organism: Thermococcus litoralis

proof_lines: pH 7.5, 37°C, dNTP incorporation opposite DNA lesions, template: abasic site

proof_lines: pH 7.5, 37°C, dNTP incorporation opposite DNA lesions, template base: O6-MeG

proof_lines: pH 7.5, 37°C, dNTP incorporation opposite DNA lesions, template base: O6-BzG


enzyme_display_name: DNA-directed DNA polymerase

substrate_name: dCTP

source_db: brenda

ki_display: Not reported

kcat_over_km_display: Not reported

source_license: CC BY 4.0

km_unit: mM

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

proof_lines: pH 7.5, 37°C, dNTP incorporation opposite DNA lesions, template base: G

proof_lines: pH 7.5, 37°C, dNTP incorporation opposite DNA lesions, template base: N2-MeG

enzyme: DNA-directed DNA polymerase

substrate: dCTP

source: brenda


substrate_name: dATP

substrate: dATP


substrate_name: dGTP

substrate: dGTP


enzyme_display_name: hexokinase

organism: Ascaris suum

substrate_name: D-glucose

kcat_display: Not reported

mutation_signature: Unknown

enzyme: hexokinase

substrate: D-glucose


substrate_name: D-fructose

substrate: D-fructose


substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Entamoeba histolytica

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

proof_lines:
recombinant HXK1, at 30°C, pH 8
recombinant HXK2, at 30°C, pH 8


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines:
recombinant HXK2, at 30°C, pH 8
recombinant HXK1, at 30°C, pH 8

substrate: Unknown


organism: Aspergillus niger

assay_conditions_summary: pH 7.8; 303.15 K; cofactor ATP


substrate_name: GTP

substrate: GTP


proof_lines:
pH 7.8, 30°C, at 0.5 mM ATP
pH 7.8, 30°C, at 0.1 mM ATP
pH 7.8, 30°C


organism: Bos taurus

smiles: C(C=O)C(C(C(CO)O)O)O


smiles: C(C(C(C(C(C=O)F)O)O)O)O


organism: Crassostrea virginica

assay_conditions_summary: pH 7.9; 297.15 K; cofactor ATP


substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


organism: Homo sapiens

mutation_type: substitution


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: wild type enzyme, at 25°C, in the presence of 0.02 mM activator LY-2121260

proof_lines: wild type enzyme, at 25°C, in the presence of 0.02 mM activator N-[2-amino-4-fluoro-5-[(1-methyl-1H-imidazol-2-yl)sulfanyl]benzyl]-1,3-thiazol-2-amine


proof_lines:
wild-type enzyme
30°C, pH 7.5, wild-type


proof_lines: glucokinase with C-terminal 10 alanine addition

proof_lines: glucokinase with C-terminal 5 alanine addition

proof_lines: recombinant hexokinase I expressed in Escherichia coli


mutation_signature: truncated enzyme with removed helix alpha13 truncated enzyme with removed helix alpha13

mutation_type: truncation


protein_accession_database: UniProt

sequence_source: UniProtKB:P35557 canonical sequence with D205A reconstructed during review

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

proof_lines: mutant enzyme D205A, kcat less than 0.00091 s-1

data_origin: experimental


organism: Solanum tuberosum

substrate_name: D-mannose

substrate: D-mannose


organism: Sus scrofa

substrate_name: D-Fructose 6-phosphate; ATP

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

assay_conditions_summary: pH 7; cofactor ATP

substrate: D-Fructose 6-phosphate; ATP


assay_conditions_summary: pH 8; cofactor ATP


assay_conditions_summary: pH 7


organism: Sulfolobus acidocaldarius

proof_lines: pH and temperature not specified in the publication


organism: Thermus aquaticus

substrate_name: dTTP

substrate: dTTP


organism: Streptococcus pneumoniae

substrate_name: primed M13

proof_lines: exonuclease activity, wild-type, pH 7.6, 37°C

substrate: primed M13


assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines: polymerase activity, D190A mutant, pH 7.6, 37°C


proof_lines: exonuclease activity, D190A mutant, pH 7.6, 37°C


mutation_signature: a truncate HK I form lacking the first 11 amino acids named HK-11aa / a truncate HK I form lacking the first 11 amino acids named HK-11aa

sequence_source: UniProt P19367 FASTA reconstructed as HK-11aa using PMID 9879670

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines: MgATP2-, recombinant HK I, a truncate HK I form lacking the first 11 amino acids named HK-11aa, and the 50 kDa C-terminal half of HK I, at 37°C, pH 7.2


proof_lines: recombinant HK I, a truncate HK I form lacking the first 11 amino acids named HK-11aa, and the 50 kDa C-terminal half of HK I, at 37°C, pH 7.2


organism: Saccharomyces cerevisiae

verification_status: unverified

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

status: unverified


substrate_name: rCTP

substrate: rCTP


organism: Triticum aestivum

assay_conditions_summary: pH 7.9; cofactor ATP


organism: Anguilla anguilla


organism: Citrus x paradisi

assay_conditions_summary: pH 7.5; cofactor ATP


proof_lines:
pH 7.5, theoretical value
pH 7.5


assay_conditions_summary: pH 6.8; 303.15 K; cofactor ATP


organism: Aquarana catesbeiana


organism: Clostridium pasteurianum


assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


substrate_name: K+

substrate: K+


organism: Cyprinus carpio


organism: Escherichia coli

kcat_over_km_origin: calculated

sequence_source: UniProtKB:P06999 direct lookup

assay_conditions_summary: pH 8.2; 303.15 K; cofactor ATP

proof_lines: wild type enzyme, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication

proof_lines: wild type enzyme, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication


assay_conditions_summary: pH 8.2; cofactor ATP


substrate_name: beta-D-glucose

proof_lines: co-substrate: ATP, mutant W167F/W257F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication

proof_lines: co-substrate: ATP, mutant W167F/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: co-substrate: ATP, mutant W167F/W257F in the presence of 20-30% glycerol and in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication

substrate: beta-D-glucose


proof_lines: mutant W167F/W257F, pH and temperature not specified in the publication

proof_lines: mutant W167F/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: mutant W167F/W257F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication


organism: Lactococcus lactis

sequence_source: UniProtKB:P0DOB6; direct UniProt JSON check links PMID 6218377 and DOI 10.1016/s0076-6879(82)90109-4 to strain C10 phosphofructokinase function/biophysical evidence

proof_lines:
pH 7.5
ATP in form of MgATP2-


organism: Geobacillus anatolicus

sequence_source: UniProtKB:Q0PL69 / NCBI Protein ABG80522.1; GF C-terminal 592-aa fragment reconstructed from Q0PL69 residues 287-878 using PMID 22652043 method context

proof_lines:
pH 8.0, 50°C, recombinant enzyme
pH 8.0, 37°C, recombinant enzyme


proof_lines:
pH 8.0, 50°C, recombinant enzyme
pH 8.0, 22°C, recombinant enzyme
pH 8.0, 37°C, recombinant enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UGP5 and applied mutation signature Y505A to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme Y505A
37°C, pH 7.0, mutant enzyme Y505A


organism: Rattus norvegicus


substrate_name: D-glucosamine

substrate: D-glucosamine


organism: Ricinus communis

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

proof_lines:
pH 7.0, 25°C, chloroplasr PFK
pH 8.0, 25°C, cytosolic PFK
pH 7.0, 25°C, cytosolic PFK


substrate_name: fructose 6-phosphate

smiles: C(C(C(C(C(=O)CO)O)O)O)OP(=O)(O)O

substrate: fructose 6-phosphate


organism: Mus musculus

sequence_source: UniProtKB:P52792 direct follow-up; paper-linked Gck/GK identity from PMID 17353190

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


assay_conditions_summary: pH 8.4; cofactor ATP

proof_lines: 12 h after isoproterenol administration, PFK-1


organism: Saccharolobus solfataricus

substrate_name: dATP

proof_lines:
template base: dA, pH 7.5, 37°C
pH 7.5, 25°C
template base: dX, pH 7.5, 37°C

substrate: dATP


substrate_name: dCTP

proof_lines: template base: 2-fluoro-2-deoxyinosine, pH 7.5, 37°C

substrate: dCTP


organism: Oryza sativa

sequence_variant_note: Resolved canonical sequence from UniProt REST Q6Z4T5 canonical sequence with D362A substitution applied during review and applied mutation signature D362A to reconstruct the assayed variant sequence.

proof_lines: 37°C, pH 7.5, mutant enzyme D362A, substitution opposite the template G


sequence_source: UniProt REST Q6Z4T5 canonical sequence checked during review

proof_lines: 37°C, pH 7.5, wild-type enzyme, substitution opposite the template G

proof_lines: 37°C, pH 7.5, wild-type enzyme, substitution opposite the template A


substrate_name: dGTP

proof_lines:
pH 7.5, 25°C
template base: dX, pH 7.5, 37°C
template base: dA, pH 7.5, 37°C

substrate: dGTP


proof_lines: template base: 2-bromo-2-deoxyinosine, pH 7.5, 37°C


substrate_name: D-glucose

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP

proof_lines:
pH 7.5, 22°C, immobilized enzyme
pH 7.5, 22°C, soluble enzyme
pH 7.5, 22°C

substrate: D-glucose


substrate_name: ATP

substrate: ATP


organism: Thermoplasma acidophilum


organism: Trypanosoma cruzi


substrate_name: Unknown

assay_conditions_summary: cofactor ATP

proof_lines: varied substrate is D-glucose, in the presence of 1 mM ATP and 3 mM MgCl2, Kis

proof_lines: varied substrate is D-glucose, in the presence of 1 mM ATP and 3 mM MgCl2, Kii

proof_lines: varied substrate is ATP, in the presence of 2 mM D-glucose and 3 mM MgCl2, Kis

substrate: Unknown


organism: Vigna mungo


organism: Streptococcus thermophilus

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


organism: Trypanosoma brucei

assay_conditions_summary: pH 7.4; cofactor ATP

proof_lines: pH and temperature not specified in the publication

proof_lines: pH 7.4, temperature not specified in the publication

proof_lines: pH 6.5, temperature not specified in the publication


organism: Sporolactobacillus inulinus

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP


organism: Thermus aquaticus

substrate_name: deoxynucleoside triphosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P19821 canonical sequence with G418K/E507Q reconstructed during review and applied mutation signature G418K/E507Q to reconstruct the assayed variant sequence.

substrate: deoxynucleoside triphosphate


sequence_source: UniProtKB:P19821 canonical sequence


organism: African swine fever virus


organism: Bos taurus

proof_lines:
pH 7.2, 37°C
polymerase delta, pH 7.5, 37°C
pH 7.5, 37°C


substrate_name: 2-Deoxyglucose; ATP

proof_lines: inhibition of fructose phosphorylation, at 37°C, pH 7.4

substrate: 2-Deoxyglucose; ATP


organism: Bacillus subtilis

substrate_name: DNA; Deoxynucleoside triphosphate

substrate: DNA; Deoxynucleoside triphosphate


organism: Dictyostelium discoideum

proof_lines: wild type enzyme, at pH 7.0 in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2 and 25°C


organism: Eimeria tenella

substrate_name: D-fructose

substrate: D-fructose


organism: Homo sapiens

sequence_source: UniProt P35557 canonical sequence, directly checked and reconstructed with V62Q substitution


substrate_name: dTTP; DNA

proof_lines: DNA polymerase lambda, in 50 mM Tris-HCl (pH 7.5), 1 mM dithiothreitol, 50% (v/v) glycerol, and 0.1 mM EDTA, at 37°C

substrate: dTTP; DNA


organism: Escherichia coli

substrate_name: dATP; DNA

proof_lines:
pol I
pol III
pol II

substrate: dATP; DNA


assay_conditions_summary: pH 8

proof_lines:
wild type hexokinase II
pH 8.0, wild-type enzyme


sequence_source: UniProtKB:P08237 canonical sequence

proof_lines: wild type enzyme, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: wild type enzyme, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


organism: Drosophila melanogaster

substrate_name: 2'-deoxyguanosine triphosphate

verification_status: corrected

sequence_source: UniProtKB reviewed Q27607 (DPOG1_DROME), direct UniProt REST FASTA lookup on 2026-05-25

assay_conditions_summary: pH 7.6; 303.15 K; buffer matches the PMID 18056280 Pol gamma primer-extension assay

proof_lines: in 50 mM Tris-HCl (pH 7.6), 100 mM KCl, 5 mM MgCl2, 10% (v/v) glycerol, 1 mM dithiothreitol, at 30°C

substrate: 2'-deoxyguanosine triphosphate

status: corrected


substrate_name: D-Glucose; ATP

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines: catalytically active recombinant carboxyl-domain of hexokinase III, at 37°C, pH 7.2

proof_lines: hexokinase III from lymphocytes, at 37°C, pH 7.2

proof_lines: hexokinase Ia, Ib and Ic, at 37°C, pH 7.2

substrate: D-Glucose; ATP


assay_conditions_summary: pH 8.1; 310.15 K; cofactor ATP

proof_lines: hexokinase III from lymphocytes, at 37°C, pH 8.1

proof_lines: MgATP2-, hexokinases Ia, Ib and Ic, at 37°C, pH 7.2

proof_lines: catalytically active recombinant carboxyl-domain of hexokinase III, at 37°C, pH 8.1


substrate_name: D-fructose 6-phosphate

proof_lines:
pH 8.0, 25°C, erythrocyte PFK
pH 7.1, 25°C, M-type PFK

substrate: D-fructose 6-phosphate


organism: Kluyveromyces lactis

proof_lines: pH 7.15, 25°C, in the presence of 1 mM AMP

proof_lines: pH 7.15, 25°C, in the presence of 0.1 mM fructose 2,6-bisphosphate


organism: Mus musculus


substrate_name: ATP; D-Fructose 6-phosphate

assay_conditions_summary: pH 7.2; 298.15 K; cofactor ATP

proof_lines: pH 7.2, 25°C, mammary gland and ascites tumor PFK

substrate: ATP; D-Fructose 6-phosphate


substrate_name: ATP; D-Glucose

substrate: ATP; D-Glucose


organism: Oncorhynchus mykiss

assay_conditions_summary: pH 7.2; 295.15 K; cofactor ATP


organism: Rattus norvegicus

proof_lines:
HK I, at 25°C, pH 7.4
HK II, at 25°C, pH 7.4


substrate_name: fructose 6-phosphate

substrate: fructose 6-phosphate


organism: Oryctolagus cuniculus

substrate_name: N-acetyl-D-glucosamine

substrate: N-acetyl-D-glucosamine


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines:
at 30°C, pH 7.5
hexokinase III
hexokinase C


assay_conditions_summary: pH 7.1; cofactor ATP


enzyme_display_name: CDQ83_07225 C.ts A/GTP-PFK

organism: Clostridium thermosuccinogenes

assay_conditions_summary: pH 7; 328.15 K; cofactor ATP

enzyme: CDQ83_07225 C.ts A/GTP-PFK


substrate_name: ATP; Glucose

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: hexokinase C, versus ATP, at 0.2 mM glucose

substrate: ATP; Glucose


proof_lines: DNA polymerase beta, in 50 mM Tris-HCl (pH 7.5), 1 mM dithiothreitol, 50% (v/v) glycerol, and 0.1 mM EDTA, at 37°C


substrate_name: D-mannose

proof_lines:
at 30°C, pH 7.5
hexokinase C
hexokinase II

substrate: D-mannose


proof_lines:
rat brain enzyme, hexokinase I
HKI, at 25°C, pH 7.4
rat liver enzyme, hexokinase IV


organism: Saccharomyces cerevisiae

substrate_name: ATP; 6-Aminoglucose

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines:
glucokinase
hexokinase PI
hexokinase PII

substrate: ATP; 6-Aminoglucose


organism: Saccharolobus solfataricus

substrate_name: North-methanocarba-dATP

substrate: North-methanocarba-dATP


organism: Solanum tuberosum

substrate_name: Unknown

assay_conditions_summary: pH 7

proof_lines:
pH 7, hexokinase 1
HK1, at pH 7
HK2

substrate: Unknown


organism: Spinacia oleracea

assay_conditions_summary: pH 7.7; 298.15 K; cofactor ATP


organism: Sulfolobus acidocaldarius

substrate_name: dTTP

proof_lines: pH and temperature not specified in the publication

substrate: dTTP


substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Sus scrofa

assay_conditions_summary: pH 8.1; 303.15 K; cofactor ATP


organism: Sparus aurata

proof_lines: Ki(slope) Ki(intercept)


assay_conditions_summary: pH 7; cofactor ATP

proof_lines: purified enzyme, at pH 7.0, in the absence of D-fructose 2,6-bisphosphate

proof_lines: purified enzyme, at pH 7.0, in the presence of 0.005 mM D-fructose 2,6-bisphosphate


organism: Thermus thermophilus


organism: Triticum aestivum


organism: Trypanosoma cruzi

substrate_name: D-fructose

substrate: D-fructose


enzyme_display_name: DNA polymerase I

organism: Thermotoga petrophila

sequence_variant_note: Resolved canonical sequence from UniProtKB:E2RWL8 / GenPept:BAJ23222.1 reconstructed as L329A from PMID:23026053 and applied mutation signature L329A to reconstruct the assayed variant sequence.

proof_lines: pH 8.2, 50 C, recombinant enzyme mutant K4polL329A

enzyme: DNA polymerase I


organism: Thermococcus pacificus

substrate_name: deoxynucleoside triphosphate

proof_lines: pH 7.5, 75°C, turnover number of each nucleotide in an equimolar mixture of the four nucleotides, unmodified Tpa DNA polymerase

proof_lines: pH 7.5, 75°C, turnover number of each nucleotide in an equimolar mixture of the four nucleotides, fusion protein of the Sso7d protein to the C-terminus of Tpa DNA polymerase

proof_lines: pH 7.5, 75°C, mol of template, in the presence of an excess of annealed primer, unmodified Tpa DNA polymerase

substrate: deoxynucleoside triphosphate


sequence_source: UniProtKB Q5SJ64, Thermus thermophilus HB8 DNA polymerase beta / PolX / TTHA1150

proof_lines:
pH 9.0, 25°C
in the absence of dNTPs
in the presence of dNTPs


organism: Zea mays

proof_lines:
non-cytosolic hexokinase from root
root, non-cytosolic enzyme
non-cytoslic hexokinase from root


organism: Escherichia coli

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

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant I126A


substrate_name: D-Fructose 6-phosphate; ATP

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant R72H

substrate: D-Fructose 6-phosphate; ATP


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant Y41A


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant Y41F


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant Y41W


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant Y41L


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant F76A


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant F76Y


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant F76W


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant M169L


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant M169A


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant R252Q


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant D127S:R252Q


organism: Gallus gallus


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant R111A


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant R111E


substrate_name: ITP; D-Fructose 6-phosphate

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant R77D

substrate: ITP; D-Fructose 6-phosphate


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant


organism: Lactococcus lactis subsp. lactis


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant Lac- Gal d


organism: Rana catesbeiana


organism: Canis familiaris

substrate_name: Glucose; ATP

substrate: Glucose; ATP


organism: Nicotiana tabacum

sequence_source: UniProtKB Q6Q8A5 direct REST lookup; entry is HXK2_TOBAC/NtHxK2, EC 2.7.1.1, organism Nicotiana tabacum, PubMed ID 15670855.


organism: Salmo salar


organism: Drosophila melanogaster

substrate_name: D-Glucose; ATP

substrate: D-Glucose; ATP


organism: Ustilago maydis


organism: Bos taurus


organism: Chlorocebus sp.


organism: Crassostrea virginica


organism: Lactobacillus casei


organism: Sus scrofa


organism: Mytilus galloprovincialis

substrate_name: ATP; D-Fructose 6-phosphate

substrate: ATP; D-Fructose 6-phosphate


organism: Plasmodium falciparum


organism: Musa acuminata


organism: Oncorhynchus mykiss


organism: Mustela vison


organism: Saccharomyces cerevisiae

substrate_name: ATP; beta-D-Fructose 6-phosphate

substrate: ATP; beta-D-Fructose 6-phosphate


organism: Saccharomyces pastorianus


organism: Ricinus communis


organism: Saccharum officinarum


organism: Enterococcus faecalis

substrate_name: DNA; Deoxynucleoside triphosphate

substrate: DNA; Deoxynucleoside triphosphate


organism: Thermus sp.


enzyme_display_name: exo-alpha-sialidase

organism: Clostridium chauvoei

substrate_name: fetuin

enzyme: exo-alpha-sialidase

substrate: fetuin


organism: Clostridium perfringens


organism: Corynebacterium diphtheriae

substrate_name: alpha-sialyllactose

substrate: alpha-sialyllactose


organism: Corynebacterium ulcerans

substrate_name: sialyllactose

substrate: sialyllactose


organism: Entamoeba histolytica


organism: Actinomyces viscosus


organism: Akkermansia muciniphila

proof_lines:
isoform Am0705, at pH 6.5 and 37°C
isoform Am0707, at pH 6.5 and 37°C
isoform Am2085, at pH 6.5 and 37°C


organism: Arthrobacter sp.

substrate_name: N-acetylneuraminyllactose

substrate: N-acetylneuraminyllactose


organism: Aspergillus fumigatus


organism: Bifidobacterium bifidum


organism: Bos taurus


organism: Staphylococcus aureus

substrate_name: Deoxynucleoside triphosphate; DNA

substrate: Deoxynucleoside triphosphate; DNA


organism: Erysipelothrix rhusiopathiae


organism: Homo sapiens

substrate_name: ganglioside GD1b

proof_lines: 37°C, pH 5.6 or 7.0, without Triton X-100

proof_lines: 37°C, pH 5.6 or 7.0 activated by 0.02% Triton X-100

substrate: ganglioside GD1b


organism: Human respirovirus 1


organism: influenza A virus


organism: influenza A virus H1N1

proof_lines: mutant enzyme D199E, at 37°C, pH not specified in the publication


organism: unidentified influenza virus

proof_lines: mutant enzyme R152K, at 37°C, pH not specified in the publication


proof_lines: mutant enzyme R152K/V94I, at 37°C, pH not specified in the publication


proof_lines: mutant enzyme R368K, at 37°C, pH not specified in the publication


proof_lines:
recombinant head domain, pH 6.5, 37°C
at pH 7.4 and 37°C
predicted Ki value


organism: Vibrio cholerae serotype O1


enzyme_display_name: mandelate racemase

organism: Pseudomonas putida

substrate_name: (R)-mandelate

proof_lines:
25°C, pH 7.5, mutant enzyme N197A
mutant N197A

enzyme: mandelate racemase

substrate: (R)-mandelate


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Sphingobacterium multivorum


organism: Sphingobacterium sp. HMA12


organism: Streptococcus oralis

substrate_name: alpha1-Acid glycoprotein

substrate: alpha1-Acid glycoprotein


organism: Streptococcus pneumoniae


organism: Streptococcus sp.

substrate_name: bovine submaxillary mucin

substrate: bovine submaxillary mucin


organism: Paraclostridium sordellii


organism: Pasteurella multocida


organism: Photobacterium damselae


organism: Porphyromonas gingivalis

sequence_source: UniProt Q7MX62 direct lookup for PG_0352

proof_lines: in the presence of 200 mM NaCl, at pH 7.4 and 20Â°C

proof_lines: in the absence of NaCl, at pH 7.4 and 20Â°C

proof_lines: in the presence of 200 mM NaCl, at pH 5.6 and 20Â°C


organism: Rattus norvegicus

proof_lines:
glomeruli
cortex
intralysosomal sialidase


organism: Respirovirus muris


organism: Sus scrofa


organism: Trichomonas vaginalis


organism: Trypanosoma cruzi


substrate_name: 4-nitrophenyl alpha-sialoside

substrate: 4-nitrophenyl alpha-sialoside


organism: Trypanosoma evansi

proof_lines: pH 6.5, 37°C, versus 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid


organism: Trypanosoma vivax


organism: unidentified influenza virus


proof_lines: wild type enzyme, at 37°C, pH not specified in the publication


proof_lines: mutant enzyme V94I, at 37°C, pH not specified in the publication


organism: Pseudomonas putida

substrate_name: (S)-2-Hydroxy-3-butenoic acid

sequence_source: UniProtKB:P11444 direct EC+organism lookup; reviewed mandelate racemase for Pseudomonas putida with BRENDA EC 5.1.2.2 cross-reference

proof_lines:
in presence of 1 mM Mg2+
4-chloro-D-mandelate
L-mandelate

substrate: (S)-2-Hydroxy-3-butenoic acid


sequence_source: UniProtKB:P11444 direct EC+organism lookup; PubMed/UniProt evidence links PMIDs 7893689 and 7893690 to mandelate racemase catalytic activity

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


sequence_source: Reconstructed E317Q from UniProtKB:P11444 canonical sequence after confirming residue 317 is E; PubMed 7893689 describes the E317Q mutant

sequence_variant_note: Mutation signature E317Q matches the mutant residue at offset +0 and the reference residue at offset +10; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines:
mutant E317Q
E317Q mutant


substrate_name: (S)-Mandelate

sequence_source: Reconstructed K166R from UniProtKB:P11444 canonical sequence after confirming residue 166 is K; PubMed 7893690 describes the K166R mutant

sequence_variant_note: Mutation signature K166R 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.

substrate: (S)-Mandelate


organism: influenza A virus H1N1

proof_lines: mutant enzyme P458T, at 37°C, pH not specified in the publication


organism: influenza B virus

substrate_name: Unknown

substrate: Unknown


organism: Micromonospora viridifaciens


organism: Oryctolagus cuniculus


organism: Paenarthrobacter ureafaciens

substrate_name: dipalmitoyl phosphatidylethanolamine-ganglioside GM1 conjugate

proof_lines:
at pH 5.5 and 37°C
strain dependent


enzyme_display_name: acetylcholinesterase

organism: Homo sapiens

substrate_name: Acetylthiocholine

source_db: oed

sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical FASTA with row-specific mutation reconstruction using paper-numbered residue offset +31. and applied mutation signature W86A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

smiles: CC(=O)SCC[N+](C)(C)C

enzyme: acetylcholinesterase

substrate: Acetylthiocholine

source: oed


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical FASTA with row-specific mutation reconstruction using paper-numbered residue offset +31. and applied mutation signature Y124A/E285A/W286A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical FASTA with row-specific mutation reconstruction using paper-numbered residue offset +31. and applied mutation signature Y72A/Y124A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical FASTA with row-specific mutation reconstruction using paper-numbered residue offset +31. and applied mutation signature E285A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


substrate_name: Propionylthiocholine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical FASTA with row-specific mutation reconstruction using paper-numbered residue offset +31. and applied mutation signature Y337F with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

smiles: CCCC(=O)SCC[N+](C)(C)C

substrate: Propionylthiocholine


substrate_name: Butyrylthiocholine

sequence_source: UniProtKB:P22303 canonical FASTA checked; row-specific variant sequence not reconstructed.

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

substrate: Butyrylthiocholine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical FASTA with row-specific mutation reconstruction using paper-numbered residue offset +31. and applied mutation signature F295L/F297V with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


substrate_name: S-Propyl thioacetate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical FASTA with row-specific mutation reconstruction using paper-numbered residue offset +31. and applied mutation signature W286A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

smiles: CCCSC(C)=O

substrate: S-Propyl thioacetate


substrate_name: propionylthiocholine

substrate: propionylthiocholine


substrate_name: acetylthiocholine, Acetylthiocholine

substrate: acetylthiocholine, Acetylthiocholine


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

column_label: Table 2. Kinetic parameters of BChE, AChE, and CocH1 against 6-MAM Table 2, 6-MAM row, enzyme column AChE; column 'K_M (uM)' = 259; column 'kcat (min^-1)' = 7.078; column 'k_cat/K_M (min^-1 M^-1)' = 2.73 x 10^4.

normalized_value_unit_evidence: Km: printed cell 259 uM converts to 0.259 mM; the exported value is 0.259 mM. kcat: printed cell 7.078 min^-1 converts to 0.11796666666666666 s^(-1); the exported value is 118.0 s^(-1). kcat/Km: printed cell 2.73 x 10^4 min^-1 M^-1 converts to 0.455 s^(-1)*mM^(-1); the exported value is 455.5984555984556 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2. Kinetic parameters of BChE, AChE, and CocH1 against 6-MAM Table 2, 6-MAM row, enzyme column AChE: Km = 259 uM; kcat = 7.078 min^-1; printed kcat/Km = 2.73 x 10^4 min^-1 M^-1.

row_label: Table 2, 6-MAM row, enzyme column AChE


substrate_name: heroin

verification_status: verified

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

column_label: Table 1: Kinetic parameters of BChE, AChE, and CocHl against heroin (Chem Biol Interact 2018, 293:107-114); printed column heads Enzyme | kcat (min^-1) | KM (uM) | kcat/KM (min^-1 M^-1) | RCE | R2. Table 1, enzyme row 'AChE' (wild-type human acetylcholinesterase), substrate heroin; column kcat (min^-1) = 2100; column KM (uM) = 2170; column kcat/KM (min^-1 M^-1) = 9.68 x 10^5; column RCE = 0.06; column R2 = 0.997. captured primary segment: AChE | kcat 2100 min^-1 | KM 2170 uM | kcat/KM 9.68 x 10^5 min^-1 M^-1 | RCE 0.06 | R2 0.997

normalized_value_unit_evidence: kcat: printed Table 1 kcat cell 2100 min^-1; 1 min^-1 is 1/60 s^-1, so 2100 / 60 = 35.0 s^(-1); the exported value is 35.0 s^(-1). Km: printed Table 1 KM cell 2170 uM; 1 uM is 1/1000 mM, so 2170 / 1000 = 2.17 mM; the exported value is 2.17 mM. kcat/Km: printed Table 1 kcat/KM cell 9.68 x 10^5 min^-1 M^-1; 1 min^-1 M^-1 is 1/60000 s^-1 mM^-1, so 9.68 x 10^5 / 60000 = 16.133333333333333 s^(-1)*mM^(-1). Quotient disclosure for this row: 35.0 / 2.17 = 16.129032258064516 s^-1 mM^-1, which is the exported kcat_over_km, and the printed efficiency cell is that quotient written to the three significant figures the table uses.

raw_value_unit_evidence: Table 1, enzyme row 'AChE', substrate heroin: kcat = 2100 min^-1; KM = 2170 uM; printed kcat/KM = 9.68 x 10^5 min^-1 M^-1.

substrate: heroin

status: verified


substrate_name: p-Nitrophenyl acetate

sequence_source: UniProt REST P22303 canonical sequence; direct lookup on 2026-05-27

substrate: p-Nitrophenyl acetate


sequence_variant_note: Resolved canonical sequence from UniProt REST P22303 canonical sequence; direct lookup on 2026-05-27 and applied mutation signature Y337A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P22303 canonical sequence; direct lookup on 2026-05-27 and applied mutation signature F338A to reconstruct the assayed variant sequence.


organism: Mus musculus

substrate_name: Acetylcholine

sequence_variant_note: Resolved canonical sequence from UniProt REST P21836 canonical sequence; direct lookup on 2026-05-27 and applied mutation signature F297I/Y337A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

smiles: CC(=O)OCC[N+](C)(C)C

substrate: Acetylcholine


sequence_variant_note: Resolved canonical sequence from UniProt REST P21836 canonical sequence; direct lookup on 2026-05-27 and applied mutation signature F295A/Y337A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_source: UniProt REST P21836 canonical sequence; direct lookup on 2026-05-27

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


sequence_variant_note: Resolved canonical sequence from UniProt REST P21836 canonical sequence; direct lookup on 2026-05-27 and applied mutation signature E202Q/F295L/Y337A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P22303 REST record checked directly; signal peptide 1-31, chain 32-614. and applied mutation signature F297V with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P22303 REST record checked directly; signal peptide 1-31, chain 32-614. and applied mutation signature F338A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P22303 REST record checked directly; signal peptide 1-31, chain 32-614. and applied mutation signature W86A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P22303 REST record checked directly; signal peptide 1-31, chain 32-614. and applied mutation signature F295L with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P22303 REST record checked directly; signal peptide 1-31, chain 32-614. and applied mutation signature W286A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P22303 REST record checked directly; signal peptide 1-31, chain 32-614. and applied mutation signature Y337A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P22303 REST record checked directly; signal peptide 1-31, chain 32-614.


sequence_source: UniProtKB:P21836 direct REST FASTA/JSON; mature-chain mutation positions mapped to precursor sequence with UniProt Signal 1-31 and Chain 32-614.

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +31, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature F295L/Y337A matches the mutant residue at offset +31 and the reference residue at offset +35; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P21836 direct REST FASTA/JSON canonical sequence; UniProt reviewed mouse acetylcholinesterase EC 3.1.1.7.


sequence_source: UniProtKB:P22303 canonical sequence; row-specific variant unresolved

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical sequence; HuAChE mature-chain mutation numbering applied at offset +31 and applied mutation signature Y72A/E285A/W286A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical sequence; HuAChE mature-chain mutation numbering applied at offset +31 and applied mutation signature Y124A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical sequence; HuAChE mature-chain mutation numbering applied at offset +31 and applied mutation signature Y72A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical sequence; HuAChE mature-chain mutation numbering applied at offset +31 and applied mutation signature E285A/W286A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical sequence; HuAChE mature-chain mutation numbering applied at offset +31 and applied mutation signature Y72A/E285A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical sequence; HuAChE mature-chain mutation numbering applied at offset +31 and applied mutation signature F297A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical sequence; HuAChE mature-chain mutation numbering applied at offset +31 and applied mutation signature F295A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical sequence; HuAChE mature-chain mutation numbering applied at offset +31 and applied mutation signature Y72A/W286A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P21836 (ACES_MOUSE); signal peptide 1-31; mature-enzyme numbering offset +31


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21836 (ACES_MOUSE); signal peptide 1-31; mature-enzyme numbering offset +31 and applied mutation signature W286R with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21836 (ACES_MOUSE); signal peptide 1-31; mature-enzyme numbering offset +31 and applied mutation signature Y72N/D74N/Y124Q/W286A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P21836 and applied mutation signature Y72N/Y124Q/W286A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters for Cholinesterase Wild-Type and Mutant Enzymes), enzyme row 'Y72N/Y124Q/W286A'; column 'Km (uM)' = 230; column 'Kss (mM)' = 14; column 'b' = 0.27; column 'kcat (10^5/min)' = 1.5; column 'kcat/Km (10^9/min M)' = 0.67.

normalized_value_unit_evidence: Km: printed Table I cell 230 uM; 230 / 1000 = 0.23 mM; the exported value is 0.23 mM. kcat: printed Table I cell 1.5 x 10^5 min^-1 = 150000 min^-1; 150000 / 60 = 2500.0 s^-1; the exported value is 2500.0 s^(-1). kcat/Km: the paper's own printed efficiency cell 0.67 x 10^9 M^-1 min^-1 converts to 11166.666666666666 s^-1 mM^-1 because 1 M^-1 min^-1 is 1/60000 s^-1 mM^-1. The quotient of the two printed component cells, re-expressed in the printed column's units, is 0.6522 x 10^9 M^-1 min^-1, which falls outside the rounding interval of the printed cell 0.67 x 10^9, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table I, enzyme row 'Y72N/Y124Q/W286A': Km = 230 uM; kcat = 1.5 x 10^5 min^-1; printed kcat/Km = 0.67 x 10^9 M^-1 min^-1.

row_label: Table I, enzyme row 'Y72N/Y124Q/W286A' (substrate acetylthiocholine)

table_label: Table I: Kinetic Parameters for Cholinesterase Wild-Type and Mutant Enzymes (Biochemistry 1993, 32(45):12074-12084)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21836 (ACES_MOUSE); signal peptide 1-31; mature-enzyme numbering offset +31 and applied mutation signature F297Y with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21836 (ACES_MOUSE); signal peptide 1-31; mature-enzyme numbering offset +31 and applied mutation signature F295Y with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P21836 and applied mutation signature Y124Q with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters for Cholinesterase Wild-Type and Mutant Enzymes), enzyme row 'Y124Q'; column 'Km (uM)' = 120; column 'Kss (mM)' = 25; column 'b' = 0.35; column 'kcat (10^5/min)' = 1.1; column 'kcat/Km (10^9/min M)' = 0.94.

normalized_value_unit_evidence: Km: printed Table I cell 120 uM; 120 / 1000 = 0.12 mM; the exported value is 0.12 mM. kcat: printed Table I cell 1.1 x 10^5 min^-1 = 110000 min^-1; 110000 / 60 = 1833.333 s^-1; the exported value is 1833.333 s^(-1). kcat/Km: the paper's own printed efficiency cell 0.94 x 10^9 M^-1 min^-1 converts to 15666.666666666666 s^-1 mM^-1 because 1 M^-1 min^-1 is 1/60000 s^-1 mM^-1. The quotient of the two printed component cells, re-expressed in the printed column's units, is 0.9167 x 10^9 M^-1 min^-1, which falls outside the rounding interval of the printed cell 0.94 x 10^9, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table I, enzyme row 'Y124Q': Km = 120 uM; kcat = 1.1 x 10^5 min^-1; printed kcat/Km = 0.94 x 10^9 M^-1 min^-1.

row_label: Table I, enzyme row 'Y124Q' (substrate acetylthiocholine)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21836 (ACES_MOUSE); signal peptide 1-31; mature-enzyme numbering offset +31 and applied mutation signature Y72N with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P21836 (ACES_MOUSE), fetched via UniProt REST FASTA on 2026-05-27; variant reconstructed from source mutation_signature using mature-chain numbering offset +31 because UniProt marks residues 1-31 as signal peptide. and applied mutation signature V300G with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P21836 (ACES_MOUSE), fetched via UniProt REST FASTA on 2026-05-27; variant reconstructed from source mutation_signature using mature-chain numbering offset +31 because UniProt marks residues 1-31 as signal peptide. and applied mutation signature Y72N/W286R with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P21836 and applied mutation signature D74N with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters for Cholinesterase Wild-Type and Mutant Enzymes), enzyme row 'D74N'; column 'Km (uM)' = 1300; column 'Kss (mM)' = 530; column 'b' = 0; column 'kcat (10^5/min)' = 0.84; column 'kcat/Km (10^9/min M)' = 0.063.

normalized_value_unit_evidence: Km: printed Table I cell 1300 uM; 1300 / 1000 = 1.3 mM; the exported value is 1.3 mM. kcat: printed Table I cell 0.84 x 10^5 min^-1 = 84000 min^-1; 84000 / 60 = 1400.0 s^-1; the exported value is 1400.0 s^(-1). kcat/Km: the paper's own printed efficiency cell 0.063 x 10^9 M^-1 min^-1 converts to 1050.0 s^-1 mM^-1 because 1 M^-1 min^-1 is 1/60000 s^-1 mM^-1. The quotient of the two printed component cells, re-expressed in the printed column's units, is 0.0646 x 10^9 M^-1 min^-1, which falls outside the rounding interval of the printed cell 0.063 x 10^9, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table I, enzyme row 'D74N': Km = 1300 uM; kcat = 0.84 x 10^5 min^-1; printed kcat/Km = 0.063 x 10^9 M^-1 min^-1.

row_label: Table I, enzyme row 'D74N' (substrate acetylthiocholine)


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P21836 (ACES_MOUSE), fetched via UniProt REST FASTA on 2026-05-27; variant reconstructed from source mutation_signature using mature-chain numbering offset +31 because UniProt marks residues 1-31 as signal peptide. and applied mutation signature Y72N/Y124Q/W286R with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P21836 (ACES_MOUSE), fetched via UniProt REST FASTA on 2026-05-27; variant reconstructed from source mutation_signature using mature-chain numbering offset +31 because UniProt marks residues 1-31 as signal peptide. and applied mutation signature Y72N/D74N/Y124Q/W286R with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P21836 (ACES_MOUSE), fetched via UniProt REST FASTA on 2026-05-27; variant reconstructed from source mutation_signature using mature-chain numbering offset +31 because UniProt marks residues 1-31 as signal peptide. and applied mutation signature Y124Q/W286R with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P21836 (ACES_MOUSE), fetched via UniProt REST FASTA on 2026-05-27; variant reconstructed from source mutation_signature using mature-chain numbering offset +31 because UniProt marks residues 1-31 as signal peptide. and applied mutation signature F297I with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P21836 (ACES_MOUSE), fetched via UniProt REST FASTA on 2026-05-27; variant reconstructed from source mutation_signature using mature-chain numbering offset +31 because UniProt marks residues 1-31 as signal peptide. and applied mutation signature Y337F with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P21836 reviewed canonical precursor sequence; F295L reconstructed on the mature acetylcholinesterase chain by applying UniProt chain start 32 as a +31 precursor offset. and applied mutation signature F295L with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P21836 and applied mutation signature Y337A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters for Cholinesterase Wild-Type and Mutant Enzymes), enzyme row 'Y337A'; column 'Km (uM)' = 110; column 'Kss (mM)' = 29; column 'b' = 0.59; column 'kcat (10^5/min)' = 0.52; column 'kcat/Km (10^9/min M)' = 0.46.

normalized_value_unit_evidence: Km: printed Table I cell 110 uM; 110 / 1000 = 0.11 mM; the exported value is 0.11 mM. kcat: printed Table I cell 0.52 x 10^5 min^-1 = 52000 min^-1; 52000 / 60 = 866.667 s^-1; the exported value is 866.667 s^(-1). kcat/Km: the paper's own printed efficiency cell 0.46 x 10^9 M^-1 min^-1 converts to 7666.666666666667 s^-1 mM^-1 because 1 M^-1 min^-1 is 1/60000 s^-1 mM^-1. The quotient of the two printed component cells, re-expressed in the printed column's units, is 0.4727 x 10^9 M^-1 min^-1, which falls outside the rounding interval of the printed cell 0.46 x 10^9, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table I, enzyme row 'Y337A': Km = 110 uM; kcat = 0.52 x 10^5 min^-1; printed kcat/Km = 0.46 x 10^9 M^-1 min^-1.

row_label: Table I, enzyme row 'Y337A' (substrate acetylthiocholine)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P21836 and applied mutation signature F295L/F297I with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters for Cholinesterase Wild-Type and Mutant Enzymes), enzyme row 'F295L/F297I'; column 'Km (uM)' = 200; column 'Kss (mM)' = 83; column 'b' = 0.67; column 'kcat (10^5/min)' = 0.12; column 'kcat/Km (10^9/min M)' = 0.059.

normalized_value_unit_evidence: Km: printed Table I cell 200 uM; 200 / 1000 = 0.2 mM; the exported value is 0.2 mM. kcat: printed Table I cell 0.12 x 10^5 min^-1 = 12000 min^-1; 12000 / 60 = 200.0 s^-1; the exported value is 200.0 s^(-1). kcat/Km: the paper's own printed efficiency cell 0.059 x 10^9 M^-1 min^-1 converts to 983.3333333333334 s^-1 mM^-1 because 1 M^-1 min^-1 is 1/60000 s^-1 mM^-1. The quotient of the two printed component cells, re-expressed in the printed column's units, is 0.0600 x 10^9 M^-1 min^-1, which falls outside the rounding interval of the printed cell 0.059 x 10^9, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table I, enzyme row 'F295L/F297I': Km = 200 uM; kcat = 0.12 x 10^5 min^-1; printed kcat/Km = 0.059 x 10^9 M^-1 min^-1.

row_label: Table I, enzyme row 'F295L/F297I' (substrate acetylthiocholine)


enzyme_display_name: beta-lactamase

organism: Aeromonas enteropelogenes

substrate_name: ceftriaxone

sequence_source: UniProtKB:B2BSN6 direct REST lookup on 2026-05-27

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

column_label: Table 3. Kinetic parameters of TRU-1, CAV-1, and AmpC beta-lactamases; row Ceftriaxone; TRU-1 columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 0.042, 6, 7.0 × 10^3

raw_value_unit_evidence: TRU-1 / Ceftriaxone: kcat=0.042 s^-1; Km=6 uM; kcat/Km=7.0 × 10^3 M^-1 s^-1

row_label: TRU-1 / Ceftriaxone

enzyme: beta-lactamase

substrate: ceftriaxone


organism: Aeromonas hydrophila

substrate_name: biapenem

sequence_source: UniProtKB:P26918 direct REST lookup on 2026-05-27

column_label: PMID 15588826 DOI 10.1016/j.jmb.2004.10.070 Table 1; row Wild-type; biapenem columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 1 wild-type CphA biapenem: kcat 300 s^-1; Km 166 uM; kcat/Km 1.8 x 10^6 M^-1 s^-1.

row_label: Wild-type / Biapenem

table_label: Table 1. Kinetic parameters of the wild type and selected mutants of CphA

substrate: biapenem


substrate_name: Imipenem

sequence_variant_note: Mutation signature N220G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: Imipenem


substrate_name: Cephaloridine

sequence_variant_note: Mutation signature N116H/R121H/N220G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: Cephaloridine


sequence_variant_note: Mutation signature N116H/N220G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: cefotaxime

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

substrate: cefotaxime


substrate_name: Nitrocefin

substrate: Nitrocefin


substrate_name: Ampicillin

substrate: Ampicillin


substrate_name: cefoxitin

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

column_label: Table label: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f. Row: Cefoxitin. Enzyme column group: TRU-1. Columns read: k cat (s^-1) cell 0.88, K m (uM) cell 0.025, k cat / K m (M^-1 s^-1) cell 3.5 x 10^7. metric: kcat; raw value: 0.88; raw unit: s^-1; normalized value: 0.88 s^(-1); metric: Km; raw value: 0.025; raw unit: uM; normalized value: 0.000025 mM; metric: kcat/Km; raw unit: M^-1 s^-1; normalized value: 35200.0 s^-1 mM^-1; assay condition: Purified TRU-1 beta-lactamase; steady-state kinetic parameters for the hydrolysis of beta-lactam substrates were determined at 30°C with 50 mM HEPES buffer (pH 7.0); the enzyme concentration in the assay mixtures ranged between 0.2 and 450 nM. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: TRU-1 columns of Table 3 row Cefoxitin: kcat 0.88 s^-1 = 0.88 s^(-1); Km 0.025 uM = 0.000025 mM (1 uM = 0.001 mM); kcat/Km 35200.0 s^-1 mM^-1. In the table asset the multiplication sign renders as ×, the superscript minus one as −1, the micro sign as μ, and superscript exponents are flattened, so the printed cell `3.5 × 10 7` is the paper's 3.5 x 10^7 M^-1 s^-1.

raw_value_unit_evidence: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f | column group header row of Table 3: TRU-1 b CAV-1 AmpC TRU-1 CAV-1 AmpC TRU-1 c CAV-1 AmpC; metric header row: Substrate k cat (s −1 ) K m (μM) k cat / K m (M −1 ·s −1 ) | row: Cefoxitin 0.88 0.5 0.2 0.025 a 0.4 0.65 3.5 × 10 7 1.3 × 10 6 3.0 × 10 5 | TRU-1 cells read: k cat = 0.88 s^-1; K m = 0.025 uM; k cat / K m = 3.5 x 10^7 M^-1 s^-1

row_label: TRU-1 | Cefoxitin

substrate: cefoxitin


substrate_name: penicillin G

column_label: Table label: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f. Row: Penicillin G. Enzyme column group: TRU-1. Columns read: k cat (s^-1) cell 27, K m (uM) cell 2, k cat / K m (M^-1 s^-1) cell 1.4 x 10^7. metric: kcat; raw value: 27; raw unit: s^-1; normalized value: 27.0 s^(-1); metric: Km; raw value: 2; raw unit: uM; normalized value: 0.002 mM; metric: kcat/Km; raw unit: M^-1 s^-1; normalized value: 13500.0 s^-1 mM^-1; assay condition: Purified TRU-1 beta-lactamase; steady-state kinetic parameters for the hydrolysis of beta-lactam substrates were determined at 30°C with 50 mM HEPES buffer (pH 7.0); the enzyme concentration in the assay mixtures ranged between 0.2 and 450 nM. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: TRU-1 columns of Table 3 row Penicillin G: kcat 27 s^-1 = 27.0 s^(-1); Km 2 uM = 0.002 mM (1 uM = 0.001 mM); kcat/Km 13500.0 s^-1 mM^-1. In the table asset the multiplication sign renders as ×, the superscript minus one as −1, the micro sign as μ, and superscript exponents are flattened, so the printed cell `1.4 × 10 7` is the paper's 1.4 x 10^7 M^-1 s^-1.

raw_value_unit_evidence: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f | column group header row of Table 3: TRU-1 b CAV-1 AmpC TRU-1 CAV-1 AmpC TRU-1 c CAV-1 AmpC; metric header row: Substrate k cat (s −1 ) K m (μM) k cat / K m (M −1 ·s −1 ) | row: Penicillin G 27 5 45 2 a 8.7 4.4 1.4 × 10 7 5.7 × 10 5 1.0 × 10 7 | TRU-1 cells read: k cat = 27 s^-1; K m = 2 uM; k cat / K m = 1.4 x 10^7 M^-1 s^-1

row_label: TRU-1 | Penicillin G

substrate: penicillin G


column_label: Table label: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f. Row: Cefotaxime. Enzyme column group: TRU-1. Columns read: k cat (s^-1) cell 0.015, K m (uM) cell 0.0009, k cat / K m (M^-1 s^-1) cell 1.7 x 10^7. metric: kcat; raw value: 0.015; raw unit: s^-1; normalized value: 0.015 s^(-1); metric: Km; raw value: 0.0009; raw unit: uM; normalized value: 0.0000009 mM; metric: kcat/Km; raw unit: M^-1 s^-1; normalized value: 16666.666666666668 s^-1 mM^-1; assay condition: Purified TRU-1 beta-lactamase; steady-state kinetic parameters for the hydrolysis of beta-lactam substrates were determined at 30°C with 50 mM HEPES buffer (pH 7.0); the enzyme concentration in the assay mixtures ranged between 0.2 and 450 nM. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: TRU-1 columns of Table 3 row Cefotaxime: kcat 0.015 s^-1 = 0.015 s^(-1); Km 0.0009 uM = 0.0000009 mM (1 uM = 0.001 mM); kcat/Km 16666.666666666668 s^-1 mM^-1. In the table asset the multiplication sign renders as ×, the superscript minus one as −1, the micro sign as μ, and superscript exponents are flattened, so the printed cell `1.7 × 10 7` is the paper's 1.7 x 10^7 M^-1 s^-1.

raw_value_unit_evidence: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f | column group header row of Table 3: TRU-1 b CAV-1 AmpC TRU-1 CAV-1 AmpC TRU-1 c CAV-1 AmpC; metric header row: Substrate k cat (s −1 ) K m (μM) k cat / K m (M −1 ·s −1 ) | row: Cefotaxime 0.015 0.2 0.17 0.0009 a 0.1 1.7 1.7 × 10 7 2.0 × 10 6 1.0 × 10 5 | TRU-1 cells read: k cat = 0.015 s^-1; K m = 0.0009 uM; k cat / K m = 1.7 x 10^7 M^-1 s^-1

row_label: TRU-1 | Cefotaxime


substrate_name: ceftazidime

column_label: Table label: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f. Row: Ceftazidime. Enzyme column group: TRU-1. Columns read: k cat (s^-1) cell 0.11, K m (uM) cell 0.12, k cat / K m (M^-1 s^-1) cell 9.2 x 10^5. metric: kcat; raw value: 0.11; raw unit: s^-1; normalized value: 0.11 s^(-1); metric: Km; raw value: 0.12; raw unit: uM; normalized value: 0.00012 mM; metric: kcat/Km; raw unit: M^-1 s^-1; normalized value: 916.6666666666666 s^-1 mM^-1; assay condition: Purified TRU-1 beta-lactamase; steady-state kinetic parameters for the hydrolysis of beta-lactam substrates were determined at 30°C with 50 mM HEPES buffer (pH 7.0); the enzyme concentration in the assay mixtures ranged between 0.2 and 450 nM. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: TRU-1 columns of Table 3 row Ceftazidime: kcat 0.11 s^-1 = 0.11 s^(-1); Km 0.12 uM = 0.00012 mM (1 uM = 0.001 mM); kcat/Km 916.6666666666666 s^-1 mM^-1. In the table asset the multiplication sign renders as ×, the superscript minus one as −1, the micro sign as μ, and superscript exponents are flattened, so the printed cell `9.2 × 10 5` is the paper's 9.2 x 10^5 M^-1 s^-1.

raw_value_unit_evidence: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f | column group header row of Table 3: TRU-1 b CAV-1 AmpC TRU-1 CAV-1 AmpC TRU-1 c CAV-1 AmpC; metric header row: Substrate k cat (s −1 ) K m (μM) k cat / K m (M −1 ·s −1 ) | row: Ceftazidime 0.11 0.2 0.12 a 0.6 9.2 × 10 5 3.3 × 10 5 | TRU-1 cells read: k cat = 0.11 s^-1; K m = 0.12 uM; k cat / K m = 9.2 x 10^5 M^-1 s^-1

row_label: TRU-1 | Ceftazidime

substrate: ceftazidime


substrate_name: piperacillin

column_label: Table label: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f. Row: Piperacillin. Enzyme column group: TRU-1. Columns read: k cat (s^-1) cell 0.54, K m (uM) cell 0.2, k cat / K m (M^-1 s^-1) cell 2.7 x 10^6. metric: kcat; raw value: 0.54; raw unit: s^-1; normalized value: 0.54 s^(-1); metric: Km; raw value: 0.2; raw unit: uM; normalized value: 0.0002 mM; metric: kcat/Km; raw unit: M^-1 s^-1; normalized value: 2700.0 s^-1 mM^-1; assay condition: Purified TRU-1 beta-lactamase; steady-state kinetic parameters for the hydrolysis of beta-lactam substrates were determined at 30°C with 50 mM HEPES buffer (pH 7.0); the enzyme concentration in the assay mixtures ranged between 0.2 and 450 nM. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: TRU-1 columns of Table 3 row Piperacillin: kcat 0.54 s^-1 = 0.54 s^(-1); Km 0.2 uM = 0.0002 mM (1 uM = 0.001 mM); kcat/Km 2700.0 s^-1 mM^-1. In the table asset the multiplication sign renders as ×, the superscript minus one as −1, the micro sign as μ, and superscript exponents are flattened, so the printed cell `2.7 × 10 6` is the paper's 2.7 x 10^6 M^-1 s^-1.

raw_value_unit_evidence: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f | column group header row of Table 3: TRU-1 b CAV-1 AmpC TRU-1 CAV-1 AmpC TRU-1 c CAV-1 AmpC; metric header row: Substrate k cat (s −1 ) K m (μM) k cat / K m (M −1 ·s −1 ) | row: Piperacillin 0.54 0.2 a 2.7 × 10 6 | TRU-1 cells read: k cat = 0.54 s^-1; K m = 0.2 uM; k cat / K m = 2.7 x 10^6 M^-1 s^-1

row_label: TRU-1 | Piperacillin

substrate: piperacillin


organism: Achromobacter sp. sallbros1

substrate_name: ampicillin

sequence_source: UniProtKB:E7BCS7 direct lookup

assay_conditions_summary: pH 7.2; 298.15 K; buffer 50 mM HEPES

column_label: Table label: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1. Row: Ampicillin. Enzyme column group: TMB-1. Columns read: k cat (s^-1) cell 3.3, K m (uM) cell 27, k cat / K m (s^-1/uM) cell 0.122. metric: kcat; raw value: 3.3; raw unit: s^-1; normalized value: 3.3 s^(-1); metric: Km; raw value: 27; raw unit: uM; normalized value: 0.027 mM; metric: kcat/Km; raw value: 0.122; raw unit: s^-1/uM; normalized value: 122 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified TMB-1 metallo-beta-lactamase; steady-state kinetics were performed at 25 degrees C in a spectrophotometer using 96-well plates; all substrates were tested as duplicates using 50 mM HEPES buffer, pH 7.2, 100 uM ZnCl2, 0.02% NaN3, and 0.1 mg/ml bovine serum albumin as a buffer system. Export row conditions: pH 7.2; 298.15 K.

normalized_value_unit_evidence: TMB-1 columns of Table 2 row Ampicillin: kcat 3.3 s^-1 = 3.3 s^(-1); Km 27 uM = 0.027 mM (1 uM = 0.001 mM); kcat/Km primary cell 0.122 s^-1/uM = 122 s^-1 mM^-1 (1 s^-1/uM = 1000 s^-1 mM^-1). In the table asset the micro sign renders as μ, the superscript minus one as −1, and superscript markers are flattened, so the printed header cells read `k cat (s −1 )`, `K m (μM)` and `k cat / K m (s −1 /μM)`.

raw_value_unit_evidence: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1 | enzyme column group header row of Table 2: TMB-1 DIM-1 a GIM-1 b; metric header row: k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) | row: Ampicillin 3.3 27 0.122 20 110 0.182 3.3 20 0.165 | TMB-1 cells read: k cat = 3.3 s^-1; K m = 27 uM; k cat / K m = 0.122 s^-1/uM

row_label: TMB-1 | Ampicillin

substrate: ampicillin


sequence_source: UniProtKB:E7BCS5 canonical sequence; NCBI FR771847 protein_id CBY88906.1


substrate_name: meropenem

substrate: meropenem


substrate_name: ertapenem

substrate: ertapenem


substrate_name: cefuroxime

substrate: cefuroxime


substrate_name: azlocillin

sequence_source: UniProtKB:P26918 direct FASTA lookup; reviewed Swiss-Prot BLAB_AERHY/cphA

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

column_label: Table label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa. Row: Azlocillin. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 90 ± 5, kcat (s^-1) cell 0.18, kcat/Km (M^-1 s^-1) cell 2.00 x 10^3 M^-1 s^-1. Km 90 ± 5 uM normalizes to 0.09 mM and equals the exported km; kcat 0.18 s^-1 equals the exported kcat; the table's printed kcat/Km cell 2.00 x 10^3 M^-1 s^-1 normalizes to 2.0 s^-1 mM^-1 and decimal-matches the exported kcat_over_km.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 4 row Azlocillin: Km 90 ± 5 uM = 0.09 mM; kcat 0.18 s^-1 = 0.18 s^-1; kcat/Km 2.0 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Azlocillin 90 6 5 0.18 2.00 3 103 170 6 10 205 1.20 3 106 6 6 0.1b 75 1.30 3 107

row_label: A. hydrophila AE036 | Azlocillin

substrate: azlocillin


substrate_name: Sulbenicillin

column_label: Table label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa. Row: Sulbenicillin. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 230 ± 10, kcat (s^-1) cell 0.50, kcat/Km (M^-1 s^-1) cell 2.10 x 10^3 M^-1 s^-1. Km 230 ± 10 uM normalizes to 0.23 mM and equals the exported km; kcat 0.50 s^-1 equals the exported kcat; the exported kcat_over_km 2.1739130434782608 s^-1 mM^-1 is the exact quotient of those same two printed cells, and the table's own printed kcat/Km cell 2.10 x 10^3 M^-1 s^-1 = 2.1 s^-1 mM^-1 is that same quantity at the three-significant-figure precision the table prints.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 4 row Sulbenicillin: Km 230 ± 10 uM = 0.23 mM; kcat 0.50 s^-1 = 0.5 s^-1; kcat/Km 2.1739130434782608 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Sulbenicillin 230 6 10 0.50 2.10 3 103 .2,000 .300 1.93 3 105c 190 6 5 225 1.20 3 106

row_label: A. hydrophila AE036 | Sulbenicillin

substrate: Sulbenicillin


substrate_name: Cefsulodin

column_label: Table label: TABLE 5. Kinetic parameters of metallo-b-lactamases with cephalosporins (D3-cephems)a. Row: Cefsulodin. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 130 ± 10, kcat (s^-1) cell 0.05, kcat/Km (M^-1 s^-1) cell 3.50 x 10^2 M^-1 s^-1. Km 130 ± 10 uM normalizes to 0.13 mM and equals the exported km; kcat 0.05 s^-1 equals the exported kcat; the exported kcat_over_km 0.38461538461538464 s^-1 mM^-1 is the exact quotient of those same two printed cells, and the table's own printed kcat/Km cell 3.50 x 10^2 M^-1 s^-1 = 0.35 s^-1 mM^-1 is that same quantity at the three-significant-figure precision the table prints.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 5 row Cefsulodin: Km 130 ± 10 uM = 0.13 mM; kcat 0.05 s^-1 = 0.05 s^-1; kcat/Km 0.38461538461538464 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 5. Kinetic parameters of metallo-b-lactamases with cephalosporins (D3-cephems)a | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Cefsulodin 130 6 10 0.05 3.50 3 102 230 6 20 12.5 5.40 3 104 5 6 0.3d 7.5 1.50 3 106

row_label: A. hydrophila AE036 | Cefsulodin

substrate: Cefsulodin


column_label: Table label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa. Row: Piperacillin. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 55 ± 2, kcat (s^-1) cell 0.43, kcat/Km (M^-1 s^-1) cell 7.80 x 10^3 M^-1 s^-1. Km 55 ± 2 uM normalizes to 0.055 mM and equals the exported km; kcat 0.43 s^-1 equals the exported kcat; the exported kcat_over_km 7.818181818181818 s^-1 mM^-1 is the exact quotient of those same two printed cells, and the table's own printed kcat/Km cell 7.80 x 10^3 M^-1 s^-1 = 7.8 s^-1 mM^-1 is that same quantity at the three-significant-figure precision the table prints.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 4 row Piperacillin: Km 55 ± 2 uM = 0.055 mM; kcat 0.43 s^-1 = 0.43 s^-1; kcat/Km 7.818181818181818 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Piperacillin 55 6 2 0.43 7.80 3 103 450 6 10 75 1.70 3 105 20 6 1 140 7.00 3 106

row_label: A. hydrophila AE036 | Piperacillin


substrate_name: Imipenem

substrate: Imipenem


substrate_name: Talampicillin

sequence_source: UniProt P26918 FASTA; direct lookup on rest.uniprot.org

column_label: Table label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa. Row: Talampicillin. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 90 ± 10, kcat (s^-1) cell 0.04, kcat/Km (M^-1 s^-1) cell 5.00 x 10^2 M^-1 s^-1. Km 90 ± 10 uM normalizes to 0.09 mM and equals the exported km; kcat 0.04 s^-1 equals the exported kcat; the exported kcat_over_km 0.4444444444444445 s^-1 mM^-1 is the exact quotient of those same two printed cells, and the table's own printed kcat/Km cell 5.00 x 10^2 M^-1 s^-1 = 0.5 s^-1 mM^-1 is that same quantity at the three-significant-figure precision the table prints.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 4 row Talampicillin: Km 90 ± 10 uM = 0.09 mM; kcat 0.04 s^-1 = 0.04 s^-1; kcat/Km 0.4444444444444445 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Talampicillin 90 6 10 0.04 5.00 3 102 —d — — 160 6 5 220 6.50 3 105

row_label: A. hydrophila AE036 | Talampicillin

substrate: Talampicillin


column_label: Table label: TABLE 5. Kinetic parameters of metallo-b-lactamases with cephalosporins (D3-cephems)a. Row: CGP-31523A. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 75 ± 5, kcat (s^-1) cell 0.05, kcat/Km (M^-1 s^-1) cell 6.00 x 10^2 M^-1 s^-1. Km 75 ± 5 uM normalizes to 0.075 mM and equals the exported km; kcat 0.05 s^-1 equals the exported kcat; the exported kcat_over_km 0.6666666666666667 s^-1 mM^-1 is the exact quotient of those same two printed cells, and the table's own printed kcat/Km cell 6.00 x 10^2 M^-1 s^-1 = 0.6 s^-1 mM^-1 is that same quantity at the three-significant-figure precision the table prints.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 5 row CGP-31523A: Km 75 ± 5 uM = 0.075 mM; kcat 0.05 s^-1 = 0.05 s^-1; kcat/Km 0.6666666666666667 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 5. Kinetic parameters of metallo-b-lactamases with cephalosporins (D3-cephems)a | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: CGP-31523A 75 6 5 0.05 6.00 3 102 250 6 10 25.0 1.00 3 105 27 6 2 38.0 1.40 3 106

row_label: A. hydrophila AE036 | CGP-31523A


substrate_name: 6-beta-Iodopenicillanic acid

sequence_source: UniProt Q6X1Y9 FASTA; direct lookup on rest.uniprot.org

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

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, row 6-beta-Iodopenicillanic acid: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM -> mM normalization, and their same-row quotient reproduces the exported kcat/Km.

raw_value_unit_evidence: Table 3 Aeromonas hydrophila A2 enzyme column, 6-beta-Iodopenicillanic acid row: Km 530 +/- 50 uM uM; kcat 0.64 s^-1.

row_label: Aeromonas hydrophila A2 enzyme | 6-beta-Iodopenicillanic acid

table_label: Table 3 Kinetic parameters determined for class B beta-lactamases

substrate: 6-beta-Iodopenicillanic acid


substrate_name: Sulbactam

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, row Sulbactam: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM -> mM normalization, and their same-row quotient reproduces the exported kcat/Km.

raw_value_unit_evidence: Table 3 Aeromonas hydrophila A2 enzyme column, Sulbactam row: Km 37 +/- 4 uM uM; kcat 0.12 s^-1.

row_label: Aeromonas hydrophila A2 enzyme | Sulbactam

substrate: Sulbactam


column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, row Imipenem: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM -> mM normalization, and their same-row quotient reproduces the exported kcat/Km.

raw_value_unit_evidence: Table 3 Aeromonas hydrophila A2 enzyme column, Imipenem row: Km 80 +/- 8 uM uM; kcat 168 s^-1.

row_label: Aeromonas hydrophila A2 enzyme | Imipenem


substrate_name: cephaloridin

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, row Cephaloridin: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM to mM normalization, and their same-row quotient reproduces the exported kcat/Km.

raw_value_unit_evidence: Table 3, Aeromonas hydrophila A2 enzyme block, row Cephaloridin: Km cell 190 +/- 8 uM; kcat cell 0.12 s^-1.

row_label: Aeromonas hydrophila A2 beta-lactamase | Cephaloridin

table_label: Table 3 Kinetic parameters determined for class B beta-lactamases (PMC1132494 scanned page 154)

substrate: cephaloridin


substrate_name: Oxacillin

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, row Oxacillin: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM to mM normalization, and their same-row quotient reproduces the exported kcat/Km.

raw_value_unit_evidence: Table 3, Aeromonas hydrophila A2 enzyme block, row Oxacillin: Km cell 25 +/- 3 uM; kcat cell 0.75 s^-1.

row_label: Aeromonas hydrophila A2 beta-lactamase | Oxacillin

substrate: Oxacillin


substrate_name: Penicillin G

sequence_source: UniProtKB Q6X1Y9 FASTA and JSON retrieved directly on 2026-05-27; sequence version 1

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, row Penicillin G: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM to mM normalization, and their same-row quotient reproduces the exported kcat/Km.

raw_value_unit_evidence: Table 3, Aeromonas hydrophila A2 enzyme block, row Penicillin G: Km cell 700 +/- 50 uM; kcat cell 5.21 s^-1.

row_label: Aeromonas hydrophila A2 beta-lactamase | Penicillin G

substrate: Penicillin G


substrate_name: carbenicillin

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, row Carbenicillin: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM to mM normalization, and their same-row quotient reproduces the exported kcat/Km.

raw_value_unit_evidence: Table 3, Aeromonas hydrophila A2 enzyme block, row Carbenicillin: Km cell 450 +/- 30 uM; kcat cell 16 s^-1.

row_label: Aeromonas hydrophila A2 beta-lactamase | Carbenicillin

substrate: carbenicillin


substrate_name: cefotaxime

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, row Cefotaxime: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM to mM normalization, and their same-row quotient reproduces the exported kcat/Km.

raw_value_unit_evidence: Table 3, Aeromonas hydrophila A2 enzyme block, row Cefotaxime: Km cell 26 +/- 3 uM; kcat cell 0.07 s^-1.

row_label: Aeromonas hydrophila A2 beta-lactamase | Cefotaxime

substrate: cefotaxime


substrate_name: Nitrocefin

substrate: Nitrocefin


substrate_name: cephalexin

substrate: cephalexin


substrate_name: Cefuroxime

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, row Cefuroxime: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM to mM normalization, and their same-row quotient reproduces the exported kcat/Km.

raw_value_unit_evidence: Table 3, Aeromonas hydrophila A2 enzyme block, row Cefuroxime: Km cell 20 +/- 3 uM; kcat cell 0.07 s^-1.

row_label: Aeromonas hydrophila A2 beta-lactamase | Cefuroxime

substrate: Cefuroxime


substrate_name: Cephaloglycin

column_label: PMC1132494 page 154 Table 3, Aeromonas hydrophila A2 enzyme block, row Cephaloglycin: the Km (uM) cell and the kcat (s^-1) cell of that one row reproduce the export values exactly after Km uM to mM normalization, and their same-row quotient reproduces the exported kcat/Km.

raw_value_unit_evidence: Table 3, Aeromonas hydrophila A2 enzyme block, row Cephaloglycin: Km cell 280 +/- 30 uM; kcat cell 0.2 s^-1.

row_label: Aeromonas hydrophila A2 beta-lactamase | Cephaloglycin

substrate: Cephaloglycin


organism: Aliivibrio salmonicida

substrate_name: cefuroxime

column_label: table label: Table 1. Comparison of kcat, KM and catalytic efficiency for ALI-1 (values from current work), IMP-119 and VIM-2.23; row label: Cefuroxime; column label: ALI-1 column of the kcat (s-1) group, ALI-1 column of the KM (uM) group and ALI-1 column of the kcat/KM (1/uM*s) group of this one printed row; no cell is taken from the IMP-1 or VIM-2 columns and no cell is taken from any other row; raw value: KM 68 ± 30 uM, kcat 11 ± 3 s-1, kcat/KM 0.16 1/uM*s; raw unit: uM for KM, s-1 for kcat, 1/uM*s for kcat/KM; normalized value: KM 0.068 mM, kcat 11.0 s^-1, kcat/KM 161.76470588235293 s^-1 mM^-1; normalized unit: mM, s^-1, s^-1 mM^-1; condition label: Table 1 kinetic analysis of ALI-1: the substrates were dissolved in a solution of 50 mM HEPES, pH 7.2 and 100 uM ZnCl2; the solutions for the kinetic analysis were made in the range of 2-1,000 uM; the kinetic analysis was performed in a reaction mixture containing 50 mM HEPES, pH 7.2 and 100 uM ZnCl2; the reaction mixture was pre-incubated for 5 min at 30 degrees Celsius. This record reads only the ALI-1 column of each metric group of Table 1; the IMP-1 and VIM-2 columns of the same printed row are literature comparison values for other enzymes and no cell is taken from them. Exported assay conditions: pH 7.2, 310.15 K. The exported pH equals the paper's printed pH 7.2. The exported temperature 310.15 K does not correspond to the 30 degrees Celsius pre-incubation the paper prints for this kinetic analysis, so this record certifies only the printed kinetic cells and asserts no temperature value. The exported row carries no cofactor_name, so nothing in the exported row conflicts with the 100 uM ZnCl2 the paper prints for this assay.

normalized_value_unit_evidence: KM 68 ± 30 uM divided by 1000 gives 0.068 mM at the export's stored precision; exported KM 0.068 mM. kcat 11 ± 3 s-1 is already in s^-1 and at the export's stored precision is 11.0 s^-1; exported kcat 11.0 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 11.0 s^-1 divided by 0.068 mM giving 161.76470588235293 s^-1 mM^-1, and of nothing else; exported kcat/Km 161.76470588235293 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, printed row Cefuroxime, ALI-1 columns: KM 68 ± 30 uM; kcat 11 ± 3 s-1; kcat/KM 0.16 1/uM*s.

row_label: Cefuroxime

substrate: cefuroxime


substrate_name: cefoxitin

column_label: table label: Table 1. Comparison of kcat, KM and catalytic efficiency for ALI-1 (values from current work), IMP-119 and VIM-2.23; row label: Cefoxitin; column label: ALI-1 column of the kcat (s-1) group, ALI-1 column of the KM (uM) group and ALI-1 column of the kcat/KM (1/uM*s) group of this one printed row; no cell is taken from the IMP-1 or VIM-2 columns and no cell is taken from any other row; raw value: KM 79 ± 30 uM, kcat 0.27 ± 0.09 s-1, kcat/KM 0.0034 1/uM*s; raw unit: uM for KM, s-1 for kcat, 1/uM*s for kcat/KM; normalized value: KM 0.079 mM, kcat 0.27 s^-1, kcat/KM 3.4177215189873418 s^-1 mM^-1; normalized unit: mM, s^-1, s^-1 mM^-1; condition label: Table 1 kinetic analysis of ALI-1: the substrates were dissolved in a solution of 50 mM HEPES, pH 7.2 and 100 uM ZnCl2; the solutions for the kinetic analysis were made in the range of 2-1,000 uM; the kinetic analysis was performed in a reaction mixture containing 50 mM HEPES, pH 7.2 and 100 uM ZnCl2; the reaction mixture was pre-incubated for 5 min at 30 degrees Celsius. This record reads only the ALI-1 column of each metric group of Table 1; the IMP-1 and VIM-2 columns of the same printed row are literature comparison values for other enzymes and no cell is taken from them. Exported assay conditions: pH 7.2, 310.15 K. The exported pH equals the paper's printed pH 7.2. The exported temperature 310.15 K does not correspond to the 30 degrees Celsius pre-incubation the paper prints for this kinetic analysis, so this record certifies only the printed kinetic cells and asserts no temperature value. The exported row carries no cofactor_name, so nothing in the exported row conflicts with the 100 uM ZnCl2 the paper prints for this assay.

normalized_value_unit_evidence: KM 79 ± 30 uM divided by 1000 gives 0.079 mM at the export's stored precision; exported KM 0.079 mM. kcat 0.27 ± 0.09 s-1 is already in s^-1 and at the export's stored precision is 0.27 s^-1; exported kcat 0.27 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.27 s^-1 divided by 0.079 mM giving 3.4177215189873418 s^-1 mM^-1, and of nothing else; exported kcat/Km 3.4177215189873418 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, printed row Cefoxitin, ALI-1 columns: KM 79 ± 30 uM; kcat 0.27 ± 0.09 s-1; kcat/KM 0.0034 1/uM*s.

row_label: Cefoxitin

substrate: cefoxitin


substrate_name: ceftazidime

column_label: table label: Table 1. Comparison of kcat, KM and catalytic efficiency for ALI-1 (values from current work), IMP-119 and VIM-2.23; row label: Ceftazidime; column label: ALI-1 column of the kcat (s-1) group, ALI-1 column of the KM (uM) group and ALI-1 column of the kcat/KM (1/uM*s) group of this one printed row; no cell is taken from the IMP-1 or VIM-2 columns and no cell is taken from any other row; raw value: KM 37 ± 12 uM, kcat 0.09 ± 0.03 s-1, kcat/KM 0.0024 1/uM*s; raw unit: uM for KM, s-1 for kcat, 1/uM*s for kcat/KM; normalized value: KM 0.037 mM, kcat 0.09 s^-1, kcat/KM 2.4324324324324325 s^-1 mM^-1; normalized unit: mM, s^-1, s^-1 mM^-1; condition label: Table 1 kinetic analysis of ALI-1: the substrates were dissolved in a solution of 50 mM HEPES, pH 7.2 and 100 uM ZnCl2; the solutions for the kinetic analysis were made in the range of 2-1,000 uM; the kinetic analysis was performed in a reaction mixture containing 50 mM HEPES, pH 7.2 and 100 uM ZnCl2; the reaction mixture was pre-incubated for 5 min at 30 degrees Celsius. This record reads only the ALI-1 column of each metric group of Table 1; the IMP-1 and VIM-2 columns of the same printed row are literature comparison values for other enzymes and no cell is taken from them. Exported assay conditions: pH 7.2, 310.15 K. The exported pH equals the paper's printed pH 7.2. The exported temperature 310.15 K does not correspond to the 30 degrees Celsius pre-incubation the paper prints for this kinetic analysis, so this record certifies only the printed kinetic cells and asserts no temperature value. The exported row carries no cofactor_name, so nothing in the exported row conflicts with the 100 uM ZnCl2 the paper prints for this assay.

normalized_value_unit_evidence: KM 37 ± 12 uM divided by 1000 gives 0.037 mM at the export's stored precision; exported KM 0.037 mM. kcat 0.09 ± 0.03 s-1 is already in s^-1 and at the export's stored precision is 0.09 s^-1; exported kcat 0.09 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.09 s^-1 divided by 0.037 mM giving 2.4324324324324325 s^-1 mM^-1, and of nothing else; exported kcat/Km 2.4324324324324325 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, printed row Ceftazidime, ALI-1 columns: KM 37 ± 12 uM; kcat 0.09 ± 0.03 s-1; kcat/KM 0.0024 1/uM*s.

row_label: Ceftazidime

substrate: ceftazidime


enzyme_display_name: Metallo-beta-lactamase type 2

substrate_name: Asparenomycin A

sequence_source: UniProtKB:P26918 reviewed Swiss-Prot FASTA

column_label: Table label: TABLE 7. Kinetic parameters of metallo-b-lactamases with carbapenem antibioticsa. Row: Asparenomycin A. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 170 ± 5, kcat (s^-1) cell 475, kcat/Km (M^-1 s^-1) cell 2.80 x 10^6 M^-1 s^-1. Km 170 ± 5 uM normalizes to 0.17 mM and equals the exported km; kcat 475 s^-1 equals the exported kcat; the table's printed kcat/Km cell 2.80 x 10^6 M^-1 s^-1 normalizes to 2800.0 s^-1 mM^-1 and decimal-matches the exported kcat_over_km.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 7 row Asparenomycin A: Km 170 ± 5 uM = 0.17 mM; kcat 475 s^-1 = 475.0 s^-1; kcat/Km 2800.0 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 7. Kinetic parameters of metallo-b-lactamases with carbapenem antibioticsa | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Asparenomycin A 170 6 5 475 2.80 3 106 20 6 1 100 5.00 3 106 2 6 0.1b 14 7.00 3 106

row_label: A. hydrophila AE036 | Asparenomycin A

enzyme: Metallo-beta-lactamase type 2

substrate: Asparenomycin A


column_label: Table label: TABLE 3. Kinetic parameters of metallo-b-lactamases with benzylpenicillin and imipenem after purificationa. Row: Penicillin G. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 680 ± 30, kcat (s^-1) cell 5, kcat/Km (M^-1 s^-1) cell 7.35 x 10^3 M^-1 s^-1. Km 680 ± 30 uM normalizes to 0.68 mM and equals the exported km; kcat 5 s^-1 equals the exported kcat; the table's printed kcat/Km cell 7.35 x 10^3 M^-1 s^-1 normalizes to 7.35 s^-1 mM^-1 and decimal-matches the exported kcat_over_km.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 3 row Penicillin G: Km 680 ± 30 uM = 0.68 mM; kcat 5 s^-1 = 5.0 s^-1; kcat/Km 7.35 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 3. Kinetic parameters of metallo-b-lactamases with benzylpenicillin and imipenem after purificationa | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Penicillin G 680 6 30 5 7.35 3 103 1,550 6 100 691 4.60 3 105 55 6 4 1,120 2.05 3 107

row_label: A. hydrophila AE036 | Penicillin G


substrate_name: tazobactam

column_label: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonam; row Tazobactam; enzyme column block A. hydrophila AE036; column Km (uM) raw value 440; column kcat (s^-1) raw value 0.65; column kcat/Km (M^-1 s^-1) raw value 1.50 3 103 (the PDF text layer renders the multiplication sign as 3 and superscript -1 as 21, so this cell reads 1.50e3 in plain notation).

normalized_value_unit_evidence: metric: kcat; raw value: 0.65 s^-1; raw unit: s^-1; normalized value: 0.65 s^(-1); metric: Km; raw value: 440 uM; raw unit: uM; normalized value: 0.44 mM; metric: kcat/Km; normalized value: 1.5 s^(-1)*mM^(-1); assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 0.65 s^-1 is already in s^-1. Km 440 uM = 440/1000 = 0.44 mM. kcat/Km table cell is printed as 1.50 3 103 in the on-disk text layer (scientific notation, mantissa then the multiplication sign rendered as 3, then the power of ten), i.e. 1500 M^-1 s^-1; 1500/1000 = 1.5 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonam; row Tazobactam; A. hydrophila AE036 block; metric: kcat; raw value: 0.65; raw unit: s^-1; metric: Km; raw value: 440; raw unit: uM; metric: kcat/Km; raw value: 1500; raw unit: M^-1 s^-1; normalized value: 1.5 s^-1 mM^-1; assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements.

row_label: Tazobactam

substrate: tazobactam


substrate_name: Epicillin

column_label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillins; row Epicillin; enzyme column block A. hydrophila AE036; column Km (uM) raw value 300; column kcat (s^-1) raw value 0.60; column kcat/Km (M^-1 s^-1) raw value 2.00 3 103 (the PDF text layer renders the multiplication sign as 3 and superscript -1 as 21, so this cell reads 2.00e3 in plain notation).

normalized_value_unit_evidence: metric: kcat; raw value: 0.60 s^-1; raw unit: s^-1; normalized value: 0.6 s^(-1); metric: Km; raw value: 300 uM; raw unit: uM; normalized value: 0.3 mM; metric: kcat/Km; normalized value: 2.0 s^(-1)*mM^(-1); assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 0.60 s^-1 is already in s^-1. Km 300 uM = 300/1000 = 0.3 mM. kcat/Km table cell is printed as 2.00 3 103 in the on-disk text layer (scientific notation, mantissa then the multiplication sign rendered as 3, then the power of ten), i.e. 2000 M^-1 s^-1; 2000/1000 = 2.0 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillins; row Epicillin; A. hydrophila AE036 block; metric: kcat; raw value: 0.60; raw unit: s^-1; metric: Km; raw value: 300; raw unit: uM; metric: kcat/Km; raw value: 2000; raw unit: M^-1 s^-1; normalized value: 2.0 s^-1 mM^-1; assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements.

row_label: Epicillin

substrate: Epicillin


column_label: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonam; row HRE-664; enzyme column block A. hydrophila AE036; column Km (uM) raw value 140; column kcat (s^-1) raw value 10.0; column kcat/Km (M^-1 s^-1) raw value 7.15 3 104 (the PDF text layer renders the multiplication sign as 3 and superscript -1 as 21, so this cell reads 7.15e4 in plain notation).

normalized_value_unit_evidence: metric: kcat; raw value: 10.0 s^-1; raw unit: s^-1; normalized value: 10.0 s^(-1); metric: Km; raw value: 140 uM; raw unit: uM; normalized value: 0.14 mM; metric: kcat/Km; normalized value: 71.5 s^(-1)*mM^(-1); assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 10.0 s^-1 is already in s^-1. Km 140 uM = 140/1000 = 0.14 mM. kcat/Km table cell is printed as 7.15 3 104 in the on-disk text layer (scientific notation, mantissa then the multiplication sign rendered as 3, then the power of ten), i.e. 71500 M^-1 s^-1; 71500/1000 = 71.5 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 6. Kinetic parameters of metallo-b-lactamases with penems, tazobactam (YTR-830), and carumonam; row HRE-664; A. hydrophila AE036 block; metric: kcat; raw value: 10.0; raw unit: s^-1; metric: Km; raw value: 140; raw unit: uM; metric: kcat/Km; raw value: 71500; raw unit: M^-1 s^-1; normalized value: 71.5 s^-1 mM^-1; assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements.


substrate_name: H2O; HRE-664 / mixed beta-lactam source group

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=8
Raw SKiD Env: Temp=-----, pH=9
Raw SKiD Env: Temp=30°C, pH=6.5


substrate_name: Meropenem

column_label: TABLE 7. Kinetic parameters of metallo-b-lactamases with carbapenem antibiotics; row Meropenem; enzyme column block A. hydrophila AE036; column Km (uM) raw value 250; column kcat (s^-1) raw value 440; column kcat/Km (M^-1 s^-1) raw value 1.75 3 106 (the PDF text layer renders the multiplication sign as 3 and superscript -1 as 21, so this cell reads 1.75e6 in plain notation).

normalized_value_unit_evidence: metric: kcat; raw value: 440 s^-1; raw unit: s^-1; normalized value: 440.0 s^(-1); metric: Km; raw value: 250 uM; raw unit: uM; normalized value: 0.25 mM; metric: kcat/Km; normalized value: 1750.0 s^(-1)*mM^(-1); assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 440 s^-1 is already in s^-1. Km 250 uM = 250/1000 = 0.25 mM. kcat/Km table cell is printed as 1.75 3 106 in the on-disk text layer (scientific notation, mantissa then the multiplication sign rendered as 3, then the power of ten), i.e. 1750000 M^-1 s^-1; 1750000/1000 = 1750.0 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 7. Kinetic parameters of metallo-b-lactamases with carbapenem antibiotics; row Meropenem; A. hydrophila AE036 block; metric: kcat; raw value: 440; raw unit: s^-1; metric: Km; raw value: 250; raw unit: uM; metric: kcat/Km; raw value: 1750000; raw unit: M^-1 s^-1; normalized value: 1750.0 s^-1 mM^-1; assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements.

row_label: Meropenem

substrate: Meropenem


substrate_name: Temocillin

column_label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillins; row Temocillin; enzyme column block A. hydrophila AE036; column Km (uM) raw value 65; column kcat (s^-1) raw value 1.75; column kcat/Km (M^-1 s^-1) raw value 2.70 3 104 (the PDF text layer renders the multiplication sign as 3 and superscript -1 as 21, so this cell reads 2.70e4 in plain notation).

normalized_value_unit_evidence: metric: kcat; raw value: 1.75 s^-1; raw unit: s^-1; normalized value: 1.75 s^(-1); metric: Km; raw value: 65 uM; raw unit: uM; normalized value: 0.065 mM; metric: kcat/Km; normalized value: 27.0 s^(-1)*mM^(-1); assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 1.75 s^-1 is already in s^-1. Km 65 uM = 65/1000 = 0.065 mM. kcat/Km table cell is printed as 2.70 3 104 in the on-disk text layer (scientific notation, mantissa then the multiplication sign rendered as 3, then the power of ten), i.e. 27000 M^-1 s^-1; 27000/1000 = 27.0 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillins; row Temocillin; A. hydrophila AE036 block; metric: kcat; raw value: 1.75; raw unit: s^-1; metric: Km; raw value: 65; raw unit: uM; metric: kcat/Km; raw value: 27000; raw unit: M^-1 s^-1; normalized value: 27.0 s^-1 mM^-1; assay condition: All assays at 30 C in 30 mM sodium cacodylate buffer, pH 6.5, containing 0.1 mM ZnCl2; table footnote a: for all data, the standard deviation values were below 10% of the mean of five different measurements.

row_label: Temocillin

substrate: Temocillin


substrate_name: Cephaloridine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P26918 plus PDBe/RCSB 1X8G author-residue mapping and applied mutation signature R121H to reconstruct the assayed variant sequence.

substrate: Cephaloridine


sequence_source: UniProtKB reviewed accession P26918 plus PDBe/RCSB 1X8G author-residue mapping


substrate_name: Oxacillin

substrate: Oxacillin


substrate_name: cephalothin

sequence_source: UniProtKB B2BSN6 direct FASTA lookup, retrieved 2026-05-27; entry is Aeromonas enteropelogenes beta-lactamase ampC with EC 3.5.2.6.

substrate: cephalothin


substrate_name: ampicillin

substrate: ampicillin


substrate_name: cefpirome

substrate: cefpirome