sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature V469A to reconstruct the assayed variant sequence.


enzyme_display_name: alcohol dehydrogenase

organism: Acetobacter pasteurianus

substrate_name: NAD+

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 8.5; 298.15 K; cofactor NAD+

proof_lines:
isozyme ADH II, pH 8.5, 25°C
isozyme ADH II, pH 6.0, 25°C
isozyme ADH I, pH 5.5, 25°C

enzyme: alcohol dehydrogenase

substrate: NAD+

source: brenda


organism: Equus caballus

proof_lines:
wild-type enzyme Adh 1
wilde-type enzyme ADh1
wild-type enzyme Adh1


organism: Homo sapiens

substrate_name: all-trans-retinal

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

proof_lines:
pH 7.5, 25°C, isozyme ADH1B2
pH 7.5, anodic enzyme form
pH 7.5, 25°C, isozyme ADH4

substrate: all-trans-retinal


organism: Hordeum vulgare

substrate_name: ethanol

assay_conditions_summary: cofactor NAD+

proof_lines:
isoenzyme III from leaf
isoenzyme II from leaf
isoenzyme I from leaf

substrate: ethanol


organism: Mesocricetus auratus

substrate_name: Cyclohexanol

proof_lines:
isoenzyme BB-ADH
isoenzyme TT-ADH
isoenzyme AA-ADH

substrate: Cyclohexanol


organism: Mus musculus

substrate_name: Hexanol

assay_conditions_summary: pH 7.5; 298.15 K; buffer 0.1 M Na-K phosphate

proof_lines:
recombinant isozyme ADH1, pH 7.5, 25°C
recombinant isozyme ADH1, pH 10.5, 25°C
recombinant isozyme ADH4, pH 7.5, 25°C

substrate: Hexanol


organism: Rattus norvegicus

assay_conditions_summary: pH 10

proof_lines:
isoenzyme ADH-3, pH 10.0
isoenzyme ADH-1, pH 10.0
isoenzyme ADH-12, pH 10.0


organism: Saccharomyces cerevisiae

substrate_name: propanal

assay_conditions_summary: pH 7; 303.15 K; cofactor NAD+

substrate: propanal


organism: Unknown

substrate_name: all-trans retinol

substrate: all-trans retinol


organism: Zymomonas mobilis

substrate_name: acetaldehyde

proof_lines:
enzyme form ADH II
enzyme form ADH I

substrate: acetaldehyde


organism: Aeropyrum pernix

substrate_name: NADH

protein_accession_database: UniProt

sequence_source: Direct UniProtKB REST lookup for Q9Y9P9 during worker run 20260619-232845-95620

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

assay_conditions_summary: pH 8; 333.15 K; cofactor NAD+

substrate: NADH


organism: Arabidopsis thaliana

sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P06525 during worker run 20260619-232845-95620 and applied mutation signature C243S to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: recombinant His-tagged mutant C243S, pH 7.5, temperature not specified in the publication


sequence_source: Direct UniProtKB REST lookup for P06525 during worker run 20260619-232845-95620

proof_lines: recombinant His-tagged wild-type enzyme, pH 7.5, temperature not specified in the publication


sequence_source: Direct UniProtKB REST lookup for P00327 during worker run 20260619-232845-95620

proof_lines:
pH 9.0, 25°C, recombinant enzyme
pH 11.0, 25°C, recombinant enzyme
pH 7.0, 25°C, recombinant enzyme


organism: Euglena gracilis

sequence_source: Direct UniProtKB REST lookup for B8QU18 during worker run 20260619-232845-95620

assay_conditions_summary: pH 9; 298.15 K; buffer bis-Tris propane; cofactor NAD+

proof_lines:
at pH 9.0 in bis-Tris propane buffer
at pH 7.0 and 25°C


organism: Flavobacterium frigidimaris

sequence_source: Direct UniProtKB REST lookup for Q8L3C9 during worker run 20260619-232845-95620


organism: Geobacillus stearothermophilus

substrate_name: benzyl alcohol

sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P42328 during worker run 20260619-232845-95620 and applied mutation signature W87A to reconstruct the assayed variant sequence.

substrate: benzyl alcohol


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P42328 during worker run 20260619-232845-95620 and applied mutation signature Y25A to reconstruct the assayed variant sequence.

proof_lines: mutant Y25A, 30°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P42328 during worker run 20260619-232845-95620 and applied mutation signature Y25A/W49F/W87F to reconstruct the assayed variant sequence.

assay_conditions_summary: 303.15 K; cofactor NAD+

proof_lines: mutant Y25A/W49F/W87F, 30°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P42328 during worker run 20260619-232845-95620 and applied mutation signature W49F/W167Y to reconstruct the assayed variant sequence.

proof_lines: mutant W49F/W167Y, 30°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P42328 during worker run 20260619-232845-95620 and applied mutation signature V260A to reconstruct the assayed variant sequence.

proof_lines: mutant V260A, 30°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P42328 during worker run 20260619-232845-95620 and applied mutation signature W49F/W87F to reconstruct the assayed variant sequence.

proof_lines: mutant W49F/W87F, 30°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P42328 during worker run 20260619-232845-95620 and applied mutation signature Y25A/W49F/W87F/V260A to reconstruct the assayed variant sequence.

proof_lines: mutant Y25A/W49F/W87F/V260A, 30°C, pH not specified in the publication


sequence_source: Direct UniProtKB REST lookup for P42328 during worker run 20260619-232845-95620

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


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P42328 during worker run 20260619-232845-95620 and applied mutation signature W49F/W87F/V260A to reconstruct the assayed variant sequence.

proof_lines: mutant W49F/W87F/V260A, 30°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P42328 during worker run 20260619-232845-95620 and applied mutation signature Y25A/W49F/W167Y/V260A to reconstruct the assayed variant sequence.

proof_lines: mutant Y25A/W49F/W167Y/V260A, 30°C, pH not specified in the publication


organism: Ogataea angusta

sequence_source: UniProtKB direct accession lookup: H9ZGN0

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

proof_lines:
pH 9.0, 22°C, recombinant enzyme
pH 6.0, 22°C, recombinant enzyme


organism: Picrophilus oshimae


organism: Pyrobaculum calidifontis

sequence_source: UniProtKB direct accession lookup: A3MVR8

assay_conditions_summary: pH 10; 333.15 K; cofactor NAD+


organism: Pyrococcus furiosus

sequence_source: UniProtKB direct accession lookup: Q8TZM9

assay_conditions_summary: pH 8.8; 343.15 K; cofactor NAD+

proof_lines:
pH 8.8, 70°C
pH 6.1, 70°C
reduction reaction, pH 6.1, 70°C


organism: Saccharolobus solfataricus

substrate_name: n-Propanol

proof_lines: 2 mM zinc sulfate in 100 mM glycine-NaOH (pH 10.5) at 65°C

substrate: n-Propanol


sequence_source: UniProtKB direct accession lookup: P39462

assay_conditions_summary: pH 10.5; 338.15 K; buffer 0.1 M glycine-NaOH

proof_lines: wild type enzyme, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C


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

assay_conditions_summary: pH 10.5; 338.15 K; buffer 0.1 M glycine-NaOH; cofactor NAD+

proof_lines: mutant enzyme W95L, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C

proof_lines: mutant enzyme W95L,, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C


proof_lines: Km above 50 mM, mutant enzyme W95L/N249Y, in 0.1 M glycine-NaOH buffer (pH 10.5), at 65°C


sequence_source: UniProtKB direct accession lookup: P00330


substrate_name: furfural

sequence_source: UniProtKB direct accession lookup: P28625

assay_conditions_summary: pH 7; 303.15 K; cofactor NADH

substrate: furfural


organism: Saccharomyces pastorianus

sequence_source: UniProtKB direct accession lookup: B6UQD0

assay_conditions_summary: pH 7.3; 303.15 K; cofactor NAD+

proof_lines: in the presence of 2 mM NAD+, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C

proof_lines: in the presence of 0.25 mM NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C

proof_lines: in the presence of 0.1 mM NADH, in 83 mM potassium phosphate, 40 mM KCl, and 0.25 mM EDTA buffer, pH 7.3, at 30°C


organism: Scyliorhinus canicula

substrate_name: Octanol

sequence_source: UniProtKB direct accession lookup: P86884

proof_lines: pH and temperature not specified in the publication

substrate: Octanol


organism: Sphingomonas sp. A1

substrate_name: D-altronate

sequence_source: UniProtKB direct accession lookup: A0A075B5H4

assay_conditions_summary: pH 7.9; 298.15 K; cofactor NADH

substrate: D-altronate


organism: Sulfolobus acidocaldarius

sequence_source: UniProtKB direct accession lookup: Q4J702

assay_conditions_summary: pH 5.5; 338.15 K; cofactor NAD+


substrate_name: cycloheptanol

sequence_source: UniProtKB direct accession lookup: Q4J9F2

substrate: cycloheptanol


organism: Sulfolobus sp.

substrate_name: benzylalcohol

sequence_source: UniProtKB direct accession lookup: P50381

substrate: benzylalcohol


organism: Zea mays

sequence_source: GenBank:L23548.1; EMBL/UniProt protein:AAB59302.1; UniProt:Q41766

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 ADH1-1S1108
mutant enzyme ADH1S-1108


sequence_source: GenBank:X04049.1; protein:CAA27681.1


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession lookup: P42328 and applied mutation signature Y25A/W49F/W167Y to reconstruct the assayed variant sequence.

proof_lines: mutant Y25A/W49F/W167Y, 30°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession lookup: P42328 and applied mutation signature W49F/W167Y/V260A to reconstruct the assayed variant sequence.

proof_lines: mutant W49F/W167Y/V260A, 30°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession lookup: P42328 and applied mutation signature C257L to reconstruct the assayed variant sequence.


organism: Geobacillus thermodenitrificans

substrate_name: NADP+

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

assay_conditions_summary: pH 8; 333.15 K; cofactor NADP+

proof_lines:
cosubstrate ethanol, pH 8, 60°C
pH 8, 60°C
cosubstrate acetaldehyde, pH 8, 60°C

substrate: NADP+


organism: Haloferax volcanii

sequence_source: UniProt REST direct accession lookup: D4GSN2

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

assay_conditions_summary: pH 6; cofactor NAD+

proof_lines: pH 6.0, temperature not specified in the publication

proof_lines: pH 11.0, temperature not specified in the publication


organism: Homo sapiens

proof_lines: isozyme ADH4, using 1-hydroxymethylpyrene as substrate


proof_lines:
isozyme ADH2, at 21-23°C
isozyme ADH1C, at 21-23°C
isozyme ADH3, at 21-23°C


organism: Kluyveromyces marxianus

sequence_source: UniProt REST direct accession lookup: V9SFA1

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication


sequence_source: UniProt REST direct accession lookup: G3FFC9


sequence_source: UniProt REST direct accession lookup: V9SCJ1


sequence_source: UniProt REST direct accession lookup: V9SDP6


organism: Moraxella sp.

sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession lookup: Q8GIX7 and applied mutation signature A25Y to reconstruct the assayed variant sequence.


sequence_source: UniProt REST direct accession lookup: Q8GIX7


organism: Mus musculus

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

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

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

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

substrate: Unknown


organism: Mycobacterium sp.

sequence_source: UniProt REST direct accession lookup: W8VSK8

proof_lines:
cosubstrate NAD+, pH 7.0, 30°C
cosubstrate butanal, pH 7.0, 30°C
cosubstrate NADH, pH 7.0, 30°C


organism: Alligator mississippiensis

substrate_name: butanol

sequence_source: UniProtKB reviewed P80222 / ADH1_ALLMI; reference PMID 8365416

substrate: butanol


organism: Arabidopsis thaliana

substrate_name: ethanol

assay_conditions_summary: pH 10.5; 298.15 K; cofactor NAD+

substrate: ethanol


organism: Aspergillus nidulans

assay_conditions_summary: cofactor NAD+

proof_lines:
reduction of propan-2-ol
reduction of ethanol


organism: Bacillus subtilis

proof_lines: in the presence of 0.025 mM Cu2+, at pH 9.5 and 37°C

proof_lines: in the presence of 0.025 mM Zn2+, at pH 9.5 and 37°C


organism: Brassica napus

assay_conditions_summary: 296.15 K; cofactor NAD+


organism: Brevibacterium sp.

substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


organism: [Candida] sp.

substrate_name: NAD+

substrate: NAD+


organism: Carboxydothermus hydrogenoformans

substrate_name: ethyl pyruvate

substrate: ethyl pyruvate


organism: Chlamydomonas moewusii


organism: Citrobacter sp. S-77


organism: Corynebacterium glutamicum R

substrate_name: propanal

proof_lines:
33°C, pH 7
33°C, pH 8

substrate: propanal


organism: Coturnix coturnix

proof_lines:
enzyme form ADH-2
enzyme form ADH-3
oxidation of ethanol


organism: Thermococcus kodakarensis

verification_status: unverified

sequence_source: UniProtKB REST accession Q5JI09, unreviewed TrEMBL entry Q5JI09_THEKO

assay_conditions_summary: pH 9; 343.15 K; cofactor NADP+

proof_lines: cosubstrate 2,3-butanediol, pH 9.0, 70°C

proof_lines: cosubstrate 1-phenylethanol, pH 9.0, 70°C

status: unverified


organism: Thermoplasma acidophilum

sequence_source: UniProtKB REST accession Q9HIM3, unreviewed TrEMBL entry Q9HIM3_THEAC


organism: Thermus sp.

sequence_source: UniProtKB REST accession B2ZRE3, unreviewed TrEMBL entry B2ZRE3_9DEIN

assay_conditions_summary: pH 6; 333.15 K; cofactor NAD+

proof_lines:
in 200 mM bicine, pH 6.0, at 60°C
in 200 mM bicine, pH 9.0, at 60°C


organism: Yokenella sp.

substrate_name: NADPH

sequence_source: UniProtKB REST accession W6CX26, unreviewed TrEMBL entry W6CX26_9ENTR

assay_conditions_summary: pH 6.5; 338.15 K; cofactor NADP+

substrate: NADPH


organism: Rhodococcus ruber

proof_lines: pH 6.0, 37°C, recombinant enzyme expressed from Saccharomyces cerevisiae

proof_lines: pH 6.0, 37°C, recombinant enzyme expressed from Arxula adeninivorans

proof_lines: pH 6.0, 37°C, recombinant enzyme expressed from Hansenula polymorpha


organism: Saccharolobus solfataricus

assay_conditions_summary: 338.15 K; cofactor NAD+

proof_lines: wild type enzyme, at 65°C, in the presence of benzaldehyde

proof_lines: wild type enzyme, at 65°C, in the presence of benzyl alcohol


substrate_name: Cyclohexanol

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

proof_lines: mutant enzyme N249Y, at 65°C, in the presence of benzyl alcohol

proof_lines: mutant enzyme N249Y, at 65°C, in the presence of benzaldehyde

substrate: Cyclohexanol


assay_conditions_summary: pH 9.2; 338.15 K; cofactor NAD+

proof_lines: in the presence of 3 mM NAD+, in 0.1 M glycine-NaOH, pH 9.2, at 65°C

proof_lines: in 50 mM Tris-HCl (pH 7.5) containing 0.2 mM NADH + H+, at 65°C


organism: Saccharomyces cerevisiae

substrate_name: acetaldehyde

substrate: acetaldehyde


organism: Saimiri sciureus

proof_lines:
pyrazole-sensitive enzyme, pH 7.5
pyrazole-sensitive enzyme, pH 7.0
pyrazole-insensitive enzyme, pH 10.0


organism: Scaptodrosophila lebanonensis

proof_lines:
oxidation of propan-2-ol
oxidation of ethanol


organism: Sporotrichum pulverulentum


organism: Sus scrofa

substrate_name: NADH

assay_conditions_summary: cofactor NADPH

substrate: NADH


organism: Thermomicrobium roseum


organism: Thermus thermophilus

assay_conditions_summary: pH 10.5; 338.15 K; cofactor NAD+


organism: Crocus sativus

assay_conditions_summary: pH 8.5; cofactor NAD+


organism: Devosia riboflavina


organism: Drosophila melanogaster


organism: Equus caballus

substrate_name: hexyl alcohol

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NAD+

proof_lines:
reduction with NADH
oxidation with NAD+
pH 7.6

substrate: hexyl alcohol


organism: Escherichia coli


organism: Fragaria x ananassa


organism: Geobacillus stearothermophilus

substrate_name: cinnamaldehyde

assay_conditions_summary: pH 7.7; 333.15 K; cofactor NAD+

substrate: cinnamaldehyde


organism: Glycine max


organism: Hafnia alvei


organism: Klebsiella oxytoca


organism: Klebsiella pneumoniae


organism: Leifsonia sp.

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+


organism: Magnusiomyces capitatus

assay_conditions_summary: pH 6; cofactor NAD+


organism: Megalodesulfovibrio gigas

proof_lines:
reduction of acetaldehyde
oxidation of ethanol


organism: Methylorubrum extorquens

substrate_name: methanol

substrate: methanol


organism: Meyerozyma guilliermondii


organism: Natronomonas pharaonis

proof_lines:
40°C, pH 9.0, 50 mM Tris-HCl, 4 M NaCl
70°C, pH 9.0, 50 mM Tris-HCl, 4 M NaCl


organism: Oenococcus oeni

assay_conditions_summary: pH 9; 333.15 K; cofactor NAD+

proof_lines:
pH 9.0, 60°C, recombinant enzyme
pH 8.0, 60°C, recombinant enzyme


organism: Oncorhynchus mykiss

proof_lines:
enzyme from liver
enzyme from caecum


organism: Oryctolagus cuniculus

assay_conditions_summary: pH 7.5; cofactor NAD+


organism: Oryza sativa


organism: Parageobacillus thermoglucosidasius

assay_conditions_summary: pH 6; 333.15 K; cofactor NADH

proof_lines: alcohol dehydrogenase domain, 60°C, pH 6.0, presence of 0.1 mM Zn2+


proof_lines: wild-type, 60°C, pH 6.0, presence of 0.1 mM Zn2+


organism: Petroselinum crispum


organism: Pseudomonas aeruginosa

substrate_name: ethylene glycol

substrate: ethylene glycol


organism: Pyrococcus furiosus

assay_conditions_summary: pH 6.1; 318.15 K; cofactor NADP+

proof_lines: 45°C, pH 6.1, cosubstrate: 3-hydroxy-2-butanone, wild-type enzyme

proof_lines: 45°C, pH 6.1, cosubstrate: NADPH, wild-type enzyme

proof_lines: 45°C, pH 8.8, cosubstrate: NAD+, wild-type enzyme


assay_conditions_summary: pH 6.1; 318.15 K; cofactor NAD+

proof_lines: 45°C, pH 6.1, cosubstrate: 3-hydroxy-2-butanone, mutant enzyme K249G/H255R

proof_lines: 45°C, pH 6.1, cosubstrate: NADH, mutant enzyme K249G/H255R

proof_lines: 45°C, pH 8.8, cosubstrate: 2,3-butanediol, mutant enzyme K249G/H255R


mutation_type: insertion

assay_conditions_summary: pH 8.8; 318.15 K; cofactor NADP+

proof_lines: pH 8.8, 45°C, mutant enzyme G211InsG, cofactor: NADP+

proof_lines: pH 8.8, 45°C, mutant enzyme G211InsG, cofactor: NAD+


proof_lines: pH 8.8, 45°C, mutant enzyme G211InsC, cofactor: NADP+

proof_lines: pH 8.8, 45°C, mutant enzyme G211InsC, cofactor: NAD+


proof_lines: pH 8.8, 45°C, mutant enzyme G211InsS, cofactor: NADP+

proof_lines: pH 8.8, 45°C, mutant enzyme G211InsS, cofactor: NAD+


proof_lines: pH 8.8, 45°C, mutant enzyme G211S, cofactor: NAD+

proof_lines: pH 8.8, 45°C, mutant enzyme G211S, cofactor: NADP+


proof_lines: pH 8.8, 45°C, mutant enzyme G211InsA, cofactor: NADP+

proof_lines: pH 8.8, 45°C, mutant enzyme G211InsA, cofactor: NAD+


proof_lines: pH 8.8, 45°C, mutant enzyme G211C, cofactor: NAD+

proof_lines: pH 8.8, 45°C, mutant enzyme G211C, cofactor: NADP+


enzyme_display_name: glutamyl endopeptidase

organism: Enterococcus faecalis

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

enzyme: glutamyl endopeptidase


organism: Triticum monococcum

assay_conditions_summary: cofactor NAD+


organism: Bacillus intermedius


organism: Bacillus licheniformis


organism: Staphylococcus aureus

proof_lines: pH and temperature not specified in the publication


organism: Staphylococcus epidermidis


organism: Streptomyces griseus

substrate_name: succinyl-Ala-Ala-Pro-Glu-p-nitroanilide

substrate: succinyl-Ala-Ala-Pro-Glu-p-nitroanilide


enzyme_display_name: cellulase

organism: Alicyclobacillus acidocaldarius

substrate_name: carboxymethylcellulose

proof_lines: mutant lacking the IgG-like domain, pH 7.5, 65°C

enzyme: cellulase

substrate: carboxymethylcellulose


organism: Bacillus sp.

substrate_name: H2O; n m m+n m n m+n n m m+n m n m+n Carboxymethylcellulose

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

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


substrate_name: p-Nitrophenyl-beta-D-cellotrioside; H2O

proof_lines: SABIO-RK modifier species: cellulase(Enzyme) mutant D154N

substrate: p-Nitrophenyl-beta-D-cellotrioside; H2O


substrate_name: H2O; p-Nitrophenyl-beta-D-cellotrioside

proof_lines: SABIO-RK modifier species: cellulase(Enzyme) mutant D193N

substrate: H2O; p-Nitrophenyl-beta-D-cellotrioside


proof_lines: SABIO-RK modifier species: cellulase(Enzyme) mutant E130Q


proof_lines: SABIO-RK modifier species: cellulase(Enzyme) mutant D191N


proof_lines: SABIO-RK modifier species: cellulase(Enzyme) mutant D300N


organism: Bacillus sp. (in: firmicutes)

substrate_name: carboxymethyl cellulose

substrate: carboxymethyl cellulose


organism: Bacillus subtilis

substrate_name: H2O; m n m+n m n m+n Carboxymethylcellulose

mutation_type: truncation

proof_lines: SABIO-RK modifier species: cellulase(Enzyme) mutant Egl330 (truncated C-terminus)

unit: lgwedgeoneswedgeone


substrate_name: m n m+n m n m+n Carboxymethylcellulose; H2O


substrate_name: 4-Nitrophenyl-beta-cellobioside; H2O

proof_lines: SABIO-RK modifier species: cellulase(Enzyme) mutant chimera (amino acids 196-287 from P06566)

substrate: 4-Nitrophenyl-beta-cellobioside; H2O


organism: bacterium enrichment culture

substrate_name: Avicel

substrate: Avicel


organism: Cellulomonas fimi

substrate_name: phosphoric acid swollen cellulose

substrate: phosphoric acid swollen cellulose


organism: Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)

substrate_name: 4-nitrophenyl acetate

source_db: uniprot

proof_lines: kcat is 7032 min(-1) for the deacetylation of 4-nitrophenyl acetate. kcat is 12 min(-1) for the deacetylation of birchwood xylan. kcat is 1.1 min(-1) for the deacetylation of glucomannan.

substrate: 4-nitrophenyl acetate

source: uniprot


organism: Fomes meliae

sequence: QAVLSETGGGDTASCDEYLYQELAYVK

wild_type_sequence: QAVLSETGGGDTASCDEYLYQELAYVK

proof_lines: Kcat is 129.41/sec for hydrolysis of carboxymethylcellulose (at pH 4.8 and 55 degrees Celsius).


organism: Thermoanaerobacterium sp

proof_lines: kcat is 46.3 sec(-1) with carboxymethyl cellulose as substrate.


organism: Aspergillus versicolor

sequence: VAAIQTVLG

wild_type_sequence: VAAIQTVLG


organism: Microbulbifer sp. (strain ALW1)

substrate_name: barley beta-glucan

substrate: barley beta-glucan


organism: Phanerodontia chrysosporium

substrate_name: carboxymethyl-cellulose (CMC)

substrate: carboxymethyl-cellulose (CMC)


organism: Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)

substrate_name: barley beta-glucan (when expressed in M.oryzae)


substrate: barley beta-glucan (when expressed in M.oryzae)


organism: Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799)


sequence_source: UniProtKB REST F4H413 direct accession check on 2026-06-20


sequence_source: UniProtKB REST P07984 direct accession check on 2026-06-20


organism: Escherichia coli

sequence_source: UniProtKB REST P37651 direct accession check on 2026-06-20


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P37651 direct accession check on 2026-06-20 and applied mutation signature G117S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P37651 direct accession check on 2026-06-20 and applied mutation signature V9A/K353E to reconstruct the assayed variant sequence.


organism: Mahella australiensis

sequence_source: UniProtKB REST F4A377 direct accession check on 2026-06-20

proof_lines: pH 7.5, 65°C, in presence of 0.5 mM Co2+


sequence_source: UniProtKB REST Q66NB7 direct accession check on 2026-06-20


organism: Pyrococcus furiosus

substrate_name: 4-nitrophenyl cellopentaoside

sequence_source: UniProtKB REST Q9V2T0 direct accession check on 2026-06-20

substrate: 4-nitrophenyl cellopentaoside


organism: Pyrococcus horikoshii

substrate_name: p-nitrophenyl cellobiose

sequence_variant_note: Resolved canonical sequence from UniProtKB REST O58925 direct accession check on 2026-06-20 and applied mutation signature C372A/C412A to reconstruct the assayed variant sequence.

substrate: p-nitrophenyl cellobiose


sequence_variant_note: Resolved canonical sequence from UniProtKB REST O58925 direct accession check on 2026-06-20 and applied mutation signature C106A/C159A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST O58925 direct accession check on 2026-06-20 and applied mutation signature C106A/C159A/C372A/C412A to reconstruct the assayed variant sequence.

proof_lines: 50°C, mutant enzyme C106A/C159A/C372A/C412A


sequence_source: UniProtKB REST O58925 direct accession check on 2026-06-20

proof_lines:
50°C, wild-type enzyme
pH 5-6, 50°C, wild-type enzyme
pH 5.5, 50°C, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB REST O58925 direct accession check on 2026-06-20 and applied mutation signature R156A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST O58925 direct accession check on 2026-06-20 and applied mutation signature H161A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST O58925 direct accession check on 2026-06-20 and applied mutation signature E163A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST O58925 direct accession check on 2026-06-20 and applied mutation signature C159A to reconstruct the assayed variant sequence.


organism: Trichoderma reesei

substrate_name: 4-nitrophenyl D-cellobioside

sequence_source: UniProtKB REST direct lookup P62694 on 2026-06-20; reviewed entry GUX1_TRIRF

substrate: 4-nitrophenyl D-cellobioside


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

proof_lines: N-glycosylation mutant residue 384, pH 4.8, 45°C

proof_lines: N-glycosylation mutant residue D270, pH 4.8, 45°C

proof_lines: N-glycosylation mutant residue D45, pH 4.8, 45°C


substrate_name: 4-methylumbelliferyl cellobioside

sequence_source: UniProtKB REST direct lookup P07981 on 2026-06-20; reviewed entry GUN1_TRIRF

substrate: 4-methylumbelliferyl cellobioside


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P07981 direct lookup on 2026-06-20 using UniProt signal peptide 1-22/chain 23-459 and source mutation Q274V and applied mutation signature Q274V with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P07981 direct lookup on 2026-06-20 using UniProt signal peptide 1-22/chain 23-459 and source mutation Q126F and applied mutation signature Q126F with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P07981 direct lookup on 2026-06-20 using UniProt signal peptide 1-22/chain 23-459 and source mutation K272F and applied mutation signature K272F with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


organism: uncultured bacterium

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


organism: uncultured rumen bacterium


organism: Volvariella volvacea

sequence_source: UniProtKB REST direct lookup B3GQ73 on 2026-06-20; unreviewed entry B3GQ73_9AGAR

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


organism: Xanthomonas campestris pv. campestris

substrate_name: carboxymethylcellulose

sequence_source: UniProtKB REST direct lookup P19487 on 2026-06-20; reviewed entry GUNA_XANCP


organism: Acetivibrio thermocellus

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

proof_lines: pH 4.2, 60°C, recombinant mutant CtGH5-F194A

proof_lines: pH 4.2, 60°C, recombinant chimeric mutant CtGH1-CtGH5-F194A

proof_lines: pH 4.2, 60°C, recombinant mutant CtGH1-CtGH5-F194A


substrate_name: lichenan

proof_lines: pH 4.2, 60°C, recombinant wild-type enzyme CtGH5

substrate: lichenan


organism: Aspergillus fumigatus


organism: Aspergillus niger


organism: Bacillus sp. (in: firmicutes)


organism: Bacillus subtilis

proof_lines: the turnover rate (kcat) of Egl330 increased by 78% compared to wild-type


organism: Beltraniella portoricensis

substrate_name: Unknown

substrate: Unknown


organism: Cellulomonas biazotea

substrate_name: carboxymethyl cellulose

proof_lines: enzyme from deoxyglucose- and streptomycin-resistant mutant 51 Smr


organism: Cellulomonas fimi

proof_lines:
pH 7.0, 37°C, oxidized mutant D216C
pH 7.0, 37°C, mutant D216C


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature G158A to reconstruct the assayed variant sequence.

data_origin: experimental

status: corrected


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature I162A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature T160A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature I157A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature P164A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature H155A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature H297N to reconstruct the assayed variant sequence.


mutation_type: deletion


proof_lines: pH 5-6, 50°C, mutant enzyme lacking 5 residues at the C-terminus and 5 residies at the N-terminus


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature Y299F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature E201Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature D385N to reconstruct the assayed variant sequence.


substrate_name: 4-nitrophenyl cellobioside

kcat_over_km_origin: calculated

substrate: 4-nitrophenyl cellobioside


organism: Rasamsonia emersonii

substrate_name: 4-methylumbelliferyl beta-D-lactoside

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

substrate: 4-methylumbelliferyl beta-D-lactoside


proof_lines:
wild-type, pH 5.0, 22°C
deglycosylated wild-type, pH 5.0, 22°C


organism: Saccharolobus solfataricus

proof_lines: pH and temperature not specified in the publication, hybrid protein (CelA-SSO1949-CelA, consisting of 262 amino acids) based on beta-endoglucanase from Sulfolobus solfataricus P2 and beta-endoglucanase from Thermotoga maritima


organism: Talaromyces verruculosus

substrate_name: beta-Glucan

substrate: beta-Glucan


organism: Thermobifida fusca

substrate_name: 2,4-dinitrophenyl beta-D-cellobioside

substrate: 2,4-dinitrophenyl beta-D-cellobioside


organism: Thermochaetoides thermophila

proof_lines: recombinant His-tagged enzyme, pH 5.0, 55°C


organism: Thermotoga maritima


proof_lines: pH 3, 80°C, chimeric fusion protein CelA-SSO1949-CelA, that consists of 70 amino acids CelA followed by 163 amino acids SSO1949 and 29 amino acids CelA


substrate: carboxymethyl cellulose


substrate_name: p-nitrophenyl-beta-D-cellotetraoside

substrate: p-nitrophenyl-beta-D-cellotetraoside


organism: Trichoderma atroviride

substrate_name: raffinose

substrate: raffinose


organism: Irpex lacteus

substrate_name: cellohexaose

substrate: cellohexaose


organism: Mycothermus thermophilus

proof_lines:
presence of Mn2+, pH 5.5, 60°C
absence of Mn2+, pH 5.5, 60°C


organism: Niallia circulans

substrate: carboxymethylcellulose


organism: Pseudoalteromonas haloplanktis

substrate_name: p-nitrophenyl-beta-D-cellobioside

substrate: p-nitrophenyl-beta-D-cellobioside


organism: Pseudoalteromonas sp. DY3


organism: Ruminiclostridium josui

substrate_name: cellopentaose

substrate: cellopentaose


organism: Ruminococcus albus


organism: Salipaludibacillus agaradhaerens

proof_lines:
in presence of 25 mM
in presence of 250 mM


substrate_name: Barley beta-glucan

substrate: Barley beta-glucan


organism: Thermothelomyces thermophilus


organism: Thermotoga petrophila


organism: Trichoderma reesei

substrate_name: soybean husk

proof_lines: substrate: amorphous celulose, endoglucanase Cel 7B

proof_lines: substrate: bacterial celulose, endoglucanase Cel 7B

substrate: soybean husk


organism: Trichoderma viride

substrate_name: cellotetraose

proof_lines:
cellulase II-A
cellulase II-B

substrate: cellotetraose


organism: Virgibacillus salarius


enzyme_display_name: protein-arginine deiminase

organism: Homo sapiens

substrate_name: Nalpha-benzoyl-L-arginine ethyl ester

sequence_variant_note: Resolved canonical sequence from UniProt Q9UM07 canonical FASTA checked during review; PMID 21731701 and NCBI RefSeq link NP_036519.2 anchor the human PADI4 identity. and applied mutation signature R8Q to reconstruct the assayed variant sequence.

enzyme: protein-arginine deiminase

substrate: Nalpha-benzoyl-L-arginine ethyl ester


sequence_variant_note: Resolved canonical sequence from UniProt Q9UM07 canonical FASTA checked during review; PMID 21731701 and NCBI RefSeq link NP_036519.2 anchor the human PADI4 identity. and applied mutation signature D547E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UM07 canonical FASTA checked during review; PMID 21731701 and NCBI RefSeq link NP_036519.2 anchor the human PADI4 identity. and applied mutation signature R8A/D547A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UM07 canonical FASTA checked during review; PMID 21731701 and NCBI RefSeq link NP_036519.2 anchor the human PADI4 identity. and applied mutation signature D273A/R544A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UM07 canonical FASTA checked during review; PMID 21731701 and NCBI RefSeq link NP_036519.2 anchor the human PADI4 identity. and applied mutation signature D547N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UM07 canonical FASTA checked during review; PMID 21731701 and NCBI RefSeq link NP_036519.2 anchor the human PADI4 identity. and applied mutation signature Y435A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UM07 canonical FASTA checked during review; PMID 21731701 and NCBI RefSeq link NP_036519.2 anchor the human PADI4 identity. and applied mutation signature Y237A/E281A to reconstruct the assayed variant sequence.


organism: Cellulomonas fimi

sequence_source: reconstructed from UniProt P07984 canonical CenA sequence after direct UniProt active-site offset check

sequence_variant_note: Mutation signature D392S could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProt P07984 direct REST check

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

proof_lines: pH 7.0, 37°C, H2O2-treated wild-type CenA


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -2, so it is treated as a source-provided variant sequence.

proof_lines:
pH 7.0, 37°C, oxidized mutant D392C
pH 7.0, 37°C, mutant D392C


sequence_variant_note: Mutation signature D392A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -4, so it is treated as a source-provided variant sequence.

proof_lines:
pH 7.0, 37°C, oxidized mutant D252C
pH 7.0, 37°C, mutant D252C


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -5, so it is treated as a source-provided variant sequence.


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

proof_lines:
chimeric xylanase/endoglucanase
endoglucanase A


organism: Chrysosporium lucknowense

proof_lines:
50°C, pH 5.5, endoglucanase EG25
50°C, pH 5.5, endoglucanase EG60
50°C, pH 5.5, endoglucanase EG51


organism: Cohnella sp. A01

substrate_name: carboxymethylcellulose

proof_lines: pH and temperature not specified in the publication


organism: Dickeya chrysanthemi


organism: Geobacillus sp.


organism: Gymnascella citrina


sequence_variant_note: Resolved canonical sequence from UniProt Q9UM07 PADI4_HUMAN canonical sequence; variant reconstructed from PMID 21731701 Table 1 mutation label and applied mutation signature R8E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UM07 PADI4_HUMAN canonical sequence; variant reconstructed from PMID 21731701 Table 1 mutation label and applied mutation signature Y435N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UM07 PADI4_HUMAN canonical sequence; variant reconstructed from PMID 21731701 Table 1 mutation label and applied mutation signature D547A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UM07 PADI4_HUMAN canonical sequence; variant reconstructed from PMID 21731701 Table 1 mutation label and applied mutation signature R8H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UM07 PADI4_HUMAN canonical sequence; variant reconstructed from PMID 21731701 Table 1 mutation label and applied mutation signature R8E/D547E to reconstruct the assayed variant sequence.


enzyme_display_name: beta-lactamase

organism: Aeromonas hydrophila

substrate_name: H2O; Imipenem

sequence_variant_note: Resolved canonical sequence from UniProtKB:P26918 canonical sequence reconstructed with R121H from selected source mutation note and applied mutation signature R121H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant R121H

enzyme: beta-lactamase

substrate: H2O; Imipenem


sequence_source: UniProtKB:P26918 canonical sequence only; variant sequence not validated

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

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N116H/R121H/N220G


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

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N116H/N220G

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


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N220G


organism: Escherichia coli

substrate_name: H2O; Cephaloridine

sequence_source: UniProtKB:P78144 REST lookup 2026-06-22

substrate: H2O; Cephaloridine


substrate_name: H2O; Cephalosporin C

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant TEMpUC19 R164N

substrate: H2O; Cephalosporin C


substrate_name: Cephalosporin C; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant TEMpUC19 D179N

substrate: Cephalosporin C; H2O


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant TEMpUC19 R164S


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant TEMpUC19 D179G


substrate_name: Penicillin G; H2O

sequence_source: UniProtKB:Q47066 REST lookup 2026-06-22

substrate: Penicillin G; H2O


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y105D


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y105R


substrate_name: H2O; Penicillin G

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y105G

substrate: H2O; Penicillin G


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y105W


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y105N


sequence_source: UniProtKB:Q8KSA6 REST lookup 2026-06-22


organism: Bacteroides fragilis

sequence_variant_note: Resolved canonical sequence from UniProt P25910 canonical sequence plus worker-validated D103N reconstruction on 2026-06-22. and applied mutation signature D103N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D103N CcrA3


sequence_variant_note: Resolved canonical sequence from UniProt P25910 canonical sequence plus worker-validated H99N reconstruction on 2026-06-22. and applied mutation signature H99N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H99N CcrA3


sequence_variant_note: Resolved canonical sequence from UniProt P25910 canonical sequence plus worker-validated C181S reconstruction on 2026-06-22. and applied mutation signature C181S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant C181S CcrA3


sequence_variant_note: Resolved canonical sequence from UniProt P25910 canonical sequence plus worker-validated K184R reconstruction on 2026-06-22. and applied mutation signature K184R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K184R CcrA3


substrate_name: H2O; Nitrocefin

sequence_source: UniProt P25910 canonical sequence fetched by direct REST accession lookup on 2026-06-22.

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

proof_lines: pH and temperature not specified in the publication

substrate: H2O; Nitrocefin


sequence_variant_note: Resolved canonical sequence from UniProt P25910 canonical sequence plus worker-validated C104R reconstruction on 2026-06-22. and applied mutation signature C104R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant C104R CcrA3


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant delta 46-51 CcrA3


sequence_variant_note: Resolved canonical sequence from UniProt P25910 canonical sequence plus worker-validated C104S reconstruction on 2026-06-22. and applied mutation signature C104S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant C104S CcrA1


sequence_variant_note: Resolved canonical sequence from UniProt P25910 canonical sequence plus worker-validated N193D reconstruction on 2026-06-22. and applied mutation signature N193D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N193D CcrA3


organism: Burkholderia pseudomallei

sequence_variant_note: Resolved canonical sequence from UniProt Q6ZZZ2 canonical sequence plus worker-validated D170N reconstruction on 2026-06-22. and applied mutation signature D170N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D170N


substrate_name: Nitrocefin; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K232N

substrate: Nitrocefin; H2O


sequence_source: UniProt Q6ZZZ2 canonical sequence fetched by direct REST accession lookup on 2026-06-22.


organism: Citrobacter diversus

sequence_source: UniProt P22390 canonical sequence fetched by direct REST accession lookup on 2026-06-22.


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


organism: Bacillus cereus

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P04190 canonical FASTA after direct residue-position check and applied mutation signature D120N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120N; fusion protein to glutathione-S-transferase


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P04190 canonical FASTA after direct residue-position check and applied mutation signature D120S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120S; fusion protein to glutathione-S-transferase


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K73R


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K73R, E166D


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant E166D


substrate_name: H2O; 6-Aminopenicillanate

sequence_source: UniProtKB P00809 canonical FASTA (https://rest.uniprot.org/uniprotkb/P00809.fasta)

substrate: H2O; 6-Aminopenicillanate


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant E166Cmc


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


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant E166C


substrate_name: Ampicillin; H2O

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

sequence_source: UniProtKB P14488 canonical FASTA (https://rest.uniprot.org/uniprotkb/P14488.fasta)

substrate: Ampicillin; H2O


organism: Bacillus licheniformis

substrate_name: H2O; Penicillin V

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K234E

substrate: H2O; Penicillin V


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K234A


substrate_name: Penicillin V; H2O

sequence_source: UniProtKB P00808 canonical FASTA (https://rest.uniprot.org/uniprotkb/P00808.fasta)

proof_lines:
Raw SKiD Env: Temp=22°C, pH=7
Raw SKiD Env: Temp=-----, pH=-----

substrate: Penicillin V; H2O


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P25910 canonical FASTA after direct residue-position check and applied mutation signature C155V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant C155V CcrA1


sequence_source: UniProtKB:P26918 direct REST lookup 2026-06-22

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

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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04190 and applied mutation signature H118S to reconstruct the assayed variant sequence.

column_label: Table 3 (kinetic parameters with respect to benzylpenicillin and nitrocefin, 10 mM Hepes/0.2 M NaCl, pH 7.5, 30 C), enzyme row 'H118S', benzylpenicillin column group; column 'Km (uM)' = 2300; column 'kcat (s^-1)' = 36; column 'kcat/Km (M^-1 s^-1)' = 12200.

normalized_value_unit_evidence: Km: printed Table 3 cell 2300 uM; 2300 / 1000 = 2.3 mM; the paper value is 2.3 mM and the exported value is 0.22 mM. kcat: printed Table 3 cell 36 s^-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 36.0 s^(-1) and the exported value is 36.0 s^(-1). kcat/Km: printed Table 3 cell 12200 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 12200 / 1000 = 12.2 s^-1 mM^-1; the paper value is 12.2 s^(-1)*mM^(-1); the catalog identity carries no catalytic-efficiency value, so this cell is transcribed as evidence only.

raw_value_unit_evidence: Table 3, enzyme row 'H118S', benzylpenicillin column group: Km = 2300 uM; kcat = 36 s^-1; printed kcat/Km = 12200 M^-1 s^-1.

table_label: Table 3: Kinetic parameters with respect to benzylpenicillin and nitrocefin for the enzyme forms of Bacillus cereus 569/H/9 metallo-beta-lactamase BcII in 10 mM Hepes/0.2 M NaCl at pH 7.5 and 30 C (Biochem. J. 2002, 363:687-696)


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant C221S


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N233Y


substrate_name: Imipenem; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant C221A

substrate: Imipenem; H2O


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H196S


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04190 and applied mutation signature H116S to reconstruct the assayed variant sequence.

column_label: Table 3 (kinetic parameters with respect to benzylpenicillin and nitrocefin, 10 mM Hepes/0.2 M NaCl, pH 7.5, 30 C), enzyme row 'H116S', benzylpenicillin column group; column 'Km (uM)' = 530; column 'kcat (s^-1)' = 47; column 'kcat/Km (M^-1 s^-1)' = 89000.

normalized_value_unit_evidence: Km: printed Table 3 cell 530 uM; 530 / 1000 = 0.53 mM; the paper value is 0.53 mM and the exported value is 0.18000000000000002 mM. kcat: printed Table 3 cell 47 s^-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 47.0 s^(-1) and the exported value is 47.0 s^(-1). kcat/Km: printed Table 3 cell 89000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 89000 / 1000 = 89.0 s^-1 mM^-1; the paper value is 89.0 s^(-1)*mM^(-1); the catalog identity carries no catalytic-efficiency value, so this cell is transcribed as evidence only.

raw_value_unit_evidence: Table 3, enzyme row 'H116S', benzylpenicillin column group: Km = 530 uM; kcat = 47 s^-1; printed kcat/Km = 89000 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04190 direct REST lookup on 2026-06-22 and applied mutation signature H263S with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H263S


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

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant BcII delta IMP


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant BcII delta IMP W64A


substrate_name: H2O; Cefotaxime

sequence_source: UniProtKB:P04190 direct REST lookup on 2026-06-22

substrate: H2O; Cefotaxime


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120E; fusion protein to glutathione-S-transferase


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120Q; fusion protein to glutathione-S-transferase


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


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

sequence_source: UniProtKB:P13661 direct accession lookup (2026-06-22)

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

source_databases_merged: sabio_rk brenda skid


substrate_name: CENTA; H2O

sequence_source: UniProtKB:Q9S169 direct accession lookup (2026-06-22)

substrate: CENTA; H2O


sequence_source: UniProtKB:P00811 direct accession lookup (2026-06-22)

proof_lines:
pH 6.5, 22°C
Raw SKiD Env: Temp=-----, pH=-----


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N132D


substrate_name: 6-beta-Iodopenicillanic acid; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant AmpC T316A

substrate: 6-beta-Iodopenicillanic acid; H2O


substrate_name: Aztreonam; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant TEM-1 S235A

substrate: Aztreonam; H2O


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant AmpC T316V


substrate_name: Cefuroxime; H2O

sequence_source: Direct UniProt FASTA accession check: tr|Q6SJ61|Q6SJ61_ECOLX Beta-lactamase OS=Escherichia coli GN=TEM-1

substrate: Cefuroxime; H2O


substrate_name: H2O; Ampicillin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant A237T

substrate: H2O; Ampicillin


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant A237T:E240C


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant W165S:A273T:E240C


substrate_name: H2O; Cephaloridine

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant A273T

substrate: H2O; Cephaloridine


sequence_source: Direct UniProt FASTA accession check: sp|P62593|BLAT_ECOLX Beta-lactamase TEM OS=Escherichia coli GN=bla

proof_lines:
pH 7.5, 25°C
Raw SKiD Env: Temp=25°C, pH=7.5


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant E240C


substrate_name: Substituted beta-amino acid

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant W165S:A237T:E240C

substrate: Substituted beta-amino acid


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant W165S


organism: Fluoribacter gormanii

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y156A


substrate_name: Penicillin G; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N225A

substrate: Penicillin G; H2O


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


substrate_name: H2O; Penicillin G

sequence_source: Direct UniProt FASTA accession check: tr|Q9K578|Q9K578_9GAMM FEZ-1 protein OS=Fluoribacter gormanii GN=blaFEZ-1

substrate: H2O; Penicillin G


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant H121A


organism: Citrobacter freundii

substrate_name: H2O; Cephalothin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D217E

substrate: H2O; Cephalothin


substrate_name: Cephalothin; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D217K

substrate: Cephalothin; H2O


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D217T


organism: Enterobacter cloacae

substrate_name: H2O; Cephalosporin C

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N346I

substrate: H2O; Cephalosporin C


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N346A


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant L293C


sequence_source: UniProtKB:P05364 REST JSON fetched 2026-06-22

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

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

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


substrate_name: H2O; Cephalosporin

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

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant P99-210-1A

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant P99-210-2A

substrate: H2O; Cephalosporin


substrate_name: H2O; Dexamethasone-Cephem-Methotrexate

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y150S

substrate: H2O; Dexamethasone-Cephem-Methotrexate


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K315H


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y221G


substrate_name: Dexamethasone-Cephem-Methotrexate; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant S318T

substrate: Dexamethasone-Cephem-Methotrexate; H2O


organism: Klebsiella pneumoniae

substrate_name: H2O; Ampicillin; H2O; Ampicillin; Substituted beta-amino acid

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-1 R244E


substrate_name: Nitrocefin; H2O; Nitrocefin; H2O; Substituted beta-amino acid

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D104K


substrate_name: Cephalothin; H2O; Cephalothin; H2O; Substituted beta-amino acid

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D104K,G238S


substrate_name: H2O; Nitrocefin; H2O; Nitrocefin; Substituted beta-amino acid

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant G238S


substrate_name: ceftaxidime; cefotaxime; benzylpenicillin; piperacillin

source_license: CC BY 4.0; CC BY-NC-ND 4.0

sequence_source: UniProtKB direct accession lookup Q09HD0

assay_conditions_summary: pH 7; 303.15 K; buffer 100 mM sodium phosphate

proof_lines: at 30°C in 100 mM sodium phosphate buffer, pH 7.0

source_databases_merged: brenda skid


substrate_name: Ampicillin; H2O; Ampicillin; H2O; Substituted beta-amino acid

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-1 R244S


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-1 R244Q

substrate: H2O; Ampicillin; H2O; Ampicillin; Substituted beta-amino acid


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-1 R244L


substrate_name: aztreonam; cefuroxime; ticarcillin; piperacillin

sequence_source: UniProtKB direct accession lookup Q4TVR4


substrate_name: cefalothin; cefotaxime; cefoxitin; penicillin G

sequence_source: UniProtKB direct accession lookup A1EGT8


substrate_name: temocillin; panipenem; Imipenem; Oxacillin

sequence_source: UniProtKB direct accession lookup Q6XEC0

proof_lines:
pH 7.0, 30°C
Raw SKiD Env: Temp=30°C, pH=7


substrate_name: ampicillin; cephalotin; cefuroxime; aztreonam

sequence_source: UniProtKB direct accession lookup Q8KQ59


substrate_name: nitrocefin; cephalothin; piperacillin; ampicillin

sequence_source: UniProtKB direct accession lookup Q9F918

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


substrate_name: piperacillin; cephalothin; nitrocefin; ampicillin

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


substrate_name: cefoperazone; nitrocefin; cephalothin; amoxicillin

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


substrate_name: H2O; Imipenem

sequence_variant_note: Resolved canonical sequence from UniProtKB E9NWK5 canonical sequence with L209F substitution reconstructed during review and applied mutation signature L209F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant L209F

substrate: H2O; Imipenem


substrate_name: Nitrocefin; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB C7C422 canonical sequence with Q123A substitution reconstructed during review and applied mutation signature Q123A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Q123A

substrate: Nitrocefin; H2O


sequence_source: UniProtKB C7C422 direct accession lookup on 2026-06-22

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

proof_lines:
pH 7.2, 25°C, recombinant enzyme
Raw SKiD Env: Temp=25°C, pH=7.2


substrate_name: H2O; Nitrocefin

sequence_source: UniProtKB P0AD64 direct accession lookup on 2026-06-22

substrate: H2O; Nitrocefin


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-1(R974) S238G/E240


substrate_name: H2O; Penicillin G

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant M69V


substrate_name: Penicillin G; H2O

sequence_source: UniProtKB P0A3M1 direct accession lookup on 2026-06-22


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


organism: Klebsiella pneumoniae subsp. ozaenae

sequence_source: UniProtKB P0A9Z9 direct accession lookup on 2026-06-22


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-2(pBP60-1) G238S/E240


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-2(pBP60-1) S238/E240K

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-2(pBP60-1) G238/E240K


organism: Kluyvera ascorbata


organism: Moraxella catarrhalis

substrate_name: H2O; Amoxicillin

sequence_source: UniProtKB Q49095 direct accession lookup on 2026-06-22

substrate: H2O; Amoxicillin


substrate_name: Amoxicillin; H2O

sequence_source: UniProtKB:Q59514; direct accession lookup 2026-06-22

substrate: Amoxicillin; H2O


organism: Morganella morganii

substrate_name: H2O; Ampicillin

sequence_source: UniProtKB:Q705J0; direct accession lookup 2026-06-22

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant M19

substrate: H2O; Ampicillin


sequence_source: UniProtKB:Q704Y9; direct accession lookup 2026-06-22

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant M37


substrate_name: H2O; Cefotaxime

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

substrate: H2O; Cefotaxime


substrate_name: Cefotaxime; H2O

substrate: Cefotaxime; H2O


sequence_source: UniProtKB:Q704Z0; direct accession lookup 2026-06-22

substrate: Penicillin G; H2O


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB:P9WKD3; direct accession lookup 2026-06-22


sequence_source: UniProtKB:A5U493; direct accession lookup 2026-06-22

substrate: H2O; Penicillin G


organism: Nocardia asteroides

sequence_source: UniProtKB:Q9EZQ7; direct accession lookup 2026-06-22


organism: Nocardia farcinica

sequence_source: UniProtKB:Q5YXD6; direct accession lookup 2026-06-22

unit: Mswedgeone


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant S221A


organism: Homo sapiens

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant evMBL8


substrate_name: Imipenem; H2O

substrate: Imipenem; H2O


organism: Klebsiella oxytoca


substrate_name: Cephalothin; H2O

substrate: Cephalothin; H2O


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K161A


substrate_name: H2O; Cephalothin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K161E

substrate: H2O; Cephalothin


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K161R


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N167A


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N167D


organism: Stenotrophomonas maltophilia

sequence_source: UniProtKB P52700 direct lookup; reviewed Swiss-Prot sequence version 1

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


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


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


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


substrate_name: H2O; Biapenem

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

substrate: H2O; Biapenem


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


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


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


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


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


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


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


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


substrate_name: Ampicillin; H2O

sequence_source: UniProtKB FASTA for O51899, O51899_STEMA beta-lactamase, Stenotrophomonas maltophilia, EC 3.5.2.6.

substrate: Ampicillin; H2O


organism: Treponema pallidum


organism: Pseudomonas aeruginosa

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


organism: Pseudomonas fluorescens

substrate_name: carbenicillin

source_db: brenda, skid

sequence_source: UniProtKB P85302 canonical sequence direct lookup on 2026-06-22

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

substrate: carbenicillin

source: brenda, skid


organism: Pseudomonas putida

source_db: sabio_rk, brenda

sequence_source: UniProtKB Q8GCU7 canonical sequence direct lookup on 2026-06-22

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

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

source: sabio_rk, brenda


organism: Serratia fonticola

substrate_name: moxalactam

sequence_source: UniProtKB Q9RMI1 canonical sequence direct lookup on 2026-06-22

proof_lines:
pH 7.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7

substrate: moxalactam


sequence_source: UniProtKB P80545 canonical sequence direct lookup on 2026-06-22


organism: Serratia marcescens

substrate_name: Cephaloridine; H2O

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

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

substrate: Cephaloridine; H2O


sequence_source: UniProtKB Q7DHD4 canonical sequence direct lookup on 2026-06-22


sequence_source: UniProtKB P52682 canonical sequence direct lookup on 2026-06-22


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


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


organism: Ochrobactrum anthropi

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant DAP-475G487-N275R


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant DAP-475G487


organism: Providencia stuartii

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant K104E


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant S164R


substrate_name: Nitrocefin; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant P51L

substrate: Nitrocefin; H2O


substrate_name: H2O; Nitrocefin

sequence_source: UniProtKB direct REST stream for accession O68473

substrate: H2O; Nitrocefin


substrate_name: H2O; Carbenicillin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant R234K

substrate: H2O; Carbenicillin


substrate_name: Penicillin G; H2O

sequence_source: UniProtKB direct REST stream for accession P16897


substrate_name: H2O; Imipenem

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant IMP-1 W64A

substrate: H2O; Imipenem


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant IMP-1 delta 61-66


organism: Aeromonas sobria


source_db: sabio_rk, brenda, skid

proof_lines:
30°C, pH 7.0
Raw SKiD Env: Temp=30°C, pH=7

source: sabio_rk, brenda, skid


substrate_name: H2O; Penicillin G


substrate_name: ceftazidime

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

substrate: ceftazidime


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P37321 and applied mutation signature T104E with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

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

column_label: Table 2 (Kinetic parameters for hydrolysis of beta-lactams by PER-1 and mutant enzymes), enzyme row T104E, Cephaloridine column group: column Km = 2.5; column kcat = 0.14; column kcat/Km = 56. The printed footnote of the table gives the units of those three columns as uM, s-1 and s-1 mM-1 respectively. The value printed on the line below each of those cells is the printed S.E.M. of that fitted parameter and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.14 in a column headed kcat, whose printed unit is s-1; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.14 s^(-1). Km: printed Table 2 cell 2.5 in a column headed Km, whose printed unit is uM; 1 uM is 0.001 mM, so 2.5 / 1000 = 0.0025 mM. kcat/Km: printed Table 2 cell 56 in a column headed kcat/Km, whose printed unit is s-1 mM-1; that is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the value is 56.0 s^(-1)*mM^(-1). The catalog carries kcat 0.44 s^(-1) and Km 0.0025 mM, and no catalytic-efficiency value, so the printed kcat/Km cell is transcribed here as evidence only.

raw_value_unit_evidence: Table 2, enzyme row T104E, Cephaloridine column group: Km = 2.5 uM; kcat = 0.14 s-1; printed kcat/Km = 56 s-1 mM-1.

table_label: Table 2: Kinetic parameters for hydrolysis of beta-lactams by PER-1 and mutant enzymes (Biochemical Journal 1998, 330(Pt 3):1443-1449). The table prints one line per enzyme and six substrate column groups, left to right: Penicillin G, Cephalothin, Cephaloridine, Cefotaxime, Ceftazidime and Aztreonam; each group prints three value columns headed Km, kcat and kcat/Km. The printed footnote reads that the units for Km, kcat, and kcat/Km are uM, s-1 and s-1 mM-1 respectively, that N.D. means not determinable, and that the values of S.E.M. are indicated below the kinetic values.


sequence_source: UniProtKB:P37321 canonical sequence with row-specific N104G reconstruction

sequence_variant_note: Mutation signature N104G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

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


sequence_source: UniProtKB:P37321 canonical sequence with row-specific Q104G reconstruction

sequence_variant_note: Mutation signature Q104G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P37321 and applied mutation signature S238G with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for hydrolysis of beta-lactams by PER-1 and mutant enzymes), enzyme row S238G, Penicillin G column group: column Km = 7.7; column kcat = 3.5; column kcat/Km = 454. The printed footnote of the table gives the units of those three columns as uM, s-1 and s-1 mM-1 respectively. The value printed on the line below each of those cells is the printed S.E.M. of that fitted parameter and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.5 in a column headed kcat, whose printed unit is s-1; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 3.5 s^(-1). Km: printed Table 2 cell 7.7 in a column headed Km, whose printed unit is uM; 1 uM is 0.001 mM, so 7.7 / 1000 = 0.0077 mM. kcat/Km: printed Table 2 cell 454 in a column headed kcat/Km, whose printed unit is s-1 mM-1; that is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the value is 454.0 s^(-1)*mM^(-1). The catalog carries kcat 76.8 s^(-1) and Km 0.007700000000000001 mM, and no catalytic-efficiency value, so the printed kcat/Km cell is transcribed here as evidence only.

raw_value_unit_evidence: Table 2, enzyme row S238G, Penicillin G column group: Km = 7.7 uM; kcat = 3.5 s-1; printed kcat/Km = 454 s-1 mM-1.


column_label: Table 2 (Kinetic parameters for hydrolysis of beta-lactams by PER-1 and mutant enzymes), enzyme row PER-1 wild type, Penicillin G column group: column Km = 31.3; column kcat = 7.2; column kcat/Km = 230. The printed footnote of the table gives the units of those three columns as uM, s-1 and s-1 mM-1 respectively. The value printed on the line below each of those cells is the printed S.E.M. of that fitted parameter and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 7.2 in a column headed kcat, whose printed unit is s-1; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 7.2 s^(-1). Km: printed Table 2 cell 31.3 in a column headed Km, whose printed unit is uM; 1 uM is 0.001 mM, so 31.3 / 1000 = 0.0313 mM. kcat/Km: printed Table 2 cell 230 in a column headed kcat/Km, whose printed unit is s-1 mM-1; that is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the value is 230.0 s^(-1)*mM^(-1). The catalog carries kcat 70.0 s^(-1) and Km 0.0313 mM, and no catalytic-efficiency value, so the printed kcat/Km cell is transcribed here as evidence only.

raw_value_unit_evidence: Table 2, enzyme row PER-1 wild type, Penicillin G column group: Km = 31.3 uM; kcat = 7.2 s-1; printed kcat/Km = 230 s-1 mM-1.


substrate_name: H2O; Cephaloridine

sequence_source: UniProtKB:P37321 canonical sequence with row-specific E166A reconstruction

sequence_variant_note: Mutation signature E166A matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

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

substrate: H2O; Cephaloridine


sequence_source: UniProtKB:P37321 canonical sequence with row-specific A164S reconstruction

sequence_variant_note: Mutation signature A164S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

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


organism: Enterobacter cloacae

proof_lines: pH and temperature not specified in the publication


organism: Escherichia coli

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

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

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


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

proof_lines: 30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1

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

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


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


organism: Haemophilus ducreyi


organism: Klebsiella pneumoniae

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


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

proof_lines: pH 7.0, temperature not specified in the publication


organism: Mycobacterium tuberculosis

proof_lines:
at 30°C
in 100 mM MES (pH 6.4)


substrate_name: H2O; Ampicillin

sequence_source: UniProtKB REST accession P52682 canonical sequence; variant not reconstructed

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

substrate: H2O; Ampicillin


sequence_source: UniProtKB REST accession P52699 canonical sequence

proof_lines:
pH 7.5, 25°C
at 30°C
Raw SKiD Env: Temp=25°C, pH=7.5


organism: Shewanella livingstonensis

substrate_name: Amoxicillin; H2O

sequence_source: UniProtKB REST accession Q53BU1 canonical sequence

substrate: Amoxicillin; H2O


organism: Staphylococcus aureus

sequence_source: UniProtKB REST accession P00807 canonical sequence


organism: Stenotrophomonas maltophilia

sequence_source: UniProtKB REST accession P52700 canonical sequence; variant not reconstructed

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


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


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


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


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


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


organism: Proteus vulgaris


organism: Pseudomonas aeruginosa

substrate_name: Cefdinir; H2O

proof_lines: pH and temperature not specified in the publication, OXA-10 beta-lactamase

substrate: Cefdinir; H2O


substrate_name: H2O; Cefdinir

proof_lines:
30°C, pH 8.0
30°C, pH 8.0, uncompetitive
30°C, pH 8.0, competitive

substrate: H2O; Cefdinir


enzyme_display_name: putrescine N-methyltransferase

organism: Calystegia sepium

substrate_name: Putrescine

source_db: oed

sequence_source: UniProtKB:Q2KTH3 Q2KTH3_CALSE REST accession lookup on 2026-06-22 (UniProtKB unreviewed TrEMBL)

smiles: NCCCCN

enzyme: putrescine N-methyltransferase

substrate: Putrescine

source: oed


organism: Datura stramonium

sequence_source: UniProtKB:Q70EW6 PMT_DATST REST accession lookup on 2026-06-22 (UniProtKB reviewed Swiss-Prot)


organism: Solanum lycopersicum

sequence_source: UniProtKB:Q2KTH4 Q2KTH4_SOLLC REST accession lookup on 2026-06-22 (UniProtKB unreviewed TrEMBL)


enzyme_display_name: glycine N-benzoyltransferase

organism: Bos taurus

substrate_name: benzoyl-CoA

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

enzyme: glycine N-benzoyltransferase

substrate: benzoyl-CoA


substrate_name: glycine

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

substrate: glycine


organism: Homo sapiens

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA


proof_lines:
mutant enzyme N156S, at pH 8.0 and 37°C
mutant N156S, pH 8.0, 37°C


proof_lines: mutant enzyme S17T/N156S, at pH 8.0 and 37°C


proof_lines: mutant enzyme N156S/R199C, at pH 8.0 and 37°C


substrate_name: Glycine; Benzoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: Glycine; Benzoyl-CoA


organism: Mus musculus

substrate_name: Glycine methyl ester

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: pH 8.0, temperature not specified in the publication

substrate: Glycine methyl ester


enzyme_display_name: glutamate carboxypeptidase

organism: Acinetobacter sp. 263903-1

substrate_name: methotrexate

enzyme: glutamate carboxypeptidase

substrate: methotrexate


organism: Pseudomonas sp.

substrate_name: Folate; H2O

sequence_source: UniProtKB:P06621 direct FASTA lookup

substrate: Folate; H2O


organism: Pseudomonas sp. RS-16

sequence_source: UniProtKB:P06621 direct FASTA lookup for canonical context only


enzyme_display_name: Carboxypeptidase G2

sequence_source: UniProtKB P06621 canonical sequence

enzyme: Carboxypeptidase G2


substrate_name: folate; methotrexate

source_db: brenda;skid

proof_lines:
at pH 7.5 and 37°C
Raw SKiD Env: Temp=37°C, pH=7.3

substrate: folate; methotrexate

source: brenda;skid


organism: Stutzerimonas stutzeri

substrate_name: pteroylglutamic acid

substrate: pteroylglutamic acid


proof_lines:
reaction with Gly
reaction with Ala
reaction with L-Asn or L-Gln


proof_lines: purified recombinant S156 haplotype, apparent value, ordered bi-bi (sequential) mechanism, at pH 8.0, temperature not specified in the publication

proof_lines: purified recombinant S156 haplotype, apparent value, random bi-bi (sequential) mechanism, at pH 8.0, temperature not specified in the publication

proof_lines: purified recombinant S156 haplotype, apparent value, ping-pong bi-bi (non-sequential) mechanism, at pH 8.0, temperature not specified in the publication


organism: Ovis aries


organism: Cohnella sp. A01

substrate_name: folate

substrate: folate


organism: Leishmania major

substrate_name: Methotrexate; H2O

substrate: Methotrexate; H2O


proof_lines: pH and temperature not specified in the publication


organism: Pseudomonas sp. RS16

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


organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)

substrate_name: O-acetyl-L-homoserine

proof_lines: kcat is 28.0 sec(-1) with O-acetyl-L-homoserine as substrate for the O-acetyl-L-homoserine sulfhydrylase activity. kcat is 37.3 sec(-1) with Na(2)S as substrate. kcat is 7.0 sec(-1) with O-acetyl-L-homoserine as substrate for the cystathion

substrate: O-acetyl-L-homoserine


organism: [Brevibacterium] flavum


organism: Corynebacterium acetophilum

proof_lines:
O-alkylhomoserine synthesis
O-acetylhomoserine sulfhydrylation


organism: Geobacillus stearothermophilus


organism: Neurospora crassa


substrate_name: O-acetyl-L-serine

substrate: O-acetyl-L-serine


organism: Saccharomyces cerevisiae

substrate_name: Unknown

substrate: Unknown


proof_lines: O-acetyl-L-serine sulfhydrylase activity, wild-type and mutant enzymes


proof_lines:
L-serine-O-sulfate as acceptor
NaHS as donor
NaHS or Na2Se as donor


organism: Schizosaccharomyces pombe


enzyme_display_name: DNA-directed RNA polymerase

organism: Escherichia phage T7

substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from direct_uniprot_p00573_variant_reconstruction and applied mutation signature R423A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.9; 310.15 K; cofactor ATP

enzyme: DNA-directed RNA polymerase

substrate: ATP


sequence_variant_note: Resolved canonical sequence from direct_uniprot_p00573_variant_reconstruction and applied mutation signature R425A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct_uniprot_p00573_variant_reconstruction and applied mutation signature W422A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct_uniprot_p00573_variant_reconstruction and applied mutation signature R425K to reconstruct the assayed variant sequence.


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

proof_lines: pH 8.0, 37°C, dGTP as elongation substrate during dinucleotide synthesis, activation with Mn2+


substrate_name: dGTP

sequence_variant_note: Resolved canonical sequence from direct_uniprot_p00573_variant_reconstruction and applied mutation signature Y639F/S641A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 37°C, initiating nucleotide in dGrA synthesis, mutant enzyme Y639F/S641A

proof_lines: pH 8.0, 37°C, initiating nucleotide in rGrA synthesis, mutant enzyme Y639F/S641A

substrate: dGTP


substrate_name: rGTP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: pH 8.0, 37°C, initiating nucleotide in rGrA synthesis, wild-type enzyme

proof_lines: pH 8.0, 37°C, initiating nucleotide in dGrA synthesis, wild-type enzyme

substrate: rGTP


sequence_variant_note: Resolved canonical sequence from direct_uniprot_p00573_variant_reconstruction and applied mutation signature S641A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 37°C, initiating nucleotide in rGrA synthesis, mutant enzyme S641A

proof_lines: pH 8.0, 37°C, initiating nucleotide in dGrA synthesis, mutant enzyme S641A


sequence_variant_note: Resolved canonical sequence from direct_uniprot_p00573_variant_reconstruction and applied mutation signature Y639F to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 37°C, initiating nucleotide in dGrA synthesis, mutant enzyme Y639F

proof_lines: pH 8.0, 37°C, initiating nucleotide in rGrA synthesis, mutant enzyme Y639F

proof_lines: pH 8.0, 37°C, dGTP as elongation substrate during dinucleotide synthesis, activation by Mg2+, mutant enzyme Y639F


organism: Lathyrus oleraceus

substrate_name: GTP

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

substrate: GTP


organism: Fusarium oxysporum

substrate_name: CDP-choline

substrate: CDP-choline


organism: Homo sapiens

proof_lines: cosubstrate di-18:1-diacylglycerol, 20°C, pH 8.0

proof_lines: optimum reaction conditions, in presence of 100 microM 1-O-alkyl-2-acetyl-sn-glycerol


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: O-acetyl-L-homoserine (OAH) (at 30 degrees Celsius in potassium phosphate buffer)

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

assay_conditions_summary: buffer potassium phosphate


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)


organism: Calystegia sepium

substrate_name: Putrescine; S-Adenosyl-L-methionine

sequence_source: UniProtKB:Q2KTH3; EMBL AM177608 / protein CAJ46252.1; direct UniProt REST check on 2026-06-22

proof_lines:
isoenzyme PMT1
isoenzyme PMT2

substrate: Putrescine; S-Adenosyl-L-methionine


organism: Unknown

substrate_name: putrescine

substrate: putrescine


organism: Clostridioides difficile

substrate_name: methanethiol

sequence_source: UniProtKB Q187D4 direct REST lookup on 2026-06-22; active TrEMBL entry Q187D4_CLOD6, O-acetylhomoserine sulfhydrylase, Clostridioides difficile strain 630, EC 2.5.1.49.

smiles: CS

substrate: methanethiol


substrate_name: hydrogen sulfide

smiles: S

substrate: hydrogen sulfide


organism: Thermus thermophilus


proof_lines: at a fixed sulfide concentration of 1 mM


organism: Bacillus subtilis

substrate_name: RNA; ATP

sequence_source: UniProtKB O31945 direct REST lookup on 2026-06-22; active reviewed Swiss-Prot entry YONO_BACSU, DNA-directed RNA polymerase YonO, Bacillus subtilis strain 168, EC 2.7.7.6.

assay_conditions_summary: cofactor ATP

substrate: RNA; ATP


substrate_name: CDPcholine; 1,2-Diacyl-sn-glycerol

sequence_source: UniProtKB Q9Y6K0 direct REST lookup on 2026-06-22; active reviewed Swiss-Prot entry CEPT1_HUMAN, choline/ethanolaminephosphotransferase 1, Homo sapiens, includes EC 2.7.8.2.

substrate: CDPcholine; 1,2-Diacyl-sn-glycerol


substrate_name: 1,2-Diacyl-sn-glycerol; CDPcholine

substrate: 1,2-Diacyl-sn-glycerol; CDPcholine


sequence_source: UniProtKB P22140 direct REST lookup on 2026-06-22; active reviewed Swiss-Prot entry EPT1_YEAST, choline/ethanolaminephosphotransferase 1, Saccharomyces cerevisiae strain S288c, includes EC 2.7.8.2.


sequence_source: UniProtKB P17898 direct REST lookup on 2026-06-22; active reviewed Swiss-Prot entry CPT1_YEAST, cholinephosphotransferase 1, Saccharomyces cerevisiae strain S288c, EC 2.7.8.2.


organism: Nicotiana tabacum

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Solanum dulcamara


organism: Escherichia coli

substrate_name: ATP; RNA

substrate: ATP; RNA


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


organism: Phytophthora infestans


organism: Rattus norvegicus


organism: Ricinus communis


organism: Secale cereale


enzyme_display_name: legumain

organism: Canavalia ensiformis

assay_conditions_summary: pH 5

enzyme: legumain


organism: Bacillus subtilis (strain 168)

substrate_name: ATP (at 10 degrees Celsius)

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

substrate: ATP (at 10 degrees Celsius)


organism: Homo sapiens


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Xenopus laevis


substrate_name: DNP-Pro-Glu-Ala-Asn-NH2 (at pH 5.0 and 35 degrees Celsius)


sequence_source: UniProtKB Q99538 FASTA, checked 2026-06-22


organism: Saccharum sp.

substrate_name: Unknown

sequence_source: UniProtKB H2EUL5 FASTA, checked 2026-06-22

proof_lines: pH and temperature not specified in the publication


organism: Hordeum vulgare

proof_lines: mutant Q86P of HvCPI-4, inhibitor concentrations between 25 and 500 nM used, incubation with 10 microgram of a soluble endosperm protein extract, at 25°C and pH 6 for 10 min

proof_lines: mutant Q86P of HvCPI-4, inhibitor concentrations between 25 and 500 nM used, incubation with 5 microgram of a soluble root protein extract, at 25°C and pH 6 for 10 min


proof_lines: inhibitor concentrations between 25 and 500 nM used, incubation with 10 microgram of a soluble endosperm protein extract, at 25°C and pH 6 for 10 min

proof_lines: inhibitor concentrations between 25 and 500 nM used, incubation with 5 microgram of a soluble root protein extract, at 25°C and pH 6 for 10 min


organism: Schistosoma mansoni


organism: Sus scrofa


organism: Calystegia sepium

substrate_name: S-Adenosyl-L-methionine; Putrescine

substrate: S-Adenosyl-L-methionine; Putrescine


organism: Datura innoxia


organism: Datura inoxia


organism: Datura stramonium

proof_lines: PMT-SPDS chimeric enzyme consisting of 181 N-terminal amino acids of putrescine N-methyltransferase and 165 C-terminal amino acids of spermidine synthase, in 20 mM HEPES, pH 8.0, 2 mM dithiothreitol, 1 mM ascorbic acid, at 37°C

proof_lines: SPDS-PMT chimeric enzyme consisting of 144 N-terminal amino acids of spermidine synthase and 162 C-terminal amino acids of putrescine N-methyltransferase, in 20 mM HEPES, pH 8.0, 2 mM dithiothreitol, 1 mM ascorbic acid, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q70EW6 (https://rest.uniprot.org/uniprotkb/Q70EW6.json) and applied mutation signature I136V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: putrescine N-methyltransferase(Enzyme) mutant I136V


proof_lines: wild type enzyme, in 20 mM HEPES, pH 8.0, 2 mM dithiothreitol, 1 mM ascorbic acid, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q70EW6 (https://rest.uniprot.org/uniprotkb/Q70EW6.json) and applied mutation signature H108L to reconstruct the assayed variant sequence.


organism: Hyoscyamus niger


organism: Physalis divaricata


organism: Solanum dulcamara


organism: Solanum lycopersicum


organism: Solanum tuberosum


organism: Bos taurus


organism: Dictyocaulus viviparus


enzyme_display_name: guanidinoacetate N-methyltransferase

organism: Rattus norvegicus

substrate_name: S-Adenosyl-L-methionine

sequence_source: UniProtKB:P10868 direct REST lookup; reviewed GAMT_RAT canonical sequence

enzyme: guanidinoacetate N-methyltransferase

substrate: S-Adenosyl-L-methionine


substrate_name: Guanidinoacetate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 direct REST lookup; variant reconstructed with +1 construct-numbering offset from PMID/PDB residue labels and applied mutation signature T135A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: Guanidinoacetate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 direct REST lookup; variant reconstructed with +1 construct-numbering offset from PMID/PDB residue labels and applied mutation signature D134N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 direct REST lookup; variant reconstructed with +1 construct-numbering offset from PMID/PDB residue labels and applied mutation signature D129A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 direct REST lookup; variant reconstructed with +1 construct-numbering offset from PMID/PDB residue labels and applied mutation signature D129N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P10868 direct REST lookup; variant reconstructed with +1 construct-numbering offset from PMID/PDB residue labels


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 direct REST lookup; variant reconstructed with +1 construct-numbering offset from PMID/PDB residue labels and applied mutation signature D134E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 canonical sequence with row-specific mutation reconstruction and applied mutation signature Y136F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 canonical sequence with row-specific mutation reconstruction and applied mutation signature D129N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 canonical sequence with row-specific mutation reconstruction and applied mutation signature T135A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 canonical sequence with row-specific mutation reconstruction and applied mutation signature Y133F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P10868 canonical sequence with row-specific mutation reconstruction


organism: Oryctolagus cuniculus

sequence_source: UniProtKB:P27115 direct lookup for canonical rabbit MGAT1 context; row-specific D144N catalytic-domain secretion-signal fusion sequence unresolved.

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

proof_lines: SABIO-RK modifier species: alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase(Enzyme) mutant D144N, catalytic domain fused to secretion signal


sequence_source: UniProtKB:P27115 direct REST/FASTA lookup on 2026-06-22.


enzyme_display_name: O-phosphoserine sulfhydrylase

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

substrate_name: O(3)-acetyl-L-serine (in the presence of 1 mM sodium sulfide at pH 6.7 and 60 degrees Celsius)

enzyme: O-phosphoserine sulfhydrylase


organism: Xenopus laevis

substrate_name: pyridylaminated Man3GlcNAc2

substrate: pyridylaminated Man3GlcNAc2


organism: Arabidopsis thaliana

proof_lines: the apparent KM is >3.0 mM for Man(3)-octyl.


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: O-phospho-L-serine (in the presence of sulfide as cosubstrate)

proof_lines: kcat is 12.1 min(-1) with O-phospho-L-serine and sulfide as substrates. kcat is 54.8 min(-1) with O-phospho-L-serine and thiosulfate as substrates.


organism: Acer pseudoplatanus


substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


organism: Cricetulus griseus


organism: Homo sapiens


proof_lines:
recombinant catalytic fragment
transferase A
transferase B


organism: Sus scrofa


organism: Aeropyrum pernix

substrate_name: O-acetyl-L-serine

substrate: O-acetyl-L-serine


organism: Mycobacterium tuberculosis

proof_lines: formation of the aminoacrylate intermediate


sequence_source: UniProt REST accession lookup for Q9XGM8, accessed 2026-06-22

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


sequence_source: UniProt REST accession lookup for P70680, accessed 2026-06-22


organism: Nicotiana tabacum

sequence_source: UniProt REST accession lookup for Q9ST97, accessed 2026-06-22

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


sequence_variant_note: Resolved canonical sequence from UniProt REST accession lookup for Q9YBL2, accessed 2026-06-22 and applied mutation signature F225A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 80°C, mutant F225A, with O-phospho-L-serine


substrate_name: hydrogen sulfide

sequence_source: UniProt REST accession lookup for Q9YBL2, accessed 2026-06-22

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

proof_lines: pH 7.5, 80°C, wild-type enzyme, with O-acetyl-L-serine

proof_lines: pH 7.5, 80°C, wild-type enzyme, with O-phospho-L-serine


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


substrate_name: O-phospho-L-serine

sequence_source: UniProt REST accession lookup for P9WP53, accessed 2026-06-22

substrate: O-phospho-L-serine


sequence_variant_note: Resolved canonical sequence from UniProt REST accession lookup for Q79FV4, accessed 2026-06-22 and applied mutation signature R243A to reconstruct the assayed variant sequence.

proof_lines: dephosphorylation, pH 7.0, 22°C, recombinant mutant R243A enzyme


sequence_source: UniProt REST accession lookup for Q79FV4, accessed 2026-06-22


proof_lines: dephosphorylation, pH 7.0, 22°C, recombinant wild-type enzyme

proof_lines: apparent second-order rate of the first half-reaction, pH 7.0, 21°C, recombinant wild-type enzyme


enzyme_display_name: cGMP-dependent protein kinase

organism: Caenorhabditis elegans

enzyme: cGMP-dependent protein kinase

substrate: Unknown


organism: Eimeria tenella

substrate_name: ATP (at 30 degrees Celsius and pH 7)

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

assay_conditions_summary: pH 7; cofactor ATP

substrate: ATP (at 30 degrees Celsius and pH 7)


organism: Toxoplasma gondii

substrate_name: ATP

substrate: ATP