organism: Sus scrofa

substrate_name: phenethyl isothiocyanate

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

substrate: phenethyl isothiocyanate


enzyme_display_name: glutathione transferase

source_db: oed

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

enzyme: glutathione transferase

source: oed


smiles: CCCCCC/C=C/C=O


organism: Zea mays

substrate_name: RX; Reduced glutathione

kcat_display: Not reported

km_display: Not reported

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

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

mutation_type: substitution

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant Asn49Ala

substrate: RX; Reduced glutathione


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant Phe35Leu


substrate_name: Reduced glutathione; RX

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant Ile118Phe

substrate: Reduced glutathione; RX


organism: Saccharomyces cerevisiae

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


organism: Salix babylonica

substrate_name: glutathione

verification_status: unverified

substrate: glutathione

status: unverified


organism: Schistosoma japonicum


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant Ser67Ala


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant Lys41Ala


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant Trp12Leu


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant Gln53Ala


enzyme_display_name: beta-lactamase

organism: Stenotrophomonas maltophilia

substrate_name: Nitrocefin

enzyme: beta-lactamase

substrate: Nitrocefin


substrate_name: Ampicillin; H2O

substrate: Ampicillin; H2O


substrate_name: cephaloridin

substrate: cephaloridin


substrate_name: Oxacillin

substrate: Oxacillin


organism: Apis mellifera macedonica

source_db: brenda

source: brenda


substrate_name: Penicillin G

verification_status: verified

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

row_label: Penicillin G

table_label: Table 3

data_origin: experimental

substrate: Penicillin G

status: verified


substrate_name: cephalexin

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

row_label: cephalexin

substrate: cephalexin


substrate_name: Ampicillin

verification_status: corrected

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

row_label: Ampicillin

substrate: Ampicillin

status: corrected


substrate_name: 6-beta-Iodopenicillanic acid

column_label: Table 3 scanned page 154; enzyme block Pseudomonas maltophilia ULA-511 L-1 enzyme; row label 6-beta-Iodopenicillanic acid; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); assay: 50 mM sodium cacodylate buffer, pH 7.0, containing 0.1 mM ZnCl2; P. maltophilia experiments at 35 C; hydrolysis followed by beta-lactam ring absorbance change; Km/kcat from Hanes linearization; low Km by nitrocefin competition

row_label: 6-beta-Iodopenicillanic acid

substrate: 6-beta-Iodopenicillanic acid


substrate_name: clavulanic acid

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

column_label: Table 1; row clavulanic acid / Recombinant L1; column Km (uM) raw value 22; column kcat (s^-1) raw value 11; column kcat/Km (s^-1 uM^-1) raw value 0.50

normalized_value_unit_evidence: kcat normalized_value=11 normalized_unit=s^-1; Km normalized_value=0.022 normalized_unit=mM; kcat/Km normalized_value=500 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=11 raw_unit=s^-1; Km raw_value=22 raw_unit=uM; kcat/Km raw_value=0.50 raw_unit=s^-1*uM^-1

row_label: clavulanic acid / Recombinant L1

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

substrate: clavulanic acid


substrate_name: Ceftizoxime

column_label: Table 1; row Ceftizoxime / Recombinant L1; column Km (uM) raw value 7.9; column kcat (s^-1) raw value 2.7; column kcat/Km (s^-1 uM^-1) raw value 0.34

normalized_value_unit_evidence: kcat normalized_value=2.7 normalized_unit=s^-1; Km normalized_value=0.0079 normalized_unit=mM; kcat/Km normalized_value=340 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=2.7 raw_unit=s^-1; Km raw_value=7.9 raw_unit=uM; kcat/Km raw_value=0.34 raw_unit=s^-1*uM^-1

row_label: Ceftizoxime / Recombinant L1

substrate: Ceftizoxime


organism: Treponema pallidum

substrate_name: Penicillin G; H2O

substrate: Penicillin G; H2O


substrate_name: Cloxacillin

kcat_over_km_origin: calculated

substrate: Cloxacillin


organism: Serratia marcescens

substrate_name: Phosphonomycin; Reduced glutathione

substrate: Phosphonomycin; Reduced glutathione


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H7A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant H7A


substrate_name: Phosphonomycin

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H67Q to reconstruct the assayed variant sequence.

substrate: Phosphonomycin


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H7Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant H7Q


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E113Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E113A to reconstruct the assayed variant sequence.


substrate_name: Monobromobimane; Reduced glutathione

substrate: Monobromobimane; Reduced glutathione


organism: Aedes aegypti

mutation_signature: Aedes aegypti EC 2.5.1.18 row remains manual_review_required because the preserved evidence stops at legacy GSTE isozyme labels and does not expose an accession

mutation_type: truncation

proof_lines: recombinant His6-tagged isozyme GSTE8-8, pH and temperature not specified in the publication

proof_lines: recombinant His6-tagged isozyme GSTE7-7, pH and temperature not specified in the publication

proof_lines: recombinant His6-tagged isozyme GSTE1-1, pH and temperature not specified in the publication


organism: Homo sapiens

assay_conditions_summary: pH 7.4; 310.15 K; buffer 250 mM Tris-HCl

proof_lines: pH 7.4, 37°C, recombinant wild-type isozyme GST-T1-1

proof_lines: pH 8.0, 30°C, recombinant wild-type enzyme

proof_lines: wild type enzyme I10C, at 30°C in 250 mM Tris-HCl buffer, pH 7.2


organism: Bulinus truncatus

proof_lines:
pH 8.5, 25°C, isozyme GST2
pH 6.0, 25°C, isozyme GST2
pH 8.5, 25°C, isozyme GST3


organism: Bos taurus

proof_lines:
isozyme I
isozyme II
isozymes I and II


substrate_name: carbenicillin

row_label: Carbenicillin

table_label: Table I. Kinetic parameters for turnover of beta-lactam antibiotics by Tp47

substrate: carbenicillin


enzyme_display_name: glucan 1,4-alpha-glucosidase

organism: Aspergillus coreanus

substrate_name: starch

proof_lines:
pH 4.0, 60°C, isozyme GA-I
pH 4.0, 65°C, isozyme GA-II

enzyme: glucan 1,4-alpha-glucosidase

substrate: starch


organism: Rattus norvegicus

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

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines:
pH 8.0, 30°C, recombinant enzyme
isoenzyme 4-4, cofactor: glutathione
isoenzyme 3-3, cofactor: glutathione


proof_lines: pH 7.4, 37°C, glutathione transferase Zeta 1c-1c


organism: Monascus purpureus

substrate_name: soluble starch

proof_lines:
pH 5.0, 37°C, isozyme GA-II
pH 5.0, 37°C, isozyme GA-I

substrate: soluble starch


enzyme_display_name: unspecific monooxygenase

substrate_name: 17beta-estradiol (2-hydroxylation)

source_db: uniprot

enzyme: unspecific monooxygenase

substrate: 17beta-estradiol (2-hydroxylation)

source: uniprot


sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.


substrate_name: estrone (16-alpha hydroxylation)

substrate: estrone (16-alpha hydroxylation)


organism: Mus musculus


substrate_name: phenacetin

substrate: phenacetin


substrate_name: all-trans-retinoate (4-hydroxylation)

substrate: all-trans-retinoate (4-hydroxylation)


organism: Drosophila melanogaster

substrate_name: glutathione

substrate: glutathione


organism: Escherichia coli (strain K12)

substrate_name: bromoacetate

substrate: bromoacetate


substrate_name: glutathione for the glutathione-conjugating activity


organism: Caenorhabditis elegans


enzyme_display_name: pyruvate kinase

organism: Spinacia oleracea

substrate_name: ADP; Phosphoenolpyruvate

proof_lines:
pH 7.1, 25°C
isozyme PKII, pH 7.1, 25°C
isozyme PKI, pH 7.1, 25°C

enzyme: pyruvate kinase

substrate: ADP; Phosphoenolpyruvate


organism: Arabidopsis thaliana

substrate_name: DHA (at pH 6.5 and 30 degrees Celsius)

substrate: DHA (at pH 6.5 and 30 degrees Celsius)


organism: Asaphis dichotoma

sequence: PSYKLHYFDLRAAGE

wild_type_sequence: PSYKLHYFDLRAAGE


organism: Brucella anthropi


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

substrate_name: ADP

assay_conditions_summary: cofactor ADP

substrate: ADP


organism: Chryseobacterium indologenes

substrate_name: benzylpenicillin (at pH 7.0 and 30 degrees Celsius)


organism: Escherichia coli

substrate_name: ampicillin

substrate: ampicillin


organism: Homo sapiens

substrate_name: palmitoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: palmitoyl-CoA


substrate_name: imipenem

substrate: imipenem


substrate_name: leukotriene D4

substrate: leukotriene D4


organism: Nocardia asteroides

substrate_name: benzylpenicillin

substrate: benzylpenicillin


organism: Nocardia farcinica (strain IFM 10152)


organism: Pseudomonas aeruginosa

substrate_name: amoxicillin (at pH 7.0 and 37 degrees Celsius)

assay_conditions_summary: pH 7


substrate_name: ampicillin (at 37 degrees Celsius and pH 7.5)


organism: Pseudomonas fluorescens

substrate_name: nitrocefin

substrate: nitrocefin


substrate_name: leukotriene B4

proof_lines: The omega-hydroxylation of VLCFAs follows dual-enzyme Michaelis-Menten kinetics, suggesting simultaneous binding of two substrate molecules. The high affinity Michaelis-Menten constants are shown.

substrate: leukotriene B4


substrate_name: all-trans-retinol

proof_lines: kcat is 0.04 min(-1) for retinol, 0.08 min(-1) for retinal, 1.24 min(-1) for 7,12-dimethyltetraphene, 0.13 min(-1) for arachidonic acid.

substrate: all-trans-retinol


organism: Priestia megaterium (strain ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19)

substrate_name: lauric acid at pH 7.4 at room temperature

proof_lines: kcat is 84.1 sec(-1) for lauric acid (PubMed:16403573). kcat is 1480 min(-1) for palmitic acid. kcat is 1880 min(-1) for N-palmitoylglycine. kcat is 1690 min(-1) for N-palmitoyl-L-methionine. kcat is 610 min(-1) for N-palmitoyl-L-glutamine.


substrate_name: glutathione (in oxidative conditions)

proof_lines: kcat is 0.5 sec(-1) with glutathione as substrate (in oxidative conditions) (PubMed:29732642). kcat is 0.85 sec(-1) with glutathione as substrate (in reductive conditions) (PubMed:29732642). kcat is 0.72 sec(-1) with 1-chloro-2,4-dinitroben

substrate: glutathione (in oxidative conditions)


substrate_name: glutathione

proof_lines: kcat is 0.11 sec(-1) for the GSH transferase reaction with CDNB as substrate.


proof_lines: kcat is 9 sec(-1) for the GSH transferase reaction with CDNB as substrate.


organism: Bacillus subtilis (strain 168)

substrate_name: lauric acid

proof_lines: kcat is 104 min(-1) for lauric acid hydroxylation. kcat is 5556 min(-1) for myristic acid hydroxylation. kcat is 676 min(-1) for palmitic acid hydroxylation. kcat is 374 min(-1) for stearic acid hydroxylation. kcat is 794 min(-1) for phytan

substrate: lauric acid


substrate_name: stearic acid

proof_lines: kcat is 430 min(-1) for stearic acid hydroxylation. kcat is 5430 min(-1) for phytanic acid hydroxylation. kcat is 6105 min(-1) for 15-methylpalmitic acid hydroxylation. kcat is 11400 min(-1) for the reduction of cytochrome c. kcat is 38150

substrate: stearic acid


substrate_name: 17-beta-estradiol (2-hydroxylation)

proof_lines: kcat is 0.15 min(-1) for retinol, 0.77 min(-1) for retinal, 2.86 min(-1) for 7,12-dimethyltetraphene, 0.48 min(-1) for arachidonic acid.

substrate: 17-beta-estradiol (2-hydroxylation)


substrate_name: dodecanoic acid

proof_lines: kcat is 42 min(-1) with dodecanoic acid as substrate. kcat is 50 min(-1) with tetradecanoic acid as substrate. kcat is 10 min(-1) with hexadecanoic acid as substrate. kcat is 0.4 min(-1) with (9Z)-octadecenoic acid as substrate. kcat is 0.4

substrate: dodecanoic acid


substrate_name: docosanoate

proof_lines: kcat is 0.067 min(-1) with menaquinone-4 (MK-4) as substrate (PubMed:24138531). The omega-hydroxylation of VLCFAs follows dual-enzyme Michaelis-Menten kinetics, suggesting simultaneous binding of two substrate molecules. The high affinity M

substrate: docosanoate


substrate_name: hexadecanoic acid

proof_lines: kcat is 0.088 min(-1) with menaquinone-4 (MK-4) as substrate (PubMed:24138531). kcat is 1.8 min(-1) with hexadecanoic acid as substrate. kcat is 1.0 min(-1) with (9Z)-octadecenoic acid as substrate. kcat is 0.54 min(-1) with (5Z,8Z,11Z,14Z)

substrate: hexadecanoic acid


organism: Gallus gallus

substrate_name: Unknown

substrate: Unknown


proof_lines: kcat is 50 sec(-1) for prostaglandin H2 as substrate (PubMed:12672824). kcat is 75 sec(-1) for prostaglandin H2 as substrate (PubMed:12672824). kcat is 21 sec(-1) for glutathione as substrate (PubMed:12672824).

substrate: glutathione


assay_conditions_summary: pH 8

proof_lines: kcats are 102 sec(-1) and 27 sec(-1) for androst-5-ene-3,17-dione and pregn-5-ene-3,20-dione as substrates, respectively (at pH 8.0 and 30 degrees Celsius).


proof_lines: kcat is 0.6 sec(-1) for leukotriene A4 as substrate (PubMed:23409838). kcat is 14.3 sec(-1) for 1-chloro-2,4-dinitrobenzene as substrate (PubMed:23409838). kcat is 0.1 sec(-1) for 5-HPETE as substrate (PubMed:23409838).


substrate_name: prostaglandin A2 (at pH 7.0 and 37 degrees Celsius)

proof_lines: kcat is 29.3 sec(-1) for the isomerization of androst-5-ene-3,17-dione.


organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)


organism: Mus musculus


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: bromosulphophthalein

substrate: bromosulphophthalein


organism: Rattus norvegicus

substrate_name: glutathione for the prostaglandin D synthase activity


substrate_name: dichloroacetic acid

substrate: dichloroacetic acid


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Geobacillus stearothermophilus

substrate_name: PEP (in the presence of 0.1 mM ribose-5-phosphate)

proof_lines: kcat is 3.204 sec(-1) (in the presence of 0.1 mM ribose-5-phosphate).


organism: Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)


organism: Bacillus licheniformis

sequence: SSNKLTTSWG

wild_type_sequence: SSNKLTTSWG

proof_lines: Because of the indeterminate molecular weight of starch, an approximate KM value of 0.2178 mg/ml was determined.


organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)

substrate_name: maltose

proof_lines: kcat is 182 sec(-1) for maltose. kcat is 270 sec(-1) for maltotriose. kcat is 321 sec(-1) for maltotetraose. kcat is 434 sec(-1) for maltopentaose. kcat is 346 sec(-1) for maltohexaose. kcat is 381 sec(-1) for maltoheptaose. kcat is 321 sec

substrate: maltose


organism: Acinetobacter baumannii

substrate_name: benzylpenicillin (at pH 7.0 and 30 degrees Celsius)

proof_lines: kcat is 5.5 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:15616297). kcat is 106 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:26459904). kcat is 1 sec(-1) with


proof_lines: kcat is 460 sec(-1) for ampicillin (at pH 7.4 and 25 degrees Celsius, in the presence of 0.025 M NaHCO3) (PubMed:23877677). kcat is 580 sec(-1) for ampicillin (at pH 7.0, in the presence of 0.05 M NaHCO3) (PubMed:30530607). kcat is 0.49 sec


organism: Aeromonas hydrophila

substrate_name: cefuroxime

proof_lines: kcat is 1200 sec(-1) for lactamase activity with imipenem as substrate (PubMed:15588826, PubMed:19651913). kcat is 300 sec(-1) for lactamase activity with biapenem as substrate (PubMed:15588826). kcat is 210 sec(-1) for lactamase activity w

substrate: cefuroxime


organism: Bacteroides fragilis

substrate_name: nitrocefin (with zinc ions at pH 7 and 25 degrees Celsius)

proof_lines: kcat is 225.7 sec(-1) for lactamase activity with nitrocefin as substrate (with zinc ions at pH 7 and 25 degrees Celsius). kcat is 107.6 sec(-1) for lactamase activity with nitrocefin as substrate (with cobalt ions at pH 7 and 25 degrees Ce


organism: Citrobacter amalonaticus

substrate_name: benzylpenicillin

proof_lines: Value for ceftazidime was determined as Ki by substrate competition with benzylpenicillin.

substrate: benzylpenicillin


organism: Elizabethkingia meningoseptica

substrate_name: cefoxitin

proof_lines: kcat is 350 sec(-1) for lactamase activity with imipenem as substrate. kcat is 300 sec(-1) for lactamase activity with 6-beta-iodopenicillanate as substrate. kcat is 280 sec(-1) for lactamase activity with penicillin G as substrate. kcat is

substrate: cefoxitin


organism: Escherichia coli

substrate_name: cloxacillin (at pH 7.0 and 30 degrees Celsius)

proof_lines: kcat is 577 sec(-1) with oxacillin as substrate (in the presence of 0.02 M NaHCO3) (PubMed:20086146). kcat is 357 sec(-1) with ampicillin as substrate (in the presence of 0.02 M NaHCO3) (PubMed:20086146). kcat is 16 sec(-1) with cephaloridi


organism: Helicobacter pylori (strain ATCC 700392 / 26695)

substrate_name: ampicillin

proof_lines: kcat is 1.06 min(-1) with ampicillin as substrate. kcat is 0.74 min(-1) with benzylpenicillin as substrate. kcat is 0.55 min(-1) with amoxicillin as substrate. kcat is 0.30 min(-1) with cephaloridine as substrate. kcat is 0.28 min(-1) with

substrate: ampicillin


proof_lines: kcat is 0.76 min(-1) with ampicillin as substrate. kcat is 0.68 min(-1) with benzylpenicillin as substrate. kcat is 0.45 min(-1) with amoxicillin as substrate. kcat is 0.45 min(-1) with nitrocefine as substrate.


organism: Klebsiella aerogenes

substrate_name: benzylpenicillin (at 30 degrees Celsius and pH 7.0)

proof_lines: kcat is 3.06 sec(-1) with benzylpenicillin as substrate (at 30 degrees Celsius and pH 7.0) (PubMed:16677302). kcat is 5.0 sec(-1) with ceftazidime as substrate (at 30 degrees Celsius and pH 7.0) (PubMed:16677302). kcat is 1.6 sec(-1) with i


organism: Klebsiella pneumoniae

proof_lines: kcat is 2.8 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:10681329). kcat is 117 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:29507065). kcat is 30 sec(-1) wit

substrate: benzylpenicillin (at pH 7.0 and 30 degrees Celsius)


substrate_name: benzylpenicillin (at pH 7.0 and 25 degrees Celsius)

proof_lines: kcat is 32 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:11257029). kcat is 340 sec(-1) with cephaloridine as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:11257029). kcat is 75 sec(-1) with ce


proof_lines: kcat is 245 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:14693513). kcat is 340 sec(-1) with ampicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:14693513). kcat is 208 sec(-1) with amp


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: pNP-butyrate

proof_lines: kcat is 0.0932 sec(-1) with pNP-butyrate as substrate.

substrate: pNP-butyrate


organism: Pseudomonas aeruginosa

substrate_name: amoxicillin (at pH 7.0 and 30 degrees Celsius)

proof_lines: kcat is 0.7 sec(-1) with amoxicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:11502535). kcat is 0.4 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:11502535). kcat is 5.75 sec(-1) with b


substrate_name: benzylpenicillin (in the presence of 0.05 M NaHCO3 at pH 7.0)

proof_lines: kcat is 109 sec(-1) with benzylpenicillin as substrate (in the presence of 0.05 M NaHCO3 at pH 7.0) (PubMed:11724923). kcat is 120 sec(-1) with benzylpenicillin as substrate (in the presence of 0.05 M NaHCO3 at pH 7.0 and 25 degrees Celsius


proof_lines: kcat is 430 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:18559652). kcat is 190 sec(-1) with ampicillin as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:18559652). kcat is 1200 sec(-1) with ca

substrate: benzylpenicillin (at pH 7.0 and 25 degrees Celsius)


substrate_name: amoxicillin (at pH 7.0 and 37 degrees Celsius)

proof_lines: kcat is 7.2 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:9494118). kcat is 8 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:10325401). kcat is 12.4 sec(-1) with


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: penicillin (at pH 7.0 and 25 degrees Celsius)

proof_lines: kcat is 29 sec(-1) with penicillin as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:15561840). kcat is 37 sec(-1) with ampicillin as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:15561840). kcat is 167 sec(-1) with carbenicill


substrate_name: ampicillin (at pH 7.0 and 37 degrees Celsius)

proof_lines: kcat is 5.9 sec(-1) with ampicillin as substrate (at pH 7.0 and 37 degrees Celsius) (PubMed:15561863). kcat is 33 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 37 degrees Celsius) (PubMed:15561863). kcat is 8.2 sec(-1) with tica


proof_lines: kcat is 87 sec(-1) with ampicillin as substrate (at pH 7.0 and 37 degrees Celsius) (PubMed:1633193). kcat is 94 sec(-1) with ampicillin as substrate (at 30 degrees Celsius) (PubMed:21730121). kcat is 508 sec(-1) with nitrocefin as substrate

substrate: ampicillin (at pH 7.0 and 37 degrees Celsius)


substrate_name: ampicillin (at pH 7.0 and 30 degrees Celsius)

proof_lines: kcat is 125 sec(-1) with ampicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:20498317). kcat is 130 sec(-1) with cefalotin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:20498317). kcat is 770 sec(-1) with nitrocefin


substrate_name: ampicillin (at pH 7.0 and 25 degrees Celsius)

proof_lines: kcat is 25 sec(-1) with ampicillin as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:26169409). kcat is 140 sec(-1) with ampicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:26282414). kcat is 357 sec(-1) with cefalotin


organism: Escherichia coli O25b:H4

substrate_name: amoxicillin (at pH 6.4 and 20 degrees Celsius)

proof_lines: kcat is 47 sec(-1) with amoxicillin as substrate (at pH 6.4 and 20 degrees Celsius) (PubMed:29941650). kcat is 40 sec(-1) with amoxicillin as substrate (at pH 6.4 and 20 degrees Celsius) (PubMed:28069651). kcat is 101 sec(-1) with ampicilli


organism: Escherichia coli (strain K12)

substrate_name: benzylpenicillin (at pH 8.2)

proof_lines: kcat is 45 sec(-1) with benzylpenicillin as substrate (at pH 8.2) (PubMed:3264154). kcat is 133 sec(-1) with benzylpenicillin as substrate (at pH 7.0) (PubMed:12323371). kcat is 4.2 sec(-1) with ampicillin as substrate (at pH 8.2) (PubMed:3

substrate: benzylpenicillin (at pH 8.2)


organism: Serratia marcescens

proof_lines: kcat is 19.3 sec(-1) with penicillin as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:11036019). kcat is 181 sec(-1) with ampicillin as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:11036019). kcat is 980 sec(-1) with cephalor

substrate: penicillin (at pH 7.0 and 25 degrees Celsius)


substrate_name: meropenem (at pH 7.0 and 30 degrees Celsius)

proof_lines: kcat is 123 sec(-1) with imipenem as substrate (at pH 7.4 and 30 degrees Celsius) (PubMed:15788415). kcat is 127 sec(-1) with imipenem as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:10898670). kcat is 162 sec(-1) with ampicillin as


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


substrate_name: reduced glutathione (GSH)

column_label: Figure 3 subpanel Gto2; curve value label Km 1.42 mM; article sequence legend maps Gto2 to accession P36156.

normalized_value_unit_evidence: Km 1.42 mM matches the exported Km 1.42 mM.

raw_value_unit_evidence: Figure 3 Gto2 panel reports Km 1.42 mM.

row_label: Gto2 reduced glutathione (GSH) Km(app)

table_label: Figure 3: Thiol transferase activity of Gto proteins as a function of GSH concentration

substrate: reduced glutathione (GSH)


column_label: Figure 3 subpanel Gto1; curve value label Km 1.13 mM; article sequence legend maps Gto1 to accession P48239.

normalized_value_unit_evidence: Km 1.13 mM matches the exported Km 1.13 mM.

raw_value_unit_evidence: Figure 3 Gto1 panel reports Km 1.13 mM.

row_label: Gto1 reduced glutathione (GSH) Km(app)


column_label: Figure 3 subpanel Gto3; curve value label Km 1.40 mM; article sequence legend maps Gto3 to accession Q04806.

normalized_value_unit_evidence: Km 1.40 mM matches the exported Km 1.4 mM.

raw_value_unit_evidence: Figure 3 Gto3 panel reports Km 1.40 mM.

row_label: Gto3 reduced glutathione (GSH) Km(app)


organism: Homo sapiens

substrate_name: phosphoenolpyruvate (at 32 degrees Celsius, pH 8.0)


substrate_name: phosphoenolpyruvate (with magnesium as divalent cation)


organism: Priestia megaterium

substrate_name: NADH

assay_conditions_summary: cofactor NADPH

proof_lines: mutant enzyme A74G/F87V/L188Q/R966D, pH and temperature not specified in the publication

substrate: NADH


substrate_name: NADPH

substrate: NADPH


proof_lines: mutant enzyme A74G/F87V/L188Q/W1046S, pH and temperature not specified in the publication


proof_lines: mutant enzyme A74G/F87V/L188Q/W1046A, pH and temperature not specified in the publication


proof_lines: mutant enzyme A74G/F87V/L188Q, pH and temperature not specified in the publication


proof_lines: mutant enzyme A74G/F87V/L188Q/R966M, pH and temperature not specified in the publication


substrate_name: benzylpenicillin (at pH 7.0 and 30 degrees Celsius)

proof_lines: kcat is 14 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:16189104). kcat is 0.55 sec(-1) with ampicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:16189104). kcat is 0.015 sec(-1) with o


proof_lines: kcat is 13 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:16189104). kcat is 0.45 sec(-1) with ampicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:16189104). kcat is 2220 sec(-1) with ni


substrate_name: ampicillin (at pH 7.4 and 25 degrees Celsius)

proof_lines: kcat is 3100 sec(-1) with ampicillin as substrate (at pH 7.4 and 25 degrees Celsius) (PubMed:19351161). kcat is 898 sec(-1) with piperacillin as substrate (at pH 7.4 and 25 degrees Celsius) (PubMed:19351161). kcat is 1179 sec(-1) with piper


substrate_name: cefuroxime

proof_lines: No activity detected against the monobactam aztreonam.


substrate_name: ampicillin (at pH 7.0)

proof_lines: kcat is 27 sec(-1) with ampicillin as substrate (at pH 7.0) (PubMed:27590339). kcat is 28.6 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:20696873). kcat is 107 sec(-1) with benzylpenicillin as substr

substrate: ampicillin (at pH 7.0)


substrate_name: ampicillin (at pH 6.4)

proof_lines: kcat is 600 min(-1) with ampicillin as substrate. kcat is 340 min(-1) with amoxicillin as substrate. kcat is 560 min(-1) with penicillin G as substrate. kcat is 2100 min(-1) with penicillin V as substrate. kcat is 690 min(-1) with piperacil

proof_lines: kcat is 21 sec(-1) with benzylpenicillin as substrate. kcat is 20 sec(-1) with phenoxymethylpenicillin as substrate. kcat is 2 sec(-1) with amoxicillin as substrate. kcat is 55 sec(-1) with azlocillin as substrate. kcat is 31 sec(-1) with n

substrate: ampicillin (at pH 6.4)


organism: Meleagris gallopavo

substrate_name: H+; Aflatoxin B1; NADPH; O2

substrate: H+; Aflatoxin B1; NADPH; O2


assay_conditions_summary: cofactor NADH

proof_lines: mutant enzyme A74G/F87V/L188Q/W1046A/S965D, pH and temperature not specified in the publication


organism: Taeniopygia guttata

substrate_name: O2; Nicotine; NADPH; H+

substrate: O2; Nicotine; NADPH; H+


organism: Acidovorax sp. KKS102

substrate_name: glutathione

proof_lines: wild type enzyme, pH and temperature not specified in the publication

substrate: glutathione


proof_lines: mutant enzyme Y12C, pH and temperature not specified in the publication


organism: Agrobacterium tumefaciens

substrate_name: 2-hydroxyethyl disulfide

proof_lines: pH 6.5, 37°C, recombinant AtuGSTH1-1, with 2-hydroxyethyl disulfide

proof_lines: pH 6.5, 37°C, recombinant AtuGSTH1-1, with 1-chloro-2,4-dinitrobenzene

substrate: 2-hydroxyethyl disulfide


proof_lines: pH 6.5, 37°C, recombinant AtuGSTH1-1 mutant R187A, with 1-chloro-2,4-dinitrobenzene


proof_lines: pH 6.5, 37°C, recombinant AtuGSTH1-1 mutant S25A, with 1-chloro-2,4-dinitrobenzene


proof_lines: pH 6.5, 37°C, recombinant AtuGSTH1-1 mutant F22A, with 1-chloro-2,4-dinitrobenzene


organism: Alburnus tarichi

proof_lines: pH and temperature not specified in the publication


organism: Alitta succinea


organism: Alternaria brassicicola

proof_lines: isoform GTT1.2, at pH 7.5, temperature not specified in the publication

proof_lines: isoform Ure2pB1, at pH 7.5, temperature not specified in the publication

proof_lines: isoform GSTFuA1, at pH 7.5, temperature not specified in the publication


organism: Anopheles dirus


substrate_name: reduced glutathione

substrate: reduced glutathione


assay_conditions_summary: pH 6.5; buffer pH 6

proof_lines: mutant enzyme Y215H, in 0.1 M phosphate buffer pH 6.5


organism: Bacillus licheniformis

substrate_name: 12-methyl-tetradecanoic acid

proof_lines: CYP102A7, at pH 7.5, highest binding affinity

substrate: 12-methyl-tetradecanoic acid


organism: Bacillus subtilis

substrate_name: omega-(p-nitrophenyl)octanoic acid

substrate: omega-(p-nitrophenyl)octanoic acid


substrate_name: omega-(p-nitrophenyl)dodecanoic acid

substrate: omega-(p-nitrophenyl)dodecanoic acid


organism: Canis familiaris

substrate_name: NADPH; Bufuralol; H+; O2

substrate: NADPH; Bufuralol; H+; O2


organism: Gallus gallus

substrate_name: H+; O2; NADPH; Bufuralol

substrate: H+; O2; NADPH; Bufuralol


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

proof_lines: complex POR-CYP1A1, presence of heme oxygenase, pH 7.5, 37°C

proof_lines: desulfuration by recombinant human CYPs to fenthion-oxon


substrate_name: Ethacrynic acid

assay_conditions_summary: pH 6.5; buffer phosphate

proof_lines: mutant enzyme Y215S, in 0.1 M phosphate buffer pH 6.5

substrate: Ethacrynic acid


proof_lines: mutant enzyme Y215F, in 0.1 M phosphate buffer pH 6.5


proof_lines: mutant enzyme R214A, in 0.1 M phosphate buffer pH 6.5


proof_lines: mutant enzyme F212W, in 0.1 M phosphate buffer pH 6.5


proof_lines: mutant enzyme Q112A, in 0.1 M phosphate buffer pH 6.5


substrate_name: NADPH


organism: Rattus norvegicus

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


organism: Rhodococcus ruber

substrate_name: NADH

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH


organism: Salmo salar

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

ki_unit: mM

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


organism: Streptomyces tubercidicus

substrate_name: avermectin

substrate: avermectin


organism: Sus scrofa

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

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


organism: Homo sapiens


substrate_name: prostaglandin A2 (at pH 7.0 and 37 degrees Celsius)


substrate: prostaglandin A2 (at pH 7.0 and 37 degrees Celsius)


organism: Mus musculus

substrate_name: prostaglandin H2

substrate: prostaglandin H2


assay_conditions_summary: pH 6.5; buffer 0.1 M phosphate

proof_lines: mutant enzyme F212A, in 0.1 M phosphate buffer pH 6.5


organism: Anopheles gambiae


organism: Arabidopsis thaliana

substrate_name: acrolein

substrate: acrolein


organism: Ascaris suum


proof_lines: mutant enzyme F212H, in 0.1 M phosphate buffer pH 6.5


proof_lines: mutant enzyme F212E, in 0.1 M phosphate buffer pH 6.5


substrate_name: reduced glutathione


proof_lines: mutant enzyme F212L, in 0.1 M phosphate buffer pH 6.5


proof_lines: wild type enzyme, in 0.1 M phosphate buffer pH 6.5


proof_lines: mutant enzyme F216A, in 0.1 M phosphate buffer pH 6.5


proof_lines: mutant enzyme Y215E, in 0.1 M phosphate buffer pH 6.5


proof_lines: mutant enzyme F212Y, in 0.1 M phosphate buffer pH 6.5


proof_lines: mutant enzyme Y215A, in 0.1 M phosphate buffer pH 6.5


proof_lines: mutant enzyme T174A, in 0.1 M phosphate buffer pH 6.5


organism: Aspergillus nidulans

substrate_name: glutathione


organism: Atactodea striata

substrate_name: GSH

substrate: GSH


organism: Bemisia tabaci

substrate_name: monochlorobimane

proof_lines:
strain GER-01
strain SUD-S

substrate: monochlorobimane


organism: Bombyx mori

proof_lines:
at 25°C
GSTO
GSTD

substrate: glutathione


proof_lines: pH 6.5, 30°C, recombinant wild-type enzyme


organism: Clonorchis sinensis


organism: Coturnix sp.

substrate_name: Unknown

proof_lines: at pH 6.5, temperature not specified in the publication

substrate: Unknown


organism: Cydia pomonella


organism: Danio rerio

substrate_name: Dichloroacetic acid

proof_lines:
isoform Gstz1, at pH 6.5 and 25°C
isoform Gstp2, at pH 6.5 and 25°C
isoform Gstp1, at pH 6.5 and 25°C

substrate: Dichloroacetic acid


organism: Drosophila melanogaster

proof_lines: GSTD1, pH and temperature not specified in the publication


organism: Eretmochelys imbricata


organism: Brucella anthropi


organism: Haloarcula hispanica

proof_lines: pH and temperature not specified in the publication


organism: Hevea brasiliensis


organism: Hippocampus abdominalis

proof_lines:
isoform GSTrho, at pH 6.5 and 25°C
isoform GSTmu, at pH 6.5 and 25°C


organism: Homo sapiens

proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant E96Y GST121 (chimeric protein between GST 1-1 and GST 2-2)


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant G97T GST121 (chimeric protein between GST 1-1 and GST 2-2)


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant G97P GST121 (chimeric protein between GST 1-1 and GST 2-2)


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant E96F GST121 (chimeric protein between GST 1-1 and GST 2-2)


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant G97S GST121 (chimeric protein between GST 1-1 and GST 2-2)


proof_lines: SABIO-RK modifier species: glutathione transferase(Enzyme) mutant Y8F GST121 (chimeric protein between GST 1-1 and GST 2-2)


assay_conditions_summary: pH 6.5; 303.15 K; buffer 0.1 M potassium phosphate

proof_lines: mutant enzyme C14A/C47A/C101A/C169A, at 30°C, in 0.1 M potassium phosphate buffer, pH 6.5


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant M91A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant K62E


organism: Gelatoporia subvermispora

substrate_name: 5-chloromethylfluorescein diacetate

proof_lines: mutant enzyme N22A, pH and temperature not specified in the publication

substrate: 5-chloromethylfluorescein diacetate


organism: Glycine max

proof_lines: pH 6.5, 30°C, recombinant GSTU4-4 mutant D48A


proof_lines: pH 6.5, 30°C, recombinant wild-type GSTU4-4


proof_lines: pH 6.5, 30°C, recombinant GSTU4-4 mutant P49A


proof_lines: pH 6.5, 30°C, recombinant GSTU4-4 mutant S13A


proof_lines: with fluorodifen as cosubstrate, pH and temperature not specified in the publication

proof_lines: with cumene hydroperoxide as cosubstrate, pH and temperature not specified in the publication

proof_lines: with tert-butyl peroxide as cosubstrate, at pH 6.5 and 25°C


organism: Callithrix jacchus

proof_lines:
isoform GSTM2, at pH 7.4 and 25°C
isoform GSTM4, at pH 7.4 and 25°C
isoform GSTM3, at pH 7.4 and 25°C


organism: Camelus dromedarius

substrate_name: phenethyl isothiocyanate

proof_lines: with phenethyl isothiocyanate as cosubstrate, at pH 7.0, temperature not specified in the publication

proof_lines: with 1-chloro-2,4-dinitrobenzene as cosubstrate, at pH 7.0, temperature not specified in the publication

substrate: phenethyl isothiocyanate


organism: Caretta caretta


organism: Cavia porcellus


organism: Chelonia mydas


organism: Chlamys islandica


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant K62A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant S19A


substrate_name: (R,R)-1-phenylpropylene oxide

assay_conditions_summary: pH 7.2; 303.15 K; buffer 250 mM Tris-HCl

proof_lines: mutant enzyme I10C, at 30°C in 250 mM Tris-HCl buffer, pH 7.2

substrate: (R,R)-1-phenylpropylene oxide


proof_lines: mutant enzyme C47A/C101A, at 30°C, in 0.1 M potassium phosphate buffer, pH 6.5


proof_lines: pH 7.4, 37°C, mutant enzyme C16A of glutathione transferase Zeta 1c-1c, reaction with (+)-2-bromo-3-(4-nitrophenyl)propanoic acid

proof_lines: pH 7.4, 37°C, mutant enzyme C16A of glutathione transferase Zeta 1c-1c, reaction with maleylacetone


assay_conditions_summary: pH 6.5; 298.15 K; buffer phosphate

proof_lines: mutant enzyme D94N, in phosphate buffer (pH 6.5), at 25°C


organism: Escherichia coli

assay_conditions_summary: pH 6.5; 298.15 K; buffer 100 mM phosphate

proof_lines: mutant enzyme C10A, at 25°C, in 100 mM phosphate buffer (pH 6.5)


proof_lines: mutant enzyme H106A, at 25°C, in 100 mM phosphate buffer (pH 6.5)


proof_lines: mutant enzyme C10S, at 25°C, in 100 mM phosphate buffer (pH 6.5)


proof_lines: mutant enzyme H106F, at 25°C, in 100 mM phosphate buffer (pH 6.5)


proof_lines: wild type enzyme, at 25°C, in 100 mM phosphate buffer (pH 6.5)


organism: Fasciola gigantica

proof_lines: wild type enzyme, at pH 7.5, temperature not specified in the publication


proof_lines: 30°C, mutant enzyme Y108F, reaction with 1,2-epoxy-3-(p-nitrophenoxy)propane

proof_lines: 30°C, mutant enzyme Y108F, reaction with 1,2-dichloro-4-nitrobenzene


proof_lines: mutant enzyme D90N, in phosphate buffer (pH 6.5), at 25°C


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant W126A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant Y18F


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant L88A


substrate_name: gamma-Glu-Cys-Sar

assay_conditions_summary: pH 7.4; 298.15 K; buffer and cosubstrate context

proof_lines: mutant enzyme I104V, in 0.1 M phosphate buffer at pH 6.5

proof_lines: mutant enzyme I104V, in the presence of cosubstrate 7-chloro-4-nitrobenz-2-oxa-1,3-diazole, in 0.1 M phosphate buffer at pH 6.5

substrate: gamma-Glu-Cys-Sar


proof_lines: mutant enzyme T67A, in phosphate buffer (pH 6.5), at 25°C


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant S200A


assay_conditions_summary: pH 7.4; 310.15 K; buffer 0.1 M phosphate

proof_lines: pH 7.4, 37°C, enzyme variant glutathione transferase Zeta 1d-1d

proof_lines: pH 7.4, 37°C, enzyme variant glutathione transferase Zeta 1c-1c

proof_lines: pH 7.4, 37°C, enzyme variant glutathione transferase Zeta 1b-1b


proof_lines: pH 7.4, 37°C, mutant enzyme R175K of glutathione transferase Zeta 1c-1c, reaction with (+)-2-bromo-3-(4-nitrophenyl)propanoic acid

proof_lines: pH 7.4, 37°C, mutant enzyme R175K of glutathione transferase Zeta 1c-1c, reaction with maleylacetone


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant P55A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant D201A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant F87A


proof_lines: pH 7.4, 37°C, mutant enzyme R175A of glutathione transferase Zeta 1c-1c, reaction with (+)-2-bromo-3-(4-nitrophenyl)propanoic acid

proof_lines: pH 7.4, 37°C, mutant enzyme R175A of glutathione transferase Zeta 1c-1c, reaction with maleylacetone


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant M91K


proof_lines: 30°C, mutant enzyme Y108A, reaction with 1,2-epoxy-3-(p-nitrophenoxy)propane

proof_lines: 30°C, mutant enzyme Y108A, reaction with 1,2-dichloro-4-nitrobenzene


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant N53A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant R202A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant F83W


proof_lines: pH 7.4, 37°C, mutant enzyme S15A of glutathione transferase Zeta 1c-1c, reaction with (+)-2-bromo-3-(4-nitrophenyl)propanoic acid

proof_lines: pH 7.4, 37°C, mutant enzyme S15A of glutathione transferase Zeta 1c-1c, reaction with maleylacetone


proof_lines: mutant enzyme R70Q, in phosphate buffer (pH 6.5) ,at 25°C

proof_lines: mutant enzyme R70Q, in phosphate buffer (pH 6.5), at 25°C


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant L15A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant F83A


proof_lines: mutant enzyme C14A/C47A/C101A, at 30°C, in 0.1 M potassium phosphate buffer, pH 6.5


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant D69A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant F87W


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant P56A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant I44A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant L58A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant P17A


organism: Liposcelis bostrychophila

proof_lines: in phosphate buffer (0.1 M, pH 6.5), at 25°C


organism: Liposcelis entomophila


organism: Liposcelis paeta

proof_lines: pH 7.5, 37°C, enzyme of Wuzhou population

proof_lines: pH 7.5, 37°C, enzymes of Hezhou and Nanyang population

proof_lines: pH 7.5, 37°C, enzyme of Nanyang population


organism: Lucilia cuprina

proof_lines: Y113F mutant, cosubstrate: 1-chloro-2,4-dinitrobenzene


proof_lines: S9A mutant, cosubstrate: 1-chloro-2,4-dinitrobenzene


proof_lines: mutant enzyme G112C, at 30°C in 250 mM Tris-HCl buffer, pH 7.2


proof_lines: 30°C, mutant enzyme Y108W, reaction with 1,2-epoxy-3-(p-nitrophenoxy)propane

proof_lines: 30°C, mutant enzyme Y108W, reaction with 1,2-dichloro-4-nitrobenzene


organism: Hordeum vulgare


organism: Hyphantria cunea


organism: Lathyrus oleraceus

substrate_name: fluorodifen

substrate: fluorodifen


organism: Lepidochelys olivacea


organism: Macaca mulatta


organism: Macrobrachium vollenhovenii


organism: Monopterus albus


organism: Mucor mucedo

proof_lines: pH 8.0, substrate concentration 0.1-0.3 mM

proof_lines: pH 8.0, substrate concentration 0.3-2.0 mM


organism: Mus musculus

proof_lines: pH 6.5, 25°C, recombinant catalytically active monoclonal antibody fragment ScFv2F3


proof_lines: pH 7.4, 37°C, recombinant mutant F2:1215


organism: Homo sapiens

proof_lines: mutant enzyme R74Q, in phosphate buffer (pH 6.5), at 25°C


proof_lines: mutant enzyme A113V, in 0.1 M phosphate buffer at pH 6.5

proof_lines: mutant enzyme A113V, in the presence of cosubstrate 7-chloro-4-nitrobenz-2-oxa-1,3-diazole, in 0.1 M phosphate buffer at pH 6.5

proof_lines: mutant enzyme A113V, in the presence of cosubstrate 1-chloro-2,4-dinitrobenzene, in 0.1 M phosphate buffer at pH 6.5


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant D69T


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant S16A


assay_conditions_summary: pH 7.4; 298.15 K; buffer 0.1 M phosphate

proof_lines: mutant enzyme I104V/A113V, at pH 7.4 and 25°C

proof_lines: mutant enzyme I104V/A113V, in 0.1 M phosphate buffer at pH 6.5

proof_lines: mutant enzyme I104V/A113V, in the presence of cosubstrate 7-chloro-4-nitrobenz-2-oxa-1,3-diazole, in 0.1 M phosphate buffer at pH 6.5


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant L183A


proof_lines: mutant enzyme F136A, at pH 7.5, temperature not specified in the publication


organism: Gallus gallus

proof_lines:
pH 7.5, 28°C, GSH-S transferase rho
with reduced glutathione

substrate: reduced glutathione


organism: Gelatoporia subvermispora

substrate_name: 4-methylumbelliferyl acetate

proof_lines: mutant enzyme N24A, pH and temperature not specified in the publication

substrate: 4-methylumbelliferyl acetate


proof_lines: wild type enzyme, pH and temperature not specified in the publication


proof_lines: mutant enzyme Y46A, pH and temperature not specified in the publication


organism: Novosphingobium aromaticivorans


proof_lines: mutant enzyme S14A/S15A, at pH 8.0 and 30°C


organism: Onchocerca volvulus


organism: Phanerodontia chrysosporium

substrate_name: dehydroascorbate

proof_lines:
isoform GSTO4, at pH 6.5 and 20°C
isoform GSTO7, at pH 6.5 and 20°C
isoform GSTO3, at pH 6.5 and 20°C

substrate: dehydroascorbate


proof_lines: recombinant wild-type, pH 6.5, temperature not specified in the publication


proof_lines: recombinant mutant S22A, pH 6.5, temperature not specified in the publication


organism: Pinus brutia

substrate_name: Ethacrynic acid

substrate: Ethacrynic acid


organism: Pinus tabuliformis


organism: Plasmodium falciparum


organism: Plasmodium vivax


organism: Nilaparvata lugens


organism: Musca domestica

proof_lines: recombinant His-tagged wild-type enzyme, pH and temperature not specified in the publication

proof_lines: recombinant detagged wild-type enzyme, pH and temperature not specified in the publication


proof_lines: recombinant His-tagged mutant R113A, pH and temperature not specified in the publication


proof_lines: recombinant His-tagged mutant F108G, pH and temperature not specified in the publication


organism: Myathropa florea


organism: Oryza sativa

proof_lines: mutant enzyme F116A, at 25°C, pH not specified in the publication


proof_lines: mutant enzyme Y113A, at 25°C, pH not specified in the publication


proof_lines: mutant enzyme L112A, at 25°C, pH not specified in the publication


proof_lines: mutant enzyme W161A, at 25°C, pH not specified in the publication


proof_lines: mutant enzyme N109A, at 25°C, pH not specified in the publication


proof_lines: mutant enzyme F162A, at 25°C, pH not specified in the publication


proof_lines: mutant enzyme M17A, at 25°C, pH not specified in the publication


proof_lines: wild type enzyme, at 25°C, pH not specified in the publication


organism: Pagrus major


organism: Paraburkholderia xenovorans

proof_lines: pH 6.5, 25°C, recombinant enzyme, with (2Z,4E)-3-chloro-6-(3,5-dichlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid

proof_lines: pH 6.5, 25°C, recombinant enzyme, with (2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid

proof_lines: pH 6.5, 25°C, recombinant enzyme, with (2E,4Z)-5-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid


organism: Penaeus vannamei


organism: Rattus norvegicus


organism: Plasmodium yoelii


organism: Plutella xylostella


organism: Populus trichocarpa

substrate_name: sulforaphane

proof_lines: isoform GSTU45, pH not specified in the publication, at 30°C

proof_lines: isoform GSTU16, pH not specified in the publication, at 30°C

substrate: sulforaphane


organism: Proteus mirabilis


organism: Saccharomyces cerevisiae

proof_lines: Ure2p mutant A122C, at 25°C and pH 8.0, in the presence of 1 mM dithiothreitol


organism: Salix babylonica

proof_lines:
isoform GSTU7, at pH 6.5 and 25°C
isoform GSTU8, at pH 6.5 and 25°C
isoform GSTU12, at pH 6.5 and 25°C


organism: Salmo salar


organism: Sarcoptes scabiei


organism: Schistocerca gregaria


organism: Schistosoma japonicum


proof_lines: pH 6.5, 25°C, recombinant wild-type enzyme


organism: Rhodotorula mucilaginosa


organism: Pseudomonas putida

substrate_name: trans-o-hydroxybenzylidene pyruvic acid

substrate: trans-o-hydroxybenzylidene pyruvic acid


organism: Zea mays

proof_lines: mutant enzyme T12P, reaction with ethacrynic acid

proof_lines: mutant enzyme T12P, reaction with 1-chloro-2,3-dinitrobenzoate


organism: Acanthocardia tuberculata

substrate_name: IDP

assay_conditions_summary: cofactor ADP

substrate: IDP


organism: Arabidopsis thaliana

substrate_name: ADP

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ADP

substrate: ADP


organism: Archaeoglobus fulgidus

assay_conditions_summary: 323.15 K; cofactor ADP

proof_lines: 50°C, pH not specified in the publication


organism: Bacillus licheniformis

substrate_name: phosphoenolpyruvate

assay_conditions_summary: pH 7.1; 303.15 K; cofactor ADP

proof_lines: pH 7.1, 30°C, in the presence of Mg2+, 7fold lower in the presence of Mn2+

substrate: phosphoenolpyruvate


organism: Brassica juncea

assay_conditions_summary: pH 7; 298.15 K; cofactor ADP


proof_lines: 4°C, 20 mM sodium phosphate buffer, pH 6.5, 0.5 mM glutathione

proof_lines: 25°C, 20 mM sodium phosphate buffer, pH 7.0, 0.5 mM glutathione


organism: Schistosoma mansoni

substrate_name: hydroxyethyldisulfide

substrate: hydroxyethyldisulfide


organism: Setaria cervi


organism: Setaria faberi


organism: Solenopsis invicta


organism: Spinacia oleracea

substrate_name: glutathione

substrate: glutathione


organism: Brassica napus

substrate_name: Phosphoenolpyruvate; ADP

assay_conditions_summary: pH 8; 297.15 K; cofactor ADP

substrate: Phosphoenolpyruvate; ADP


organism: Brassica rapa subsp. oleifera

assay_conditions_summary: pH 6.8; 303.15 K; cofactor ADP


organism: Busycotypus canaliculatum

assay_conditions_summary: pH 7; 293.15 K; cofactor ADP

proof_lines: in the absence of fructose 1,6-diphosphate

proof_lines: in the presence of fructose 1,6-diphosphate


organism: Canis familiaris

substrate_name: ADP; Phosphoenolpyruvate

substrate: ADP; Phosphoenolpyruvate


organism: Canis lupus familiaris


organism: Chlamydomonas reinhardtii


organism: Zea mays

substrate_name: alachlor

proof_lines: mutant enzyme F35L, reaction with ethacrynic acid

substrate: alachlor


proof_lines: mutant enzyme T12I, reaction with ethacrynic acid

proof_lines: mutant enzyme T12I, reaction with 1-chloro-2,3-dinitrobenzoate


proof_lines: pH 6.5, 30°C, recombinant wild-type enzyme

proof_lines: wild-type enzyme GST I, reaction with ethacrynic acid


proof_lines: mutant enzyme I118F, reaction with ethacrynic acid


proof_lines: pH 6.5, 35°C, in presence of cloquintocet-mexyl


organism: Homo sapiens

proof_lines: mutant S12D, pH not specified in the publication, 30°C


proof_lines: mutant C436A, pH not specified in the publication, 30°C


proof_lines: mutant C436T, pH not specified in the publication, 30°C


assay_conditions_summary: pH 6; 298.15 K; cofactor ADP

proof_lines: wild type enzyme, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°C

proof_lines: wild type enzyme, in the presence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°C


substrate_name: Unknown

proof_lines: mutant enzyme H391Y, in the absence of D-fructose 1,6-bisphosphate

proof_lines: mutant enzyme H391Y, in the presence of 2.5 mM D-fructose 1,6-bisphosphate

substrate: Unknown


proof_lines: Y235A mutant, Vmax = 1.1 micromol/min/mg


organism: Tetranychus urticae

proof_lines:
isoform GSTd14, at pH 6.5 and 25°C
isoform GSTd10, at pH 6.5 and 25°C
isoform GSTm09, at pH 6.5 and 25°C


organism: Thermosynechococcus vestitus

assay_conditions_summary: 303.15 K; buffer 0.1 M potassium phosphate

proof_lines: at 30°C in 0.1 M potassium phosphate buffer


organism: Trachemys scripta elegans

substrate_name: GSH

proof_lines:
homodimeric enzyme
heterodimeric enzyme

substrate: GSH


organism: Trichinella spiralis


organism: Triticum aestivum


organism: Wuchereria bancrofti


organism: Cicer arietinum


organism: Columba livia


organism: Coprinopsis lagopus


organism: Corynebacterium glutamicum

assay_conditions_summary: pH 7; 308.15 K; cofactor ADP


organism: Cupriavidus necator


organism: Cynodon dactylon


organism: Sus scrofa

proof_lines:
pH 7.8, 30°C
at pH 7.5 and 30°C


organism: Synechococcus elongatus


organism: Synechocystis sp.


organism: Syrphus ribesii


organism: Taenia crassiceps

proof_lines:
isoform GST2, at pH 7.5 and 25°C
isoform GST2, at pH 8.5 and 25°C
isoform GST1, at pH 8.5 and 25°C


organism: Taenia solium

proof_lines:
recombinant enzyme, at 25°C
at 25°C


organism: Musa cavendishii

assay_conditions_summary: pH 6.9; 298.15 K; cofactor ADP

proof_lines: hyperbolic saturation kinetics, pH 6.9, 25°C


organism: Mustela vison


organism: Mycolicibacterium smegmatis


organism: Nautilus pompilius


organism: Oryctolagus cuniculus

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ADP

proof_lines:
recombinant enzyme, at pH 7.4 and 37°C
native enzyme, at pH 7.4 and 37°C


organism: Pelophylax ridibundus


organism: Homo sapiens

proof_lines: mutant C436S, pH not specified in the publication, 30°C


assay_conditions_summary: pH 8; 305.15 K; cofactor ADP

proof_lines: in the presence of D-fructose 1,6-bisphosphate

proof_lines: pH 8.0, 32°C, activation by 2 mM D-fructose-1,6-bisphosphate


assay_conditions_summary: pH 7.6; 310.15 K; cofactor ADP


organism: Lactococcus lactis

substrate_name: GDP

substrate: GDP


organism: Lactococcus lactis subsp. lactis

substrate_name: Pyruvate; ATP

assay_conditions_summary: cofactor ATP

substrate: Pyruvate; ATP


organism: Leishmania mexicana

assay_conditions_summary: pH 7.5; cofactor ADP


proof_lines: Y235S mutant, Vmax = 1.2 micromol/min/mg


proof_lines: mutant C436D, pH not specified in the publication, 30°C


proof_lines: mutant C436H, pH not specified in the publication, 30°C


proof_lines: mutant C436N, pH not specified in the publication, 30°C


proof_lines: mutant enzyme K422R, in the absence of D-fructose 1,6-bisphosphate

proof_lines: mutant enzyme K422R, in the presence of 2.5 mM D-fructose 1,6-bisphosphate


proof_lines: mutant enzyme E117K, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°C


organism: Periplaneta americana

assay_conditions_summary: cofactor ADP


organism: Pigeon


organism: Plasmodium falciparum

proof_lines: in presence of inhibitor suramin, pH and temperature not specified in the publication


organism: Rhodotorula toruloides


organism: Saccharolobus solfataricus

proof_lines: 50°C, pH not specified in the publication

proof_lines: 65°C, pH not specified in the publication

proof_lines: 70°C, pH not specified in the publication


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 6.2; 303.15 K; cofactor ADP

proof_lines:
cosubstrate phosphoenolpyruvate
pH 6.2, 30°C


organism: Lethenteron camtschaticum

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ADP


organism: Meganyctiphanes norvegica

assay_conditions_summary: pH 7

proof_lines:
15?, pH 7.0, isoform PK I, in winter
15?, pH 7.0, isoform PK I, in summer
15?, pH 7.0, isoform PK II, in summer


organism: Metacarcinus magister

proof_lines: in the presence of fructose 1,6-diphosphate


organism: Mucor rouxii


organism: Mus musculus


proof_lines: pH 6.2, wild-type enzyme, Mn2+-activated

proof_lines: pH 6.2, wild-type enzyme, Mn2+- and fructose 1,6-bisphosphate activated

proof_lines: pH 6.2, wild-type enzyme, Mg2+ and fructose 1,6-bisphosphate activated


proof_lines: mutant enzyme T298A, activated be Tl+ and Mn2+


proof_lines: mutant enzyme T298S, activated be Tl+ and Mn2+


proof_lines: pH 6.2, mutant enzyme T298C, Mn2+-activated

proof_lines: mutant enzyme T298C, activated be Tl+ and Mn2+

proof_lines: pH 6.2, mutant enzyme T298C, Mn2+- and fructose 1,6-bisphosphate activated


organism: Saccharomyces pastorianus


organism: Schistosoma mansoni


organism: Trypanosoma brucei

proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R19Q


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant F463V


organism: Trypanosoma brucei brucei

proof_lines: recombinant enzyme, pH 7.2, 25°C, in presence of fructose 2,6-bisphosphate

proof_lines: recombinant enzyme, pH 7.2, 25°C, in presence of fructose 1,6-bisphosphate


organism: Trypanosoma congolense


organism: Trypanosoma cruzi


organism: Urocitellus richardsonii

proof_lines: purified enzyme, pH 7.0, 25°C/room temperature


organism: Vibrio cholerae serotype O1

assay_conditions_summary: pH 7; 298.15 K; cofactor ADP

proof_lines: pH 7.0, 25°C, recombinant non-His-tagged enzyme, in presence of fructose 1,6-bisphosphate

proof_lines: pH 7.0, 25°C, recombinant His-tagged enzyme, in presence of fructose 1,6-bisphosphate


organism: Vigna radiata

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ADP


organism: Zapus hudsonius


organism: Zymomonas mobilis

assay_conditions_summary: pH 6.5; 298.15 K; cofactor ADP


organism: Agroathelia rolfsii

substrate_name: starch

proof_lines:
soluble, glucoamylase G1 or G3
glucoamylase G2 or G3
soluble, glucoamylase G2

substrate: starch


organism: Aspergillus awamori

substrate_name: kojibiose

proof_lines: wild-type enzyme or mutant enzymes Gly183Lys or S184H

substrate: kojibiose


organism: Toxoplasma gondii

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ADP

proof_lines: PykII, in 100 mM Tris-HCl,pH 8.5, at 37°C


organism: Trachemys scripta


organism: Trachemys scripta elegans

assay_conditions_summary: pH 7.2; 295.15 K; cofactor ADP

proof_lines:
muscle enzyme, pH 7.2, 22°C
muscle enzyme, pH 6.6, 22°C
liver enzyme, pH 6.6, 22°C


assay_conditions_summary: pH 7.4; 298.15 K; cofactor ADP


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant L76R


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R22G


organism: Selenomonas ruminantium

assay_conditions_summary: pH 7; cofactor ATP


organism: Sparus aurata

substrate_name: pyruvate

proof_lines:
25°C, sample taken in June
25°C, sample taken in January

substrate: pyruvate


organism: Streptococcus mutans

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: in the presence of glucose 6-phosphate, at pH 7.5


organism: Streptococcus sanguis


organism: Sus scrofa

assay_conditions_summary: 298.15 K; cofactor ADP

proof_lines:
bound enzyme
solubilized enzyme
at 25°C


organism: Synechococcus elongatus


substrate_name: maltose

substrate: maltose


substrate_name: isomaltose

substrate: isomaltose


proof_lines: recombinant enzyme expressed in Pichia pastoris


proof_lines:
mutant enzyme G183K
mutant enzyme Gly183Lys


proof_lines:
mutant enzyme S184H
mutant S184H


organism: Aspergillus neotritici


organism: Aspergillus niger


organism: Entamoeba histolytica


organism: Entodinium sp.


organism: Geobacillus stearothermophilus

assay_conditions_summary: pH 7.2; 303.15 K; buffer 50 mM imidazole-HCl; cofactor ADP

proof_lines: wild type enzyme, in the presence of 0.1 mM ribose 5'-phosphate, in 50 mM imidazole-HCl buffer, pH 7.2, 50 mM KCl, 7 mM MgCl2, 0.12 mM NADH, 0.02 mg/ml lactate dehydrogenase, 2 mM PEP, and 4 mM ADP, at 30°C


proof_lines: mutant enzyme C9S/C268S, in the presence of 0.1 mM ribose 5'-phosphate, in 50 mM imidazole-HCl buffer, pH 7.2, 50 mM KCl, 7 mM MgCl2, 0.12 mM NADH, 0.02 mg/ml lactate dehydrogenase, 2 mM PEP, and 4 mM ADP, at 30°C


organism: Homo sapiens

proof_lines: mutant C436M, pH not specified in the publication, 30°C


proof_lines: Y235F mutant, Vmax = 0.6 micromol/min/mg


proof_lines: pH 4.5, 35°C, recombinant wild-type enzyme


proof_lines: pH 4.5, 35°C, recombinant mutant D20C/A27C/S30P/G137A


organism: Aspergillus niveus


organism: Synechococcus sp.

proof_lines:
allosteric enzyme, pH 7.5, 24°C
allosteric enzyme, pH 7.0, 24°C


organism: Takifugu rubripes

assay_conditions_summary: pH 7.4; cofactor ADP

proof_lines: activated by fructose D-1,6-bisphosphate


organism: Tenebrio molitor

proof_lines: in the presence of fructose 1,6-diphosphate


organism: Thermofilum pendens

assay_conditions_summary: pH 6; 318.15 K; cofactor ADP

proof_lines: pH 6.0, 45°C, recombinant enzyme with His6 tag


organism: Thermoplasma acidophilum


organism: Thermoproteus tenax

assay_conditions_summary: pH 7; 323.15 K; cofactor ADP


organism: Caulobacter vibrioides


organism: Clostridium thermoamylolyticum

proof_lines:
pH 4.5, recombinant enzyme
pH 4.5, 65°C, recombinant enzyme


organism: Fusarium solani

substrate_name: soluble starch

proof_lines:
pH 4.5, 40°C, purified native enzyme
pH 4.5, 40°C, native enzyme
pH 5.5, 40°C, native enzyme

substrate: soluble starch


organism: Gymnascella citrina

proof_lines:
immobilized enzyme, pH 5.5, 50°C
free enzyme, pH 5.5, 50°C
pH 3.5-5.5, 50°C


substrate_name: maltotetraose

proof_lines: ntMGAM, N-terminal subunit of MGAM, Vmax: 7.65 U/mg

proof_lines: ntMGAM, N-terminal subunit of MGAM, Vmax: 9.58 U/mg

substrate: maltotetraose


organism: Humicola sp.


organism: Thermoactinomyces vulgaris


organism: Thermoanaerobacter ethanolicus

substrate_name: potato starch

substrate: potato starch


organism: Thermomyces lanuginosus

proof_lines:
pH 5.0, 70°C
values about 0.8 mg/ml for starch


organism: Thermothielavioides terrestris

substrate_name: maltotriose

substrate: maltotriose


organism: Achromobacter sp. sallbros1

substrate_name: aztreonam

proof_lines:
or below, pH 7.2, 25°C
pH 7.2, 25°C

substrate: aztreonam


organism: Aspergillus oryzae

substrate_name: maltohexaose

substrate: maltohexaose


organism: Aspergillus phoenicis

substrate_name: amylose

substrate: amylose


organism: Athelia rolfsii

substrate_name: Maltose; H2O

substrate: Maltose; H2O


organism: Aureobasidium pullulans


organism: Caldanaerobacter subterraneus subsp. tengcongensis MB4


organism: Camelus dromedarius


organism: Acinetobacter bereziniae

substrate_name: meropenem

proof_lines: 30°C, pH not specified in the publication

substrate: meropenem


organism: Acinetobacter pittii

substrate_name: cefoxitin

substrate: cefoxitin


organism: Acinetobacter sp.

substrate_name: cephaloridine

proof_lines: pH and temperature not specified in the publication

substrate: cephaloridine


organism: Aeromonas enteropelogenes

substrate_name: cefepime

substrate: cefepime


organism: Aeromonas hydrophila

substrate_name: biapenem

substrate: biapenem


substrate_name: cefotaxime

assay_conditions_summary: pH 6.5; 303.15 K; buffer 20 mM sodium cacodylate

proof_lines:
above, wild-type, 30°C, pH 6.5
below, wild-type, 30°C, pH 6.5
wild-type, 30°C, pH 6.5

substrate: cefotaxime


organism: Rasamsonia emersonii


organism: Rhizopus arrhizus

proof_lines:
recombinant AmyD, pH 5.5, 40°C
recombinant AmyC, pH 5.5, 40°C
enzyme form GII


organism: Rhizopus sp.


organism: Saccharomyces cerevisiae


organism: Saccharophagus degradans

proof_lines: S05 value, Hill coefficient 1.1, pH 6, 20°C

proof_lines: S05 value, Hill coefficient 1.1, pH 6, 39°C


organism: Tetracladium sp.

substrate_name: starch

substrate: starch


substrate_name: nitrocefin

proof_lines:
T157A mutant, 30°C, pH 6.5
above, T157A mutant, 30°C, pH 6.5

substrate: nitrocefin


proof_lines:
V67D mutant, 30°C, pH 6.5
above, V67D mutant, 30°C, pH 6.5


proof_lines:
H196A mutant, 30°C, pH 6.5
above, H196A mutant, 30°C, pH 6.5


proof_lines: mutant enzyme N116H/N220G, in 20 mM sodium cacodylate buffer, pH 6.5


organism: Lentinula edodes


organism: Moesziomyces antarcticus

substrate_name: short-chain amylose

substrate: short-chain amylose


organism: Paecilomyces variotii

substrate_name: isomaltose

substrate: isomaltose


organism: Penaeus japonicus


organism: Picrophilus oshimae


organism: Rana japonica

substrate_name: amylopectin

substrate: amylopectin


proof_lines:
H118A mutant, 30°C, pH 6.5
above, H118A mutant, 30°C, pH 6.5


organism: Aeromonas sobria

substrate_name: Imipenem; H2O

substrate: Imipenem; H2O


organism: Aeromonas veronii

substrate_name: Unknown

substrate: Unknown


organism: Aeromonas veronii bv. sobria

substrate_name: Imipenem

substrate: Imipenem


organism: Aliivibrio salmonicida

substrate_name: ceftazidime

proof_lines: pH 7.2, 37°C, recombinant enzyme, in presence of NaCl

substrate: ceftazidime


organism: Bacillus anthracis

proof_lines: wild-type inhibitor protein, pH 7.5, 25°C


substrate_name: cephalexin

substrate: cephalexin


organism: Bacillus cereus

substrate_name: cephalosporin C

proof_lines:
beta-lactamase III
pH 7, 20°C
beta-lactamse II

substrate: cephalosporin C


organism: Bacillus licheniformis

proof_lines:
strain 6346/C
strain 749/C
both strains


substrate_name: penicillin G

proof_lines: mutant E166C, carrying 6-bromoacetyl-2-dimethylaminonaphthalene label, pH 7.0, 22°C

substrate: penicillin G


organism: Burkholderia pseudomallei

substrate_name: cephalothin

substrate: cephalothin


organism: Chryseobacterium indologenes

substrate_name: cefazolin

assay_conditions_summary: pH 6.5; buffer 30 mM sodium cacodylate

proof_lines: in 30 mM sodium cacodylate buffer (pH 6.5) plus 0.05 mM ZnSO4

substrate: cefazolin


organism: Citrobacter freundii

substrate_name: meropenem

substrate: meropenem


organism: Elizabethkingia meningoseptica

substrate_name: cefoxitin

substrate: cefoxitin


organism: Enterobacter cloacae

substrate_name: Nitrocefin; H2O

assay_conditions_summary: pH 7; 303.15 K; buffer 50mM sodium phosphate

proof_lines: at 30°C in 50mM sodium phosphate buffer (pH 7.0)

substrate: Nitrocefin; H2O


organism: Escherichia coli

substrate_name: H2O; Nitrocefin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant 71BLA chimeric PGK/BLA

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant 89BLA chimeric PGK/BLA

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant 129BLA chimeric PGK/BLA

substrate: H2O; Nitrocefin


substrate_name: Penicillin G; H2O

assay_conditions_summary: pH 7; 303.15 K; buffer 50 mM phosphate

proof_lines: 30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1

proof_lines: in 50 mM phosphate buffer (pH 7.0), at 30°C

proof_lines: 30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2

substrate: Penicillin G; H2O


substrate_name: H2O; Penicillin G

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant S70C

substrate: H2O; Penicillin G


proof_lines: mutant R61H/E64H/43H, 25°C, pH not specified in the publication


proof_lines: mutant M182T/T195S/A224V, 25°C, pH not specified in the publication


substrate_name: cefotaxime

substrate: cefotaxime


organism: Aeromonas hydrophila

substrate_name: nitrocefin

substrate: nitrocefin


substrate_name: biapenem

substrate: biapenem


proof_lines:
K224Q mutant, 30°C, pH 6.5
above, K224Q mutant, 30°C, pH 6.5


proof_lines:
H263A mutant, 30°C, pH 6.5
above, H263A mutant, 30°C, pH 6.5


proof_lines:
V67I mutant, 30°C, pH 6.5
above, V67I mutant, 30°C, pH 6.5


organism: Achromobacter xylosoxidans

substrate_name: benzylpenicillin

proof_lines: Km above 2 mM, in 100 mM Tris-H2SO4, 300 mM K2SO4 (pH 7.0), at 30°C

substrate: benzylpenicillin


organism: Acinetobacter baumannii

proof_lines: pH 7.2, temperature not specified in the publication, recombinant enzyme


proof_lines: 25°C, pH not specified in the publication, addition of 20 mM sodium bicarbonate, mutant enzyme W165A


substrate_name: Imipenem

proof_lines: 25°C, pH not specified in the publication, without sodium bicarbonate, wild-type enzyme

proof_lines: 25°C, pH not specified in the publication, addition of 20 mM sodium bicarbonate, wild-type enzyme

proof_lines: 25°C, pH not specified in the publication, addition of 20 mM sodium bicarbonate, wild-type 0.85 enzyme

substrate: Imipenem


proof_lines: 25°C, pH not specified in the publication, addition of 20 mM sodium bicarbonate, mutant enzyme W166A

proof_lines: 25°C, pH not specified in the publication, without sodium bicarbonate, mutant enzyme W166A


organism: Acinetobacter baylyi

substrate_name: ampicillin

substrate: ampicillin


substrate_name: cefepime

substrate: cefepime


proof_lines:
wild-type AmpC-B2
wild-type AmpC-A
wild type, pH 7.4, room temperature


organism: Haemophilus ducreyi

substrate_name: Ampicillin; H2O

substrate: Ampicillin; H2O


organism: [Haemophilus] ducreyi


organism: Janthinobacterium lividum

substrate_name: ceftazidime

substrate: ceftazidime


organism: Klebsiella aerogenes

substrate_name: cephaloridine

substrate: cephaloridine


proof_lines: 100 microM nitrocefin as the reporter substrate, TEM-149 mutant T182M, pH 7.0, 25°C


substrate_name: Unknown

substrate: Unknown


substrate_name: cefuroxime

proof_lines:
wild-type, pH 7.0, 22°C
wild type

substrate: cefuroxime


organism: Bacillus sp. (in: firmicutes)

substrate_name: penicillin G

proof_lines:
penicillinase II
penicillinase I

substrate: penicillin G


organism: Bacteroides fragilis

proof_lines: pH and temperature not specified in the publication


organism: Brachyspira pilosicoli

substrate_name: carbenicillin

proof_lines: at 25°C in 100 mM sodium phosphate (pH 7.0)

substrate: carbenicillin


organism: Burkholderia cenocepacia


proof_lines:
mutant AmpC-B2-S287N
mutant AmpC-A-S287N


organism: Fluoribacter gormanii


organism: Fusobacterium nucleatum

substrate_name: CENTA

substrate: CENTA


organism: Mycobacterium tuberculosis

substrate_name: Nitrocefin; H2O

proof_lines:
pH 6.5, 22°C, recombinant enzyme
in 100 mM MES (pH 6.4)
at 30°C

substrate: Nitrocefin; H2O


organism: Mycolicibacterium smegmatis

proof_lines: pH 8.0, 30°C, recombinant wild-type enzyme


substrate_name: Bocillin-FL

substrate: Bocillin-FL


organism: Pectobacterium carotovorum

substrate_name: meropenem

substrate: meropenem


organism: plasmid pBC


organism: plasmid pBG66

substrate_name: cephalexin

proof_lines: pH and temperature not specified in the publication, wild-type enzyme

substrate: cephalexin


proof_lines: pH and temperature not specified in the publication, mutant enzyme N166A/N170G


proof_lines: pH and temperature not specified in the publication, mutant enzyme N170G


proof_lines: pH and temperature not specified in the publication, mutant enzyme N170A


organism: Aspergillus niger

substrate_name: maltose

proof_lines: pH 4.5, 35°C, recombinant mutant S30P/H391Y

substrate: maltose


proof_lines: pH 4.5, 35°C, recombinant mutant S30P/T290A/H391Y


proof_lines: pH 4.5, 35°C, recombinant mutant S30P/T290A


proof_lines: pH 4.5, 35°C, recombinant mutant S30P/T62A/H391Y


substrate_name: starch

proof_lines: 30°C, pH 4.2, glucoamylase immobilized on macroporous silica

substrate: starch


organism: Kluyvera ascorbata

substrate_name: Imipenem

assay_conditions_summary: pH 7; 298.15 K; buffer 0.01 M phosphate

proof_lines: Km above 1.0 mM, in 0.01 M phosphate buffer (pH 7.0), at 25°C

substrate: Imipenem


organism: Laribacter hongkongensis

substrate_name: cephalothin

substrate: cephalothin


organism: Metapseudomonas otitidis

substrate_name: piperacillin

proof_lines: pH not specified in the publication, 30°C, recombinant enzyme

substrate: piperacillin


organism: Moraxella catarrhalis

proof_lines:
enzyme 1, BRO-1
enzyme 2, BRO-2


organism: Morganella morganii


organism: Morganella morganii subsp. morganii

substrate_name: benzylpenicillin

assay_conditions_summary: pH 7; 303.15 K; buffer 20 mM phosphate

proof_lines: in 20 mM phosphate buffer, (pH 7.0) at 30°C

substrate: benzylpenicillin


organism: plasmid pQE32Chl17

substrate_name: cefotaxime

substrate: cefotaxime


organism: plasmid RGN238

substrate_name: cephaloridine

proof_lines: pH and temperature not specified in the publication, OXA-1 beta-lactamase

substrate: cephaloridine


organism: Proteus penneri


organism: Proteus vulgaris


organism: Providencia stuartii

substrate_name: ampicillin

substrate: ampicillin


organism: plasmid pGEM-T-easy

proof_lines: mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate

proof_lines: mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate


proof_lines: mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate

proof_lines: mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate


proof_lines: mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate

proof_lines: mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate


proof_lines: wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate

proof_lines: wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate


proof_lines: mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate


organism: Pseudomonas aeruginosa

substrate_name: Cefdinir; H2O

substrate: Cefdinir; H2O


substrate_name: penicillin G

substrate: penicillin G


organism: Pseudomonas fluorescens

substrate_name: Oxacillin

proof_lines: at 30°C in 50mM sodium phosphate buffer (pH 7.0)

substrate: Oxacillin


organism: Stenotrophomonas maltophilia

proof_lines:
below, mutant D120S, pH 7.0, 25°C
mutant D120S, pH 7.0, 25°C


substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: nitrocefin

proof_lines:
H116C, not applicable Zn(2+) content
H116C with 0.85 equiv of Zn(2+)

substrate: nitrocefin


proof_lines:
wild-type enzyme, pH 7.0, 25°C
wild-typewith 1.90 equiv of Zn(2+)


proof_lines:
H121C with 0.98 equiv of Zn(2+)
H121C, not applicable Zn(2+) content


organism: Streptomyces albus


organism: Pseudomonas luteola

substrate_name: ceftazidime

proof_lines: pH and temperature not specified in the publication

substrate: ceftazidime


organism: Pseudomonas putida

substrate_name: carbenicillin

proof_lines: enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin

proof_lines: inhibitor binding constant (Ki) using 10 microM nitrocefin as indicator substrate

substrate: carbenicillin


organism: Psychrobacter immobilis


organism: Riemerella anatipestifer

substrate_name: cefepime

substrate: cefepime


organism: Serratia fonticola

substrate_name: moxalactam

proof_lines: at 25°C in 50 mM sodium phosphate (pH 7.0)

substrate: moxalactam


organism: Serratia marcescens

proof_lines: wild-type inhibitor protein, pH 7.5, 25°C


organism: Shigella sonnei


organism: Shouchella clausii

proof_lines: kcat less than 0.01/sec at 30°C in 100 mM sodium phosphate (pH 7)

proof_lines: kcat less than 0.3/sec at 30°C in 100 mM sodium phosphate (pH 7)


organism: Shouchella lehensis

substrate_name: ampicilin

substrate: ampicilin


organism: Staphylococcus aureus

proof_lines:
beta-lactamase D
beta-lactamase A
beta-lactamase B


substrate_name: H2O; Cefdinir

proof_lines: lactamase ZnFe-L1, 1.0 Zn(2+), 1.0 Fe(3+)

substrate: H2O; Cefdinir


proof_lines:
below, mutant D120C, pH 7.0, 25°C
mutant D120C, pH 7.0, 25°C


organism: Klebsiella aerogenes

proof_lines: 100 microM nitrocefin as the reporter substrate, TEM-149 wild-type, pH 7.0, 25°C


organism: Klebsiella pneumoniae

substrate_name: Penicillin G; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant M69I

substrate: Penicillin G; H2O


substrate_name: H2O; Penicillin G

assay_conditions_summary: pH 6.8; 313.15 K; buffer 50 mM HEPES

proof_lines:
beta-lactamases CTX-M-26
at 40°C in 50 mM HEPES buffer (pH 6.8)
pH 7.0, 30°C

substrate: H2O; Penicillin G


proof_lines: pH 7.5, 25°C, recombinant His-tagged wild-type enzyme


proof_lines: pH 7.5, 25°C, recombinant His-tagged mutant E162A


proof_lines: pH 7.5, 25°C, recombinant His-tagged mutant E164A


assay_conditions_summary: buffer additive

proof_lines: mutant enzyme D120A, 1 mM Zn(NO3)2 added


proof_lines: mutant enzyme D120E, 1 mM Zn(NO3)2 added


assay_conditions_summary: pH 7; 303.15 K; buffer 50 mM sodium phosphate

proof_lines: at 30°C in 50 mM sodium phosphate buffer (pH 7.0)


organism: Shewanella algae

substrate_name: meropenem

substrate: meropenem


organism: Shewanella frigidimarina

substrate_name: cefalothin

substrate: cefalothin


organism: Shewanella livingstonensis

substrate_name: cefuroxime

substrate: cefuroxime


organism: Streptomyces cacaoi

substrate_name: benzylpenicillin

substrate: benzylpenicillin


organism: Streptomyces sp.


organism: synthetic construct

substrate_name: cephalothin

substrate: cephalothin


organism: Yersinia enterocolitica

substrate_name: cefalotin

substrate: cefalotin


organism: Yersinia ruckeri


enzyme_display_name: RNA helicase

organism: Saccharomyces cerevisiae

substrate_name: H2O; ATP

proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant Q169A

enzyme: RNA helicase

substrate: H2O; ATP


substrate_name: ATP; H2O

proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant F162A

substrate: ATP; H2O


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant T166S


substrate_name: ATP

substrate: ATP


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant F162L


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant T166A


assay_conditions_summary: cofactor ATP

proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant A457D


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant F405Y


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant F405L + P174S


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant F405L + D479N


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant F405L + I348T


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant F405L + A457D


substrate_name: RNA

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

substrate: RNA


assay_conditions_summary: pH 6.5; 303.15 K; cofactor ATP


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant His6-tagged K92A


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant His6-tagged S228A


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant His6-tagged T230A


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant F405L


proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant I348T


substrate_name: Poly(dA)

substrate: Poly(dA)


assay_conditions_summary: pH 6.5; 298.15 K; cofactor ATP


organism: Homo sapiens


assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P06634 and applied mutation signature Q169A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer of 50 mM potassium acetate; cofactor ATP

column_label: Table I (Kinetic parameters for RNA-dependent ATPase activity), enzyme row 'Q169A'; column 'Km (mM)' = 33; column 'Vmax (%wt)' = 29; column 'kcat (min^-1)' = 61; column 'kcat/Km (M^-1 min^-1)' = 1900; column 'Ki (mM)' = ND.

normalized_value_unit_evidence: Km: printed Table I cell 33 under the head Km (mM); mM is already the canonical unit, so no unit conversion applies and the value is 33.0 mM, which is what the catalog carries. kcat: printed Table I cell 61 under the head kcat (min^-1); 1 min^-1 is 1/60 s^(-1), so 61 / 60 = 1.0166666666666666 s^(-1). The catalog carries 1.017 s^(-1), that same conversion written to three decimal places; this pass carries the full-precision conversion of the printed cell. kcat/Km: printed Table I cell 1900 under the head kcat/Km (M^-1 min^-1); 1 M^-1 min^-1 is 0.001 mM^-1 combined with 1/60 s^(-1), that is 1/60000 s^(-1)*mM^(-1), so 1900 / 60000 = 0.03166666666666667 s^(-1)*mM^(-1). The catalog carries 0.030818181818181814 s^(-1)*mM^(-1), the arithmetic quotient 1.017 / 33.0 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy adopted 2026-09-03 carries the printed primary cell on kcat_over_km.

raw_value_unit_evidence: PMID: 15201868; Table I, enzyme row 'Q169A': Km = 33 in a column headed Km (mM); kcat = 61 in a column headed kcat (min^-1); printed kcat/Km = 1900 in a column headed kcat/Km (M^-1 min^-1).

row_label: Table I, enzyme row 'Q169A'

table_label: Table I: Kinetic parameters for RNA-dependent ATPase activity (The EMBO Journal 2004, 23(13):2478-2487). Printed column heads: Km (mM); Vmax (%wt); kcat (min^-1); kcat/Km (M^-1 min^-1); Ki (mM).


assay_conditions_summary: pH 7.5; 303.15 K; buffer used 50 mM potassium acetate; cofactor ATP

column_label: Table I; row WT; columns Km, kcat, and kcat/Km print 0.34 +/- 0.05 mM, 210 +/- 20 min^-1, and 620000 +/- 90000 M^-1 min^-1; these primary cells do not match the OED exported tuple 0.3 mM, 5.667 s^-1, and 18.89 s^-1*mM^-1.

normalized_value_unit_evidence: paper WT Km=0.34 mM; paper WT kcat=3.5 s^-1; paper printed kcat/Km=10.3 s^-1*mM^-1; export expects Km=0.3 mM, kcat=5.667 s^-1, kcat/Km=18.89 s^-1*mM^-1

row_label: WT

table_label: Table I. Kinetic parameters for RNA-dependent ATPase activity


sequence_variant_note: Mutation signature T166S matches the mutant residue at offset +6 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P06634 and applied mutation signature F162A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic parameters for RNA-dependent ATPase activity), enzyme row 'F162A'; column 'Km (mM)' = 3.5; column 'Vmax (%wt)' = 9.3; column 'kcat (min^-1)' = 20; column 'kcat/Km (M^-1 min^-1)' = 5600; column 'Ki (mM)' = ND.

normalized_value_unit_evidence: Km: printed Table I cell 3.5 under the head Km (mM); mM is already the canonical unit, so no unit conversion applies and the value is 3.5 mM, which is what the catalog carries. kcat: printed Table I cell 20 under the head kcat (min^-1); 1 min^-1 is 1/60 s^(-1), so 20 / 60 = 0.3333333333333333 s^(-1). The catalog carries 0.333 s^(-1), that same conversion written to three decimal places; this pass carries the full-precision conversion of the printed cell. kcat/Km: printed Table I cell 5600 under the head kcat/Km (M^-1 min^-1); 1 M^-1 min^-1 is 0.001 mM^-1 combined with 1/60 s^(-1), that is 1/60000 s^(-1)*mM^(-1), so 5600 / 60000 = 0.09333333333333334 s^(-1)*mM^(-1). The catalog carries 0.09514285714285715 s^(-1)*mM^(-1), the arithmetic quotient 0.333 / 3.5 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy adopted 2026-09-03 carries the printed primary cell on kcat_over_km.

raw_value_unit_evidence: PMID: 15201868; Table I, enzyme row 'F162A': Km = 3.5 in a column headed Km (mM); kcat = 20 in a column headed kcat (min^-1); printed kcat/Km = 5600 in a column headed kcat/Km (M^-1 min^-1).

row_label: Table I, enzyme row 'F162A'


sequence_variant_note: Mutation signature Q169E matches the mutant residue at offset -14 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant Q169E


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R376A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; cofactor ATP

column_label: Table 1 | row R376A | columns KM (uM), kcat (min^-1), Relative kcat/KM.

normalized_value_unit_evidence: kcat=0.02666667 s^-1 from 1.6 min^-1 / 60; KM not determined in paper and not required for this row.

raw_value_unit_evidence: Table 1 row R376A: KM (ATP)=ND; kcat=1.6 +/- 0.5 min^-1; Relative kcat/KM=ND.

table_label: Table 1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H375E to reconstruct the assayed variant sequence.

column_label: Table 1 | row H375E | columns KM (uM), kcat (min^-1), Relative kcat/KM.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K389A to reconstruct the assayed variant sequence.

column_label: Table 1 | row K389A | columns KM (uM), kcat (min^-1), Relative kcat/KM.

raw_value_unit_evidence: Table 1 row K389A: KM (ATP)=450 +/- 200 uM; kcat=17 +/- 2 min^-1; Relative kcat/KM=3.06.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K92A/K389A to reconstruct the assayed variant sequence.

column_label: Table 1 | row K92AK389A (K92A/K389A double mutant) | columns KM (uM), kcat (min^-1), Relative kcat/KM.

normalized_value_unit_evidence: kcat=0.01166667 s^-1 from 0.7 min^-1 / 60; KM not determined in paper and not required for this row.

raw_value_unit_evidence: Table 1 row K92AK389A: KM (ATP)=ND; kcat=0.7 +/- 0.1 min^-1; Relative kcat/KM=ND.


column_label: Table 1 | row Has1p | columns KM (uM), kcat (min^-1), Relative kcat/KM.

raw_value_unit_evidence: Table 1 row Has1p: KM (ATP)=440 +/- 90 uM; kcat=5.4 +/- 0.9 min^-1; Relative kcat/KM=1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S228A to reconstruct the assayed variant sequence.

column_label: Table 1 | row S228A | columns KM (uM), kcat (min^-1), Relative kcat/KM.

raw_value_unit_evidence: Table 1 row S228A: KM (ATP)=760 +/- 410 uM; kcat=3.8 +/- 1 min^-1; Relative kcat/KM=0.41.


sequence_source: UniProt REST /uniprotkb/P20448.json


sequence_source: UniProt REST /uniprotkb/C7GTW8.json


sequence_source: UniProt REST /uniprotkb/P20447.json


organism: West Nile virus

sequence_source: UniProt REST /uniprotkb/Q9Q6P4.json

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


organism: Xenopus laevis

substrate_name: H2O; dATP

sequence_source: UniProt REST /uniprotkb/P24346.json

substrate: H2O; dATP


substrate_name: dATP

assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP

substrate: dATP


organism: Venezuelan equine encephalitis virus (strain Trinidad donkey)

substrate_name: a 12 residues substrate for nsp2 protease activity


organism: Kokobera virus

substrate_name: ATPase of serine protease NS3

substrate: ATPase of serine protease NS3


organism: Reovirus type 3 (strain Dearing)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Caenorhabditis elegans


organism: Classical swine fever virus (strain Alfort/Tuebingen)

substrate_name: Sub-UpU

sequence_variant_note: Source notes indicate a mutant or variant enzyme, but no machine-applicable substitution signature was available.

substrate: Sub-UpU


organism: Deformed wing virus

substrate_name: a 15 AA peptide

substrate: a 15 AA peptide


organism: Dengue virus type 2 (strain Puerto Rico/PR159-S1/1969)

substrate_name: N-acetyl-Gly-Arg-Arg-AMC

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

substrate: N-acetyl-Gly-Arg-Arg-AMC


organism: Hepatitis GB virus B

substrate_name: ATP for NS3 NTPase

substrate: ATP for NS3 NTPase


column_label: PMID 12466530 page 5081, biochemical properties prose; substrate ATP; metric Km.

raw_value_unit_evidence: Lineweaver-Burk plot was linear up to ATP concentrations of 100 uM and yielded a Km value of 41.9 uM.

row_label: hSuv3p NTPase/helicase / ATP

table_label: Characterisation of the biochemical properties of the hSuv3p NTPase/helicase


organism: Semliki forest virus

substrate_name: nsP2 RNA triphosphatase activity (at pH 8.0)

assay_conditions_summary: pH 8


organism: Tick-borne encephalitis virus European subtype (strain Neudoerfl)


organism: Venezuelan equine encephalitis virus (strain 3880)

substrate: a 12 residues substrate for nsp2 protease activity


organism: Bamboo mosaic virus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L543A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant NTPase L543A (aa 514-892)

proof_lines: SABIO-RK modifier species: RNA helicase(Enzyme) mutant RNA 5'-triphosphatase L543A (aa 514-892)


sequence_variant_note: Resolved canonical sequence from accession_anchored:O37174 and applied mutation signature Q826A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 293.15 K; cofactor ATP

column_label: Table 2, enzyme row 'Q826A'; ATPase column group: column 'Km (uM)' = 8.7 ± 2.3, column 'kcat (s^-1)' = 0.73 ± 0.07; RNA 5'-triphosphatase column group: column 'Km (uM)' = 120 ± 34, column 'kcat (min^-1)' = 1.0 ± 0.4; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 ATPase cell 0.73 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.73 s^(-1). Km: printed Table 2 ATPase cell 8.7 uM; 8.7 / 1000 = 0.0087 mM. kcat/Km: Table 2 carries no kcat/Km column, so the paper value 83.9080459770115 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.73 / 0.0087 of this row's own two printed ATPase cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row Q826A, ATPase column group: Km = 8.7 ± 2.3 uM; kcat = 0.73 ± 0.07 s^-1; Table 2 carries no kcat/Km column.

row_label: Table 2, enzyme row 'Q826A', ATPase column group

table_label: Table 2: Effects of selected mutations on ATPase and RNA 5'-triphosphatase activities (Virology 2007, 367:41-50)


sequence_variant_note: Resolved canonical sequence from accession_anchored:O37174 and applied mutation signature D858A to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'D858A'; ATPase column group: column 'Km (uM)' = 73 ± 26, column 'kcat (s^-1)' = 6.2 ± 0.7; RNA 5'-triphosphatase column group: column 'Km (uM)' = 220 ± 50, column 'kcat (min^-1)' = 1.2 ± 0.4; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 ATPase cell 6.2 s^-1; already in s^-1, no unit conversion applies; the paper value is 6.2 s^(-1). Km: printed Table 2 ATPase cell 73 uM; 73 / 1000 = 0.073 mM. kcat/Km: Table 2 carries no kcat/Km column, so the paper value 84.93150684931507 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 6.2 / 0.073 of this row's own two printed ATPase cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row D858A, ATPase column group: Km = 73 ± 26 uM; kcat = 6.2 ± 0.7 s^-1; Table 2 carries no kcat/Km column.

row_label: Table 2, enzyme row 'D858A', ATPase column group


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q826A to reconstruct the assayed variant sequence.

assay_conditions_summary: buffer components as described under Materials and methods; cofactor ATP

column_label: Table 2; row Q826A; ATPase Km (uM) and ATPase kcat (s^-1) columns.

normalized_value_unit_evidence: Km=0.0087 mM from 8.7 uM; kcat=0.73 s^-1 directly from ATPase kcat column.

raw_value_unit_evidence: Table 2 reports ATPase Km 8.7 +/- 2.3 uM and kcat 0.73 +/- 0.07 s^-1 for Q826A.

table_label: Table 2. Effects of selected mutations on ATPase and RNA 5'-triphosphatase activities


sequence_variant_note: Resolved canonical sequence from accession_anchored:O37174 and applied mutation signature L543A to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'L543A'; ATPase column group: column 'Km (uM)' = 150 ± 45, column 'kcat (s^-1)' = 4.6 ± 0.6; RNA 5'-triphosphatase column group: column 'Km (uM)' = 82 ± 23, column 'kcat (min^-1)' = 1.2 ± 0.2; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 ATPase cell 4.6 s^-1; already in s^-1, no unit conversion applies; the paper value is 4.6 s^(-1). Km: printed Table 2 ATPase cell 150 uM; 150 / 1000 = 0.15 mM. kcat/Km: Table 2 carries no kcat/Km column, so the paper value 30.666666666666664 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 4.6 / 0.15 of this row's own two printed ATPase cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row L543A, ATPase column group: Km = 150 ± 45 uM; kcat = 4.6 ± 0.6 s^-1; Table 2 carries no kcat/Km column.

row_label: Table 2, enzyme row 'L543A', ATPase column group


column_label: Table 1, substrate row 'ATP'; column 'Km (uM)' = 150; column 'kcat (s^-1)' = 67; column 'kcat/Km (uM^-1 s^-1)' = 0.45.

normalized_value_unit_evidence: kcat: printed Table 1 cell 67 s^-1; already in s^-1, no unit conversion applies; the paper value is 67.0 s^(-1). Km: printed Table 1 cell 150 uM; 150 / 1000 = 0.15 mM. kcat/Km: printed Table 1 cell 0.45 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.45 x 1000 = 450.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row ATP: Km = 150 uM; kcat = 67 s^-1; printed kcat/Km = 0.45 uM^-1 s^-1.

row_label: Table 1, substrate row 'ATP'

table_label: Table 1: Kinetic parameters of NTP hydrolysis catalyzed by wild-type helicase-like domain of BaMV replicase (Virology 2007, 367:41-50)

unit: Mswedgeone


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D858A to reconstruct the assayed variant sequence.

column_label: Table 2; row D858A; ATPase Km (uM) and ATPase kcat (s^-1) columns.

normalized_value_unit_evidence: Km=0.073 mM from 73 uM; kcat=6.2 s^-1 directly from ATPase kcat column.

raw_value_unit_evidence: Table 2 reports ATPase Km 73 +/- 26 uM and kcat 6.2 +/- 0.7 s^-1 for D858A.


organism: Hepacivirus C


organism: Dengue virus type 2 (strain Thailand/NGS-C/1944)

substrate_name: triphosphorylated RNA

proof_lines: Vmax with 0.65 nmol/s/ug enzyme for RTPase activity with triphosphorylated RNA as substrate.

substrate: triphosphorylated RNA


organism: Homo sapiens

substrate_name: ATP (in the absence of nucleic acid)

proof_lines: kcat is 14 min(-1) for ATP hydrolysis in the absence of nucleic acid (PubMed:17357160). kcat is 36 min(-1) for ATP hydrolysis in the presence of ssDNA oligonucleoside dA200 (PubMed:17357160). kcat is 1.6 min(-1) for ATP hydrolysis in the ab

substrate: ATP (in the absence of nucleic acid)


proof_lines: kcat is 1.9 min(-1) for ATP hydrolysis in the absence of nucleic acid (PubMed:21589879). kcat is 3.8 min(-1) for ATP hydrolysis in the presence of RNA oligo(rU)20 (PubMed:21589879). kcat is 2.1 min(-1) for ATP hydrolysis in the presence of


organism: Severe acute respiratory syndrome coronavirus

substrate_name: peptide TSAVLQSGFRK-NH(2)

proof_lines: The kinetic parameters are studied for the 3C-like proteinase domain.

substrate: peptide TSAVLQSGFRK-NH(2)


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)


enzyme_display_name: non-chaperonin molecular chaperone ATPase

substrate_name: ATP (at 2.5 mM potassium acetate)

proof_lines: kcat is 0.95 min(-1) with ATP as substrate (at 2.5 mM potassium acetate) and 0.81 min(-1) with ATP as substrate (at 100 mM potassium acetate).

substrate: ATP (at 2.5 mM potassium acetate)


organism: Saccharomyces cerevisiae

substrate_name: H2O; ATP

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

mutation_type: deletion

proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Hsp104delta38 (C-terminal)

substrate: H2O; ATP


substrate_name: ATP; H2O

mutation_signature: Δ4

proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Hsp104delta4 (C-terminal)

substrate: ATP; H2O


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Hsp104 T317A


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Hsp104 Y819W


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Hsp104 R826M


substrate_name: ATP

enzyme: non-chaperonin molecular chaperone ATPase

substrate: ATP


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant E645K


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Y662A


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Y662F


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: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Y662K


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Y662W


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant K620T


proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant E285Q


sequence_variant_note: Mutation signature K218T matches the mutant residue at offset +0 and the reference residue at offset -13; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant K218T


sequence_variant_note: Mutation signature E687Q matches the mutant residue at offset +0 and the reference residue at offset +2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant E687Q


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Δ22 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant Hsp104delta22 (C-terminal)


organism: Escherichia coli


sequence_variant_note: Mutation signature K220T matches the mutant residue at offset +1 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: non-chaperonin molecular chaperone ATPase(Enzyme) mutant ClpAT K220T


organism: Pseudomonas aeruginosa