 1.7 uM; Vmax 0.5 +/- 0.10 pmol 2-hydroxyestradiol/pmol P450/min.

row_label: L432V/A443G, 2-hydroxyestradiol


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed_accession:Q16678 and applied mutation signature L432V/N453S to reconstruct the assayed variant sequence.

column_label: Complete article PDF, Table 5, L432V/N453S row, apparent Km for 2-hydroxyestradiol and Vmax for 2-hydroxyestradiol columns.

raw_value_unit_evidence: Table 5: apparent Km 7.5 +/- 0.5 uM; Vmax 0.3 +/- 0.05 pmol 2-hydroxyestradiol/pmol P450/min.

row_label: L432V/N453S, 2-hydroxyestradiol


substrate_name: Estradiol-17beta; H+; O2; NADPH

sequence_variant_note: Resolved canonical sequence from uniprot_reviewed_accession:Q16678 and applied mutation signature N453S to reconstruct the assayed variant sequence.

column_label: Complete article PDF, Table 5, CYP1B1.4 row (N453S), apparent Km for 2-hydroxyestradiol and Vmax for 2-hydroxyestradiol columns.

raw_value_unit_evidence: Table 5: apparent Km 9.4 +/- 1.8 uM; Vmax 0.55 +/- 0.06 pmol 2-hydroxyestradiol/pmol P450/min.

row_label: CYP1B1.4, N453S, 2-hydroxyestradiol

substrate: Estradiol-17beta; H+; O2; NADPH


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

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

column_label: exact cells: substrate block MeIQx, 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 0.09 s^-1 from min^-1 / 60; paper KM normalized to 0.027 mM from uM / 1000; paper kcat/KM normalized/row-consistent as 3.333333333333333 s^-1*mM^-1. Expected row values: kcat 0.09 s^(-1); KM 0.027 mM; kcat/KM 3.333333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Kinetic data for P450 1A2 variants; substrate block MeIQx; row wild-type; kcat 5.4 +/- 0.4 pmol/min/pmol P450; KM 27 +/- 6 uM; kcat/KM 0.20 min^-1*uM^-1; fold 1.

row_label: MeIQx / wild-type


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I386F to reconstruct the assayed variant sequence.

column_label: exact cells: substrate block Phenacetin, row I386F, 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 0.043 s^-1 from min^-1 / 60; paper KM normalized to 0.32 mM from uM / 1000; paper kcat/KM normalized/row-consistent as 0.134375 s^-1*mM^-1. Expected row values: kcat 0.043 s^(-1); KM 0.32 mM; kcat/KM 0.134375 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Kinetic data for P450 1A2 variants; substrate block Phenacetin; row I386F; kcat 2.6 +/- 1.0 pmol/min/pmol P450; KM 320 +/- 161 uM; kcat/KM 0.008 min^-1*uM^-1; fold 0.1.

row_label: Phenacetin / I386F


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 PhIP, 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 0.483 s^-1 from min^-1 / 60; paper KM normalized to 0.062 mM from uM / 1000; paper kcat/KM normalized/row-consistent as 7.790322580645161 s^-1*mM^-1. Expected row values: kcat 0.483 s^(-1); KM 0.062 mM; kcat/KM 7.790322580645161 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Kinetic data for P450 1A2 variants; substrate block PhIP; row D348N; kcat 29 +/- 2 pmol/min/pmol P450; KM 62 +/- 12 uM; kcat/KM 0.46 min^-1*uM^-1; fold 3.0.

row_label: PhIP / D348N


column_label: exact cells: substrate block IQ, 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 0.097 s^-1 from min^-1 / 60; paper KM normalized to 0.021 mM from uM / 1000; paper kcat/KM normalized/row-consistent as 4.619047619047619 s^-1*mM^-1. Expected row values: kcat 0.097 s^(-1); KM 0.021 mM; kcat/KM 4.619047619047619 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Kinetic data for P450 1A2 variants; substrate block IQ; row wild-type; kcat 5.8 +/- 0.1 pmol/min/pmol P450; KM 21 +/- 2 uM; kcat/KM 0.27 min^-1*uM^-1; fold 1.

row_label: IQ / wild-type


column_label: exact cells: substrate block MeIQ, 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 0.05 s^-1 from min^-1 / 60; paper KM normalized to 0.026 mM from uM / 1000; paper kcat/KM normalized/row-consistent as 1.9230769230769234 s^-1*mM^-1. Expected row values: kcat 0.05 s^(-1); KM 0.026 mM; kcat/KM 1.9230769230769234 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Kinetic data for P450 1A2 variants; substrate block MeIQ; row wild-type; kcat 3.0 +/- 0.2 pmol/min/pmol P450; KM 26 +/- 7 uM; kcat/KM 0.12 min^-1*uM^-1; fold 1.

row_label: MeIQ / wild-type