proof_lines:
37°C, pH 7.4
cosubstrate glutathione, 37°C, pH 7.4


organism: Ommastrephes sloanei

substrate_name: 3'-Phosphoadenylyl sulfate; Chondroitin sulfate A

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

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

km_unit: mM

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


organism: Rhodococcus erythropolis

source_db: brenda

source_license: CC BY 4.0

sequence_variant_note: Resolved canonical sequence from UniProtKB:P54997 and applied mutation signature Y63F/Q65H to reconstruct the assayed variant sequence.

source: brenda


sequence_variant_note: Resolved canonical sequence from UniProtKB:P54997 and applied mutation signature Y63F to reconstruct the assayed variant sequence.

mutation_type: substitution


sequence_variant_note: Resolved canonical sequence from UniProtKB:P54997 and applied mutation signature Y63S to reconstruct the assayed variant sequence.


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


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


enzyme_display_name: S-inosyl-L-homocysteine hydrolase

organism: Methanocaldococcus jannaschii

substrate_name: Inosine

enzyme: S-inosyl-L-homocysteine hydrolase

substrate: Inosine


enzyme_display_name: C5a peptidase

organism: Streptococcus pyogenes

substrate_name: Peptide; H2O

enzyme: C5a peptidase

substrate: Peptide; H2O


substrate_name: C75-BODIPY-labeled recombinant human C5a peptide

sequence_variant_note: Resolved canonical sequence from direct_uniprot_rest:P15926 and applied mutation signature D783A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D783A, pH and temperature not specified in the publication


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

substrate: C75-BODIPY-labeled recombinant human C5a peptide


substrate_name: H2O; CXCL8

substrate: H2O; CXCL8


enzyme_display_name: complement subcomponent C1r

organism: Homo sapiens

substrate_name: N-Acetyl-Gly-Lys methyl ester

source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

data_origin: experimental

enzyme: complement subcomponent C1r

substrate: N-Acetyl-Gly-Lys methyl ester

status: unverified

source: oed


substrate_name: N-Acetyl-Gly-Lys methyl ester; H2O

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

proof_lines: pH 7.4, 37°C, substrate is a fragment consisting of complement control protein domains, CCP1 and CCP2, plus serine

substrate: N-Acetyl-Gly-Lys methyl ester; H2O


organism: Mus musculus

substrate_name: Fetuin glycopeptide I; H2O

substrate: Fetuin glycopeptide I; H2O


organism: Saccharomyces cerevisiae


enzyme_display_name: arylformamidase

organism: Bacillus anthracis

substrate_name: N-formyl-L-kynurenine

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

proof_lines:
pH 7.4, 25°C, recombinant enzyme
Raw SKiD Env: Temp=25°C, pH=7.4

source_databases_merged: brenda skid

enzyme: arylformamidase

substrate: N-formyl-L-kynurenine


organism: Burkholderia cenocepacia


organism: Cupriavidus metallidurans

substrate_name: L-Formylkynurenine

substrate: L-Formylkynurenine


substrate_name: H2O; L-Formylkynurenine

substrate: H2O; L-Formylkynurenine


organism: Drosophila melanogaster

proof_lines:
pH 7.4, 22°C, recombinant enzyme
Raw SKiD Env: Temp=22°C, pH=7.4


enzyme_display_name: caffeoyl-CoA O-methyltransferase

organism: Vanilla planifolia

substrate_name: tricetin

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

enzyme: caffeoyl-CoA O-methyltransferase

substrate: tricetin


organism: Vitis vinifera

substrate_name: cyanidin 3-O-glucoside

sequence_source: UniProtKB:Q43237 canonical sequence from direct REST accession check on 2026-06-29

assay_conditions_summary: pH 8.5; 303.15 K; cofactor CoA

proof_lines: GST-tagged recombinant enzyme, at pH 8.5 and 30°C

proof_lines: thrombin-cleaved enzyme, at pH 8.5 and 30°C

substrate: cyanidin 3-O-glucoside


enzyme_display_name: methionine S-methyltransferase

organism: Wollastonia biflora

substrate_name: L-Methionine; S-Adenosyl-L-methionine

ki_unit: mM

sequence_source: UniProtKB:Q9SWR3 canonical sequence from direct REST accession check on 2026-06-29

enzyme: methionine S-methyltransferase

substrate: L-Methionine; S-Adenosyl-L-methionine


organism: Medicago sativa

sequence_source: UniProtKB:P93324 canonical sequence from direct REST accession check on 2026-06-29


enzyme_display_name: indole-3-acetate O-methyltransferase

organism: Arabidopsis thaliana

sequence_source: UniProtKB:Q9FLN8 canonical sequence from direct REST accession check on 2026-06-29

enzyme: indole-3-acetate O-methyltransferase


organism: Oryza sativa Japonica Group

substrate_name: S-adenosyl-L-methionine

sequence_source: UniProtKB:Q0J998 canonical sequence from direct REST accession check on 2026-06-29

substrate: S-adenosyl-L-methionine


enzyme_display_name: MMP 1-O-methyltransferase

organism: Mycolicibacterium hassiacum

sequence_source: UniProtKB:K5B7F3 canonical sequence from direct REST accession check on 2026-06-29

enzyme: MMP 1-O-methyltransferase


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


organism: Panax ginseng

substrate_name: ginsenoside F2

sequence_source: UniProtKB:A0A0A6ZFY4 direct exact accession lookup, release 2026_02

proof_lines:
at pH 8.0 and 35°C
pH 7.5, 30°C

substrate: ginsenoside F2


sequence_source: UniProtKB:O43825 direct exact accession lookup, release 2026_02


sequence_source: UniProtKB:Q9Y5Z6 direct exact accession lookup, release 2026_02


organism: Streptomyces hygroscopicus subsp. limoneus

substrate_name: GDP-valienol

sequence_source: UniProtKB:Q15JG1 direct exact accession lookup, release 2026_02

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

substrate: GDP-valienol


enzyme_display_name: alkylcobalamin dealkylase

substrate_name: Methylcobalamin; Glutathione

sequence_source: UniProtKB:Q9Y4U1 direct exact accession lookup, release 2026_02

enzyme: alkylcobalamin dealkylase

substrate: Methylcobalamin; Glutathione


enzyme_display_name: 3-aminobutanoyl-CoA transaminase

organism: Candidatus Cloacimonas acidaminovorans

sequence_source: UniProtKB:B0VH76 direct exact accession lookup, release 2026_02

assay_conditions_summary: pH 8.1; 301.15 K; cofactor CoA

enzyme: 3-aminobutanoyl-CoA transaminase


substrate_name: pyruvate

substrate: pyruvate


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


smiles: O=C(O)CCC(=O)C(=O)O


organism: Bacillus subtilis

sequence_source: UniProtKB:O31665 direct exact accession lookup, release 2026_02

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


organism: Zea mays


enzyme_display_name: diaminobutyrate--pyruvate transaminase

organism: Pseudomonas aeruginosa

sequence_source: UniProtKB:Q9I168 direct exact accession lookup, release 2026_02

enzyme: diaminobutyrate--pyruvate transaminase


substrate_name: Pyruvate; L-2,4-Diaminobutanoate

substrate: Pyruvate; L-2,4-Diaminobutanoate


organism: Staphylococcus aureus

substrate_name: 2',3'-Cyclic GMP

sequence_source: UniProtKB reviewed accession Q2FZ08; direct REST accession check on 2026-06-29

substrate: 2',3'-Cyclic GMP


substrate_name: H2O; Bis-4-nitrophenyl phosphate

substrate: H2O; Bis-4-nitrophenyl phosphate


substrate_name: Bis-4-nitrophenyl phosphate

substrate: Bis-4-nitrophenyl phosphate


substrate_name: 2',3'-Cyclic AMP

substrate: 2',3'-Cyclic AMP


sequence_source: UniProtKB reviewed accession Q7A6D4; direct REST accession check on 2026-06-29


sequence_source: UniProtKB reviewed accession O31521; direct REST accession check on 2026-06-29


sequence_source: UniProtKB reviewed accession O34559; direct REST accession check on 2026-06-29


organism: Bifidobacterium longum

sequence_source: UniProtKB reviewed accession E8MGH8; direct REST accession check on 2026-06-29


organism: Kribbella flavida

sequence_source: UniProtKB reviewed accession D2PPM7; direct REST accession check on 2026-06-29

proof_lines:
pH 8.0, 35°C
Raw SKiD Env: Temp=35°C, pH=8


enzyme_display_name: exo beta-1,2-glucooligosaccharide sophorohydrolase (non-reducing end)

organism: Parabacteroides distasonis

sequence_source: UniProtKB reviewed accession A6LGF6; direct REST accession check on 2026-06-29


enzyme: exo beta-1,2-glucooligosaccharide sophorohydrolase (non-reducing end)


organism: Streptococcus pyogenes

substrate_name: Peptide

sequence_source: UniProtKB reviewed accession P15926; direct REST accession check on 2026-06-29

substrate: Peptide


organism: Homo sapiens

assay_conditions_summary: cofactor ATP


substrate_name: ATP

assay_conditions_summary: pH 7.4; cofactor ATP

proof_lines:
pH 7.4
ATP in form of CaATP2-

substrate: ATP


enzyme_display_name: glycerate 2-kinase

organism: Escherichia coli

verification_status: verified

assay_conditions_summary: pH 7.5; 295.15 K; buffer pH 7; cofactor ATP

column_label: Table 1: Kinetic Constants for Enzymes in the (D)-Glucarate/Galactarate Catabolic Pathway (Biochemistry 1998, volume 37, pages 14369-14375); printed column heads kcat (s^-1) | Km (uM) | kcat/Km (M^-1 s^-1). Table 1, row GK (ATP); column kcat (s^-1) = 2.5; column Km (uM) = 61; column kcat/Km (M^-1 s^-1) = 4.1 x 10^4. captured primary segment: GK (ATP) | kcat 2.5 ± 0.4 s^-1 | Km 61 ± 2 uM | kcat/Km 4.1 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.5 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 2.5 s^(-1); the exported value is 2.5 s^(-1). Km: printed Table 1 cell 61 uM; 1 uM is 1/1000 mM, so 61 / 1000 = 0.061 mM; the exported value is 0.061 mM. kcat/Km: printed Table 1 cell 4.1 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.1 x 10^4 / 1000 = 41.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 2.5 / 0.061 = 40.98360655737705 s^-1 mM^-1, the exported value, and the printed efficiency cell is that quotient written to the two significant figures the table uses.

raw_value_unit_evidence: Table 1, row GK (ATP): kcat = 2.5 s^-1; Km = 61 uM; printed kcat/Km = 4.1 x 10^4 M^-1 s^-1.

row_label: Table 1, row GK (ATP)

enzyme: glycerate 2-kinase

status: verified


substrate_name: ATP; D-Glycerate

column_label: Table 1: Kinetic Constants for Enzymes in the (D)-Glucarate/Galactarate Catabolic Pathway (Biochemistry 1998, volume 37, pages 14369-14375); printed column heads kcat (s^-1) | Km (uM) | kcat/Km (M^-1 s^-1). Table 1, row GK (glycerate); column kcat (s^-1) = 2.5; column Km (uM) = 51; column kcat/Km (M^-1 s^-1) = 5.0 x 10^4. captured primary segment: GK (glycerate) | kcat 2.5 ± 0.1 s^-1 | Km 51 ± 1 uM | kcat/Km 5.0 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.5 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 2.5 s^(-1); the exported value is 2.5 s^(-1). Km: printed Table 1 cell 51 uM; 1 uM is 1/1000 mM, so 51 / 1000 = 0.051 mM; the exported value is 0.051 mM. kcat/Km: printed Table 1 cell 5.0 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.0 x 10^4 / 1000 = 50.0 s^(-1)*mM^(-1); the live export row stores no kcat_over_km field for this identity, so the printed cell is carried in the typed kcat_over_km_provenance only.

raw_value_unit_evidence: Table 1, row GK (glycerate): kcat = 2.5 s^-1; Km = 51 uM; printed kcat/Km = 5.0 x 10^4 M^-1 s^-1.

row_label: Table 1, row GK (glycerate)

substrate: ATP; D-Glycerate


substrate_name: D-Glycerate

verification_status: corrected

assay_conditions_summary: pH 7.5; 295.15 K; buffer pH 7; cofactor NADH

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.5 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 2.5 s^(-1); the exported value is 2.5 s^(-1). Km: printed Table 1 cell 51 uM; 1 uM is 1/1000 mM, so 51 / 1000 = 0.051 mM; the exported value is 0.051 mM. kcat/Km: printed Table 1 cell 5.0 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.0 x 10^4 / 1000 = 50.0 s^(-1)*mM^(-1); the exported value is 49.01960784313726 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

table_label: Table 1: Kinetic Constants for Enzymes in the (D)-Glucarate/Galactarate Catabolic Pathway (Biochemistry 1998, volume 37, pages 14369-14375); printed column heads kcat (s^-1) | Km (uM) | kcat/Km (M^-1 s^-1)

substrate: D-Glycerate

status: corrected


organism: Escherichia coli K-12


substrate_name: (R)-glycerate

substrate: (R)-glycerate


organism: Picrophilus torridus


organism: Pyrococcus horikoshii

substrate_name: D-glycerate

substrate: D-glycerate


organism: Saccharolobus solfataricus

km_display: Not reported

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines: pH 6.5, 80°C, substrate-inhibition model


organism: Synechocystis sp.


organism: Thermoplasma acidophilum

assay_conditions_summary: pH 8; 328.15 K; cofactor ATP


organism: Thermoproteus tenax


organism: Thermotoga maritima


organism: Berberis koetineana

proof_lines:
isoenzyme NMT-III
isoenzyme NMT-II
isoenzyme NMT-I


organism: Medicago truncatula

substrate_name: isoliquiritigenin

substrate: isoliquiritigenin


enzyme_display_name: pinosylvin synthase

organism: Pinus densiflora

substrate_name: p-Coumaroyl-CoA

assay_conditions_summary: cofactor CoA

proof_lines:
isozyme PDSTS3
isozyme PDSTS2

enzyme: pinosylvin synthase

substrate: p-Coumaroyl-CoA


organism: Unknown

substrate_name: di-p-nitrophenyl phosphate

substrate: di-p-nitrophenyl phosphate


enzyme_display_name: cyanoalanine nitrilase

organism: Sorghum bicolor

proof_lines: isozyme complex NIT4A/B2, in 50 mM potassium phosphate (pH 8.0), 1 mM dithiothreitol, at 37°C

proof_lines: isozyme complex NIT4A/B1, in 50 mM potassium phosphate (pH 8.0), 1 mM dithiothreitol, at 37°C

enzyme: cyanoalanine nitrilase


enzyme_display_name: porphobilinogen synthase

substrate_name: 5-aminolevulinic acid

sequence_source: UniProtKB reviewed accession P13716 direct lookup

assay_conditions_summary: pH 9

proof_lines: wild type, pH 9, predominantly hexamer and/or dimer

enzyme: porphobilinogen synthase

substrate: 5-aminolevulinic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P13716 canonical sequence with F12L reconstructed from selected mutation_signature and applied mutation signature F12L to reconstruct the assayed variant sequence.

proof_lines:
F12L, pH 9
F12L, pH 7


proof_lines:
Raw SKiD Env: Temp=-----, pH=9
Raw SKiD Env: Temp=-----, pH=7


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB reviewed accession Q59643 direct lookup

proof_lines:
37°C, pH 8.5
Raw SKiD Env: Temp=-----, pH=-----


organism: Methanocaldococcus jannaschii

substrate_name: L-homocysteine

sequence_source: UniProtKB reviewed Swiss-Prot exact accession Q58783; REST lookup 2026-06-29.

substrate: L-homocysteine


substrate_name: Inosine

substrate: Inosine


substrate_name: S-Inosyl-L-homocysteine

substrate: S-Inosyl-L-homocysteine


enzyme_display_name: retinoid isomerohydrolase

organism: Bos taurus

substrate_name: H2O; All-trans-Retinyl palmitate

sequence_source: UniProtKB reviewed Swiss-Prot exact accession Q28175; REST lookup 2026-06-29.

enzyme: retinoid isomerohydrolase

substrate: H2O; All-trans-Retinyl palmitate


organism: Danio rerio

substrate_name: an all-trans retinyl ester

proof_lines: pH and temperature not specified in the publication

substrate: an all-trans retinyl ester


organism: Acinetobacter baumannii

substrate_name: D-mannitol 1-phosphate

sequence_source: UniProtKB TrEMBL exact accession D0C7J2; REST lookup 2026-06-29.

substrate: D-mannitol 1-phosphate


enzyme_display_name: pseudouridine 5'-phosphatase

organism: Homo sapiens

substrate_name: Pseudouridine 5'-phosphate; H2O

sequence_source: UniProtKB reviewed Swiss-Prot exact accession Q08623; REST lookup 2026-06-29.

enzyme: pseudouridine 5'-phosphatase

substrate: Pseudouridine 5'-phosphate; H2O


organism: Escherichia coli

substrate_name: p-nitrophenyl phosphate

substrate: p-nitrophenyl phosphate


sequence_source: UniProtKB reviewed Swiss-Prot exact accession P67095; REST lookup 2026-06-29.

assay_conditions_summary: pH 8.5; buffer Tris-HCl

proof_lines: in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2

proof_lines: in Tris-HCl buffer (pH 8.5) in the presence of 5 mM MnCl2


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

proof_lines: pH 7.5, 37°C, mutant Y544A N-terminal domain of CpdB


proof_lines: pH 7.5, 37°C, mutant H117A N-terminal domain of CpdB


substrate_name: bis-4-nitrophenyl phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Swiss-Prot exact accession P08331 with direct Y544A reconstruction; REST lookup 2026-06-29. and applied mutation signature Y544A to reconstruct the assayed variant sequence.

substrate: bis-4-nitrophenyl phosphate


substrate_name: CDP-choline

proof_lines:
pH 7.5, 37°C, N-terminal domain of CpdB
pH 7.5, 37°C
pH 7.5, 37°C, mature enzyme CpdB

substrate: CDP-choline


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Swiss-Prot exact accession P08331 with direct H117A reconstruction; REST lookup 2026-06-29. and applied mutation signature H117A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed Swiss-Prot exact accession P08331; REST lookup 2026-06-29.

proof_lines: substrate bis-4-nitrophenyl phosphate, wild-type, pH 7.5, 37°C

proof_lines: substrate bis-4-nitrophenyl phosphate, isolated N-terminal domain,wild-type, pH 7.5, 37°C


sequence_source: UniProtKB reviewed Swiss-Prot exact accession P08331 only as canonical context; row-specific chimera/domain sequence not resolved.

proof_lines: chimera CpdB catalytic domain/UshA specificity domain, pH not specified in the publication, temperature not specified in the publication

proof_lines: chimera UshA catalytic domain/CpdB specificity domain, pH not specified in the publication, temperature not specified in the publication

proof_lines: isolated N-terminal domain, pH 7.5, 37°C


enzyme_display_name: tabersonine 16-hydroxylase

organism: Catharanthus roseus

substrate_name: tabersonine

source_db: uniprot

enzyme: tabersonine 16-hydroxylase

substrate: tabersonine

source: uniprot


enzyme_display_name: (-)-pinoresinol reductase

organism: Arabidopsis thaliana

substrate_name: (-)-pinoresinol

enzyme: (-)-pinoresinol reductase

substrate: (-)-pinoresinol


substrate_name: (+)-pinoresinol

substrate: (+)-pinoresinol


organism: Petunia hybrida

substrate_name: Unknown

substrate: Unknown


organism: Medicago sativa

substrate_name: isoliquiritigenin

substrate: isoliquiritigenin


substrate_name: indole-3-acetic acid (IAA)

substrate: indole-3-acetic acid (IAA)


organism: Pinus strobus

substrate_name: cinnamoyl-CoA

substrate: cinnamoyl-CoA


organism: Pinus sylvestris


enzyme_display_name: glycine C-acetyltransferase

organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: L-glycine (with acetyl-CoA at pH 6 and at 70 degrees Celsius)

assay_conditions_summary: pH 6; cofactor CoA

enzyme: glycine C-acetyltransferase


enzyme_display_name: kojibiose phosphorylase

organism: Thermoanaerobacter brockii

substrate_name: kojibiose

enzyme: kojibiose phosphorylase

substrate: kojibiose


organism: Citrus maxima

substrate_name: prunin

substrate: prunin


substrate_name: UDP-alpha-D-galactose

substrate: UDP-alpha-D-galactose


organism: Mus musculus


organism: Escherichia coli (strain K12)

substrate_name: glycerate

substrate: glycerate


organism: Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)

substrate_name: glycerate (at 50 degrees Celsius and at pH 7.3)

assay_conditions_summary: pH 7.3; cofactor ATP


organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

substrate_name: glycerate (at 45 degrees Celsius and at pH 7.0)

assay_conditions_summary: pH 7; cofactor ATP


organism: Streptomyces coeruleorubidus

proof_lines: kcat is 21.9 min(-1) with (3R)-3-[(carboxymethyl)amino]butanoate as substrate.


enzyme_display_name: methylxanthine N(1)-demethylase

organism: Pseudomonas putida

substrate_name: theophylline (at pH 7.5 and 30 degrees Celsius)

proof_lines: kcat is 190 min(-1) for caffeine (at pH 7.5 and 30 degrees Celsius).

enzyme: methylxanthine N(1)-demethylase


enzyme_display_name: methylxanthine N(3)-demethylase

substrate_name: 3-methylxanthine (at pH 7.5 and 30 degrees Celsius)

proof_lines: kcat is 46 min(-1) for theobromine (at pH 7.5 and 30 degrees Celsius).

enzyme: methylxanthine N(3)-demethylase


substrate_name: tabersonine in a T16H/16OMT coupled system

assay_conditions_summary: cofactor NADPH

proof_lines: concentrations of tabersonine greater than 30 uM are inhibitory.


enzyme_display_name: ent-sandaracopimaradiene 3-hydroxylase

organism: Oryza sativa subsp. japonica

substrate_name: ent-cassadiene

proof_lines: kcat is 1.4 sec(-1) with syn-pimaradiene as substrate.

enzyme: ent-sandaracopimaradiene 3-hydroxylase

substrate: ent-cassadiene


enzyme_display_name: phenylacetonitrile alpha-monooxygenase

organism: Prunus mume

substrate_name: phenylacetaldoxime (in the presence of NADPH at pH 7.6 and 30 degrees Celsius)

assay_conditions_summary: pH 7.6; cofactor NADPH

proof_lines: kcat is 46.3 min(-1) with phenylacetaldoxime as substrate (in the presence of NADPH at pH 7.6 and 30 degrees Celsius) (PubMed:25015725). kcat is 24.2 min(-1) with phenylacetonitrile as substrate (in the presence of NADPH at pH 7.6 and 30 de

enzyme: phenylacetonitrile alpha-monooxygenase


enzyme_display_name: NAD(P)H oxidase (H2O-forming)

organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

substrate_name: NADH

proof_lines: kcat is 68 sec(-1) for NADH oxidase activity. kcat is 50 sec(-1) for NADPH oxidase activity.

enzyme: NAD(P)H oxidase (H2O-forming)

substrate: NADH


enzyme_display_name: kaempferol 4'-O-methyltransferase

organism: Solanum habrochaites

substrate_name: myricetin (in the presence of S-adenosylmethionine)

proof_lines: kcat is 7.40x10(-3) sec(-1) with myricetin as substrate (in the presence of S-adenosylmethionine) (PubMed:21343428). kcat is 5.76x10(-3) sec(-1) with kaempferide as substrate (in the presence of S-adenosylmethionine) (PubMed:21343428). kcat

enzyme: kaempferol 4'-O-methyltransferase


enzyme_display_name: MMP 1-O-methyltransferase

organism: Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)

enzyme: MMP 1-O-methyltransferase


enzyme_display_name: demethoxycurcumin synthase

organism: Curcuma longa

substrate_name: feruloyl-CoA

proof_lines: kcat is 0.19 min(-1) with feruloyl-CoA. kcat is 0.36 min(-1) with p-coumaroyl-CoA.

enzyme: demethoxycurcumin synthase

substrate: feruloyl-CoA


substrate_name: kojibiose (at pH 7.5, 30 degrees Celsius)

proof_lines: kcat is 1.0 sec(-1) for phosphorolysis of kojibiose, and kcat is 0.8 sec(-1) for the reverse reaction.


organism: Amycolatopsis orientalis

substrate_name: devancoaminyl-vancomycin

substrate: devancoaminyl-vancomycin


enzyme_display_name: inosine/xanthosine triphosphatase

organism: Escherichia coli

substrate_name: xanthosine 5'-triphosphate

sequence_source: UniProtKB P39411 direct REST lookup on 2026-06-29; UniProtKB reviewed entry P39411 / NCPP_ECOLI, Inosine/xanthosine triphosphatase, EC 3.6.1.73, Escherichia coli strain K12; PDB cross-reference 1U5W

enzyme: inosine/xanthosine triphosphatase

substrate: xanthosine 5'-triphosphate


substrate_name: guanosine 5'-triphosphate

substrate: guanosine 5'-triphosphate


substrate_name: 2'-deoxyinosine 5'-triphosphate

substrate: 2'-deoxyinosine 5'-triphosphate


substrate_name: inosine 5'-triphosphate

substrate: inosine 5'-triphosphate


enzyme_display_name: D-ornithine/D-lysine decarboxylase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: D-Lysine

sequence_source: UniProtKB Q8ZNC4 direct REST lookup on 2026-06-29; UniProtKB reviewed entry Q8ZNC4 / DOKDC_SALTY, D-ornithine/D-lysine decarboxylase, EC 4.1.1.116, Salmonella typhimurium strain LT2

proof_lines: pH 7.0, 25°C, recombinant His-tagged enzyme

enzyme: D-ornithine/D-lysine decarboxylase

substrate: D-Lysine


substrate_name: D-ornithine

substrate: D-ornithine


enzyme_display_name: carboxynorspermidine decarboxylase

organism: Vibrio vulnificus

substrate_name: Carboxynorspermidine

sequence_source: UniProtKB Q8D8D2 direct REST lookup on 2026-06-29; UniProtKB reviewed entry Q8D8D2 / NSPC_VIBVU, Carboxynorspermidine/carboxyspermidine decarboxylase, EC 4.1.1.96, Vibrio vulnificus strain CMCP6

enzyme: carboxynorspermidine decarboxylase

substrate: Carboxynorspermidine


substrate_name: carboxyspermidine

smiles: NCCCCNCCC(N)C(=O)O

substrate: carboxyspermidine


substrate_name: carboxynorspermidine

smiles: NCCCNCCC(N)C(=O)O

substrate: carboxynorspermidine


enzyme_display_name: 2-dehydro-3-deoxy-D-gluconate aldolase

organism: Picrophilus oshimae

sequence_source: UniProtKB Q6KZI8 checked directly; not accepted as the row sequence because organism does not match selected row

proof_lines: pH 6.2, 60°C, enzyme purified from Picrophilus torridus

enzyme: 2-dehydro-3-deoxy-D-gluconate aldolase


organism: Picrophilus torridus

sequence_source: UniProtKB Q6KZI8 direct REST lookup on 2026-06-29; UniProtKB reviewed entry Q6KZI8 / KDGA_PICTO, 2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolase, EC 4.1.2.14 and EC 4.1.2.51, Picrophilus torridus strain KAW 2/3; PDB cross-reference 4UXD


enzyme_display_name: porphobilinogen synthase

sequence_source: UniProtKB P0ACB2 direct REST lookup on 2026-06-29; UniProtKB reviewed entry P0ACB2 / HEM2_ECOLI, Delta-aminolevulinic acid dehydratase, EC 4.2.1.24, Escherichia coli strain K12

enzyme: porphobilinogen synthase


enzyme_display_name: arylformamidase

organism: Mus musculus

substrate_name: H2O; L-Formylkynurenine; H2O; L-Formylkynurenine; Formate; L-Kynurenine

sequence_source: UniProtKB:Q8K4H1 direct lookup

enzyme: arylformamidase


substrate_name: N-formyl-L-kynurenine

proof_lines:
pH 7.4, native wild-type enzyme
pH 7.4, recombinant wild-type enzyme

substrate: N-formyl-L-kynurenine


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB:Q9I234 direct lookup


organism: Saccharomyces cerevisiae

source_db: brenda; skid

sequence_source: UniProtKB:Q04066 direct lookup

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7.4

source: brenda; skid


organism: Streptomyces coelicolor

sequence_source: UniProtKB:Q9X8R1 direct lookup

proof_lines: pH 7.4, temperature not specified in the publication, recombinant His6-tagged enzyme


enzyme_display_name: N-substituted formamide deformylase

organism: Arthrobacter pascens

substrate_name: N-benzylformamide; N-butylformamide

sequence_source: UniProtKB:Q68AP4 direct lookup

enzyme: N-substituted formamide deformylase

substrate: N-benzylformamide; N-butylformamide


substrate_name: N-Benzylformamide; H2O; N-Benzylformamide; H2O; Formate; Benzylamine; N-Butylformamide; H2O; N-Butylformamide; Butylamine


enzyme_display_name: cyanoalanine nitrilase

organism: Lupinus angustifolius

substrate_name: H2O; 3-Cyano-L-alanine; H2O; 3-Cyano-L-alanine; L-Aspartate; NH3

sequence_source: UniProtKB:Q3LRV4 direct lookup

enzyme: cyanoalanine nitrilase


source_db: sabio_rk; brenda

sequence_source: UniProtKB:Q5QGZ8 direct lookup

substrate: H2O; 3-Cyano-L-alanine; H2O; 3-Cyano-L-alanine; L-Aspartate; NH3

source: sabio_rk; brenda


enzyme_display_name: ADP-sugar diphosphatase

organism: Arabidopsis thaliana

substrate_name: ADP-ribose; H2O; ADP-ribose; H2O; AMP; D-Ribose 5-phosphate; ADPglucose; H2O; ADPglucose; D-Glucose 1-phosphate

sequence_source: UniProtKB:Q9SZ63 direct lookup

assay_conditions_summary: cofactor ADP

enzyme: ADP-sugar diphosphatase


enzyme_display_name: UDP-2,3-diacylglucosamine diphosphatase

organism: Caulobacter vibrioides

sequence_source: UniProtKB:A0A0H3C8Q1 direct lookup

proof_lines: in 100 mM sodium acetate, 50 mM bis(2-hydroxyethyl)imino-tris(hydroxymethyl)hexane, and 50 mM Tris, 2 mM MgCl2, at 30°C, pH not specified in the publication

enzyme: UDP-2,3-diacylglucosamine diphosphatase


sequence_source: UniProtKB:P43341 direct lookup

proof_lines:
pH 8.0, 30°C
Raw SKiD Env: Temp=30°C, pH=8


organism: Haemophilus influenzae

sequence_source: UniProtKB:P44046 direct lookup


organism: Klebsiella pneumoniae

substrate_name: Unknown

sequence_source: UniProtKB:A6T5R0 direct lookup

substrate: Unknown


organism: Klebsiella pneumoniae subsp. pneumoniae

assay_conditions_summary: pH 8


organism: Escherichia coli (strain K12)

substrate_name: mannitol phosphorylation

substrate: mannitol phosphorylation


organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

substrate_name: adenosylcobinamide phosphate

substrate: adenosylcobinamide phosphate


enzyme_display_name: cardiolipin synthase (CMP-forming)

substrate_name: phosphatidylglycerol (dioleoyl species)

enzyme: cardiolipin synthase (CMP-forming)

substrate: phosphatidylglycerol (dioleoyl species)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: phosphatidylglycerol

substrate: phosphatidylglycerol


enzyme_display_name: thiosulfate--thiol sulfurtransferase

organism: Homo sapiens

substrate_name: glutathione

enzyme: thiosulfate--thiol sulfurtransferase

substrate: glutathione


organism: Nototodarus sloanii

substrate_name: PAPS

substrate: PAPS


enzyme_display_name: retinoid isomerohydrolase

organism: Bos taurus

substrate_name: all-trans-retinyl palmitate

enzyme: retinoid isomerohydrolase

substrate: all-trans-retinyl palmitate


organism: Danio rerio

substrate_name: 11-cis retinol

substrate: 11-cis retinol


organism: Gallus gallus


enzyme_display_name: pseudouridine 5'-phosphatase

enzyme: pseudouridine 5'-phosphatase


organism: Bacillus subtilis (strain 168)

substrate_name: unsaturated rhamnogalacturonan disaccharide (at pH 6 and 30 degrees Celsius)

assay_conditions_summary: pH 6


enzyme_display_name: adenylylsulfatase

substrate_name: P(1)-P(3)-bis(5'-adenosyl) triphosphate

enzyme: adenylylsulfatase

substrate: P(1)-P(3)-bis(5'-adenosyl) triphosphate


organism: Vibrio alginolyticus

substrate_name: carboxynorspermidine (at 37 degrees Celsius and pH 8.25)


organism: Vibrio vulnificus (strain CMCP6)

substrate_name: carboxynorspermidine


organism: Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)

substrate_name: KDG (at 60 degrees Celsius and pH 6.2)

substrate: KDG (at 60 degrees Celsius and pH 6.2)


substrate_name: 5-aminolevulinic acid

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

substrate: 5-aminolevulinic acid


substrate_name: 5-aminolevulinate at pH 7

assay_conditions_summary: pH 7

substrate: 5-aminolevulinate at pH 7


organism: Gardenia jasminoides

substrate_name: beta-D-glucosyl crocetin

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

proof_lines: kcat is 0.036 sec(-1) for beta-D-glucosyl crocetin. kcat is 0.071 sec(-1) for bis(beta-D-glucosyl) crocetin.

substrate: beta-D-glucosyl crocetin


organism: Panax ginseng

substrate_name: protopanaxadiol (at pH 7 and 35 degrees Celsius)

proof_lines: kcat is 55.6 usec(-1) with protopanaxadiol as substrate (at pH 7 and 35 degrees Celsius). kcat is 134.7 usec(-1) with compound K as substrate (at pH 7 and 35 degrees Celsius).


substrate_name: ginsenoside Rh2 (at pH 8 and 40 degrees Celsius)

proof_lines: kcat is 8.6 sec(-1) with ginsenoside Rh2 as substrate (at pH 7 and 35 degrees Celsius). kcat is 0.41 sec(-1) with ginsenoside F2 as substrate (at pH 7 and 35 degrees Celsius) (PubMed:25320211). kcat is 1111 sec(-1) with ginsenoside Rh2 as s


organism: Streptomyces hygroscopicus subsp. limoneus

substrate_name: GDP-valienol

proof_lines: kcat is 7 min(-1) with GDP-valienol as substrate. kcat is 7 min(-1) with validamine 7-phosphate as substrate.

substrate: GDP-valienol


enzyme_display_name: alkylcobalamin dealkylase

proof_lines: kcat is 11.7 h(-1) for the dealkylation of methylcobalamin (MeCbl) (PubMed:19801555). kcat is 0.006 h(-1) for the dealkylation of 5'-deoxyadenosylcobalamin (AdoCbl) (PubMed:19801555).

enzyme: alkylcobalamin dealkylase


enzyme_display_name: 3-aminobutanoyl-CoA transaminase

organism: Cloacimonas acidaminovorans (strain Evry)

proof_lines: kcat is 1.80 sec(-1) for 3-aminobutyryl-CoA. kcat is 1.80 sec(-1) for alpha-ketoglutarate. kcat is 0.4 sec(-1) for pyruvate.

enzyme: 3-aminobutanoyl-CoA transaminase


substrate_name: KMTB

substrate: KMTB


substrate_name: PtdIns (in the absence of phosphatidylserine)

assay_conditions_summary: cofactor ATP

proof_lines: In the absence of the carrier phosphatidylserine, enzymatic kinetics toward PtdIns4P are non-linear.


enzyme_display_name: glycerate 2-kinase

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

substrate_name: ATP

proof_lines: kcat is 14.4 sec(-1) for phosphorylation of D-glycerate.

enzyme: glycerate 2-kinase

substrate: ATP


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

substrate_name: adenosylcobinamide

proof_lines: kcat is 15.1 min(-1) for adenosylcobinamide kinase activity. kcat is 5.6 min(-1) for guanylyltransferase activity.

substrate: adenosylcobinamide


organism: Rhodococcus qingshengii

substrate_name: HBPS

substrate: HBPS


enzyme_display_name: S-inosyl-L-homocysteine hydrolase

organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

substrate_name: inosine (at pH 7.0 and 70 degrees Celsius)

proof_lines: kcat is 0.83 sec(-1) for the synthesis of SIH from inosine and L-homocysteine. kcat is 0.42 sec(-1) for the hydrolysis of SIH (at pH 7.0 and 70 degrees Celsius).

enzyme: S-inosyl-L-homocysteine hydrolase


substrate_name: unsaturated rhamnogalacturonan disaccharide (at pH 4 and 30 degrees Celsius)


organism: Mus musculus

substrate_name: fetuin glycopeptide I

substrate: fetuin glycopeptide I


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: asialofetuin

substrate: asialofetuin


substrate_name: N-formyl-L-kynurenine

substrate: N-formyl-L-kynurenine


organism: Arthrobacter pascens

substrate_name: N-benzylformamide

substrate: N-benzylformamide


organism: Arabidopsis thaliana

substrate_name: Ala(CN) (for the nitrilase activity)

substrate: Ala(CN) (for the nitrilase activity)


organism: Lupinus angustifolius

substrate_name: Ala(CN)

substrate: Ala(CN)


substrate_name: ADP-D-ribose

substrate: ADP-D-ribose


organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15)


organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)


substrate_name: adenosine 5'-phosphoramidate (at pH 6.8)


enzyme_display_name: isopenicillin-N synthase

organism: Hapsidospora chrysogena

substrate_name: Unknown

enzyme: isopenicillin-N synthase

substrate: Unknown


enzyme_display_name: (-)-pinoresinol reductase

organism: Thuja plicata

substrate_name: (-)-pinoresinol

proof_lines: wild type isoform PLR2, at pH 8.0 and 30°C

enzyme: (-)-pinoresinol reductase

substrate: (-)-pinoresinol


proof_lines: mutant G267V of isoform PLR2, at pH 8.0 and 30°C


enzyme_display_name: NAD(P)H oxidase (H2O-forming)

organism: Giardia duodenalis

substrate_name: NADH

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADPH

enzyme: NAD(P)H oxidase (H2O-forming)

substrate: NADH


enzyme_display_name: caffeoyl-CoA O-methyltransferase

organism: Ammi majus

substrate_name: quercetin

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

proof_lines: pH 7.5, 37°C, in presence of 0.1 mM Co2+

proof_lines: pH 7.5, 37°C, in presence of 0.15 mM Mg2+

enzyme: caffeoyl-CoA O-methyltransferase

substrate: quercetin


organism: Azadirachta indica

substrate_name: caffeic acid

substrate: caffeic acid


organism: Camellia sinensis

assay_conditions_summary: pH 6.8; 308.15 K; cofactor CoA


organism: Citrus reticulata

substrate_name: tricetin

substrate: tricetin


organism: Citrus sinensis

substrate_name: caffeoyl-CoA

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

substrate: caffeoyl-CoA


organism: Medicago sativa

assay_conditions_summary: cofactor CoA


organism: Nicotiana tabacum

sequence_variant_note: Resolved canonical sequence from UniProtKB O24144 FASTA; PMID 11459845 and NCBI protein 30580325 link to O24144 and applied mutation signature Q61S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB O24144 FASTA; PMID 11459845 and NCBI protein 30580325 link to O24144


organism: Oryza sativa

assay_conditions_summary: pH 7.5; 310.15 K; buffer Tris-HCl; cofactor CoA

proof_lines: OMT-17, in 10 mM Tris-HCl buffer (pH 7.5), at 37°C


organism: Triticum aestivum

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA


enzyme_display_name: kaempferol 4'-O-methyltransferase

organism: Dianthus caryophyllus

substrate_name: S-Adenosyl-L-methionine; Kaempferol

enzyme: kaempferol 4'-O-methyltransferase

substrate: S-Adenosyl-L-methionine; Kaempferol


enzyme_display_name: indole-3-acetate O-methyltransferase

organism: Illicium anisatum

enzyme: indole-3-acetate O-methyltransferase


organism: Populus trichocarpa

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


enzyme_display_name: MMP 1-O-methyltransferase

organism: Mycolicibacterium smegmatis

enzyme: MMP 1-O-methyltransferase


enzyme_display_name: pinosylvin synthase

organism: Pinus sylvestris

substrate_name: phenylpropionyl-CoA

enzyme: pinosylvin synthase

substrate: phenylpropionyl-CoA


enzyme_display_name: gallate dioxygenase

organism: Pseudomonas putida

substrate_name: gallate

enzyme: gallate dioxygenase

substrate: gallate


organism: Sphingobium sp. SYK-6

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


enzyme_display_name: tabersonine 16-hydroxylase

organism: Catharanthus roseus

substrate_name: NADPH

enzyme: tabersonine 16-hydroxylase

substrate: NADPH


enzyme_display_name: taxadiene 5alpha-hydroxylase

organism: Taxus cuspidata

enzyme: taxadiene 5alpha-hydroxylase


organism: Taxus media

assay_conditions_summary: cofactor NADP+


organism: Homo sapiens

substrate_name: taurochenodeoxycholate

substrate: taurochenodeoxycholate


enzyme_display_name: ent-sandaracopimaradiene 3-hydroxylase

substrate_name: ent-cassadiene

proof_lines: pH and temperature not specified in the publication

enzyme: ent-sandaracopimaradiene 3-hydroxylase

substrate: ent-cassadiene


organism: Actinomyces sp.


organism: Amycolatopsis lactamdurans


organism: Flavobacterium sp.


enzyme_display_name: demethoxycurcumin synthase

organism: Curcuma longa

proof_lines: pH 8.0, 37°C, with cinnamoyl-diketide-N-acetylcysteaminyl-CoA

enzyme: demethoxycurcumin synthase


enzyme_display_name: glycine C-acetyltransferase

organism: Bos taurus

substrate_name: acetyl-CoA

enzyme: glycine C-acetyltransferase

substrate: acetyl-CoA


organism: Escherichia coli

substrate_name: propionyl-CoA

substrate: propionyl-CoA


organism: Thermus thermophilus


enzyme_display_name: trehalose 6-phosphate phosphorylase

organism: Lactococcus lactis ssp. lactis

substrate_name: glucose 6-phosphate

enzyme: trehalose 6-phosphate phosphorylase

substrate: glucose 6-phosphate


enzyme_display_name: kojibiose phosphorylase

substrate_name: D-glucose

enzyme: kojibiose phosphorylase

substrate: D-glucose


organism: Lactobacillus acidophilus

proof_lines: pH 6.2, 45°C, recombinant loop 3 mutant 2 of maltose phosphorylase

proof_lines: pH 6.2, 45°C, recombinant loop 3 mutant 3 of maltose phosphorylase

proof_lines: pH 6.2, 45°C, recombinant loop 3 mutant 1 of maltose phosphorylase


organism: Thermoanaerobacter brockii

substrate_name: kojibiose

substrate: kojibiose


substrate_name: phosphate

substrate: phosphate


substrate_name: beta-D-glucose 1-phosphate

substrate: beta-D-glucose 1-phosphate


organism: Citrus maxima

substrate_name: UDP-L-rhamnose

proof_lines: pH 7.5, 37°C, cosubstrate hesperetin 7-O-glucoside

proof_lines: pH 7.5, 37°C, cosubstrate naringenin 7-O-glucoside

substrate: UDP-L-rhamnose


organism: Dipsacus asperoides

substrate_name: UDP-beta-L-rhamnose

substrate: UDP-beta-L-rhamnose


organism: Panax major

substrate_name: protopanaxadiol

substrate: protopanaxadiol


organism: Salinispora tropica

substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


organism: Gallus gallus


organism: Mus musculus


organism: Oryctolagus cuniculus


organism: Rattus norvegicus


enzyme_display_name: alkylcobalamin dealkylase

organism: Homo sapiens

substrate_name: nitrocobalamin

enzyme: alkylcobalamin dealkylase

substrate: nitrocobalamin


organism: Solanum lycopersicum


enzyme_display_name: diaminobutyrate--pyruvate transaminase

organism: Halomonas elongata

substrate_name: L-glutamate

enzyme: diaminobutyrate--pyruvate transaminase

substrate: L-glutamate


organism: Halorhodospira halochloris


organism: Pseudomonas aeruginosa

substrate_name: pyruvate

proof_lines: pH 7.5, 25°C, with 2-oxoglutarate, recombinant enzyme

proof_lines: pH 7.5, 25°C, with pyruvate, recombinant enzyme

substrate: pyruvate


substrate_name: ATP

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: pH 7.5, 30°C, reaction with phosphatidylinositol, without phosphatidylserine

proof_lines: pH 7.5, 30°C, reaction with phosphatidylinositol, in presence of phosphatidylserine

proof_lines: pH 7.5, 30°C, in presence of phosphatidylserine

substrate: ATP


enzyme_display_name: glycerate 2-kinase

organism: Escherichia coli

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP

enzyme: glycerate 2-kinase


organism: Hyphomicrobium methylovorum

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines: cosubstrate D-glycerate, at pH 7.0, 30°C


organism: Picrophilus oshimae


organism: Pyrococcus horikoshii

substrate_name: (R)-glycerate

assay_conditions_summary: pH 7; 318.15 K; cofactor ATP

proof_lines: the reaction mixture contains 1 mM (R)-glycerate, 1 mM ATP, 10 mM MgCl2, 0.3 mM NADH, 1 mM phosphoenolpyruvate, 10 nM purified glycerate kinase, 3.5 units pyruvate kinase and 5 units lactate dehydrogenase in 50 mM potassium phosphate (pH 7.

substrate: (R)-glycerate


organism: Thermoplasma acidophilum

assay_conditions_summary: pH 8; 328.15 K; cofactor ATP

proof_lines: in 100 mM Tris-HCl (pH 8), 5 mM EGTA, 1 mM (R)-glycerate, 1 mM ATP, 10 mM MgCl2, at 55°C


substrate_name: D-mannitol[side 1]

assay_conditions_summary: pH 7; 310.15 K; buffer HEPES

proof_lines: in sodium phosphate buffer, at pH 7.0 and 37°C

substrate: D-mannitol[side 1]


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: 5'-deoxyadenosylcobinamide phosphate

substrate: 5'-deoxyadenosylcobinamide phosphate


enzyme_display_name: cardiolipin synthase (CMP-forming)

substrate_name: egg yolk phosphatidylglycerol

proof_lines: pH 8.5, 37°C, at optimal concentration of phospholipid activators

proof_lines: at high Co2+ concentration, pH pH 9.0, 37°C

proof_lines: at low Co2+ concentration, pH pH 9.0, 37°C

enzyme: cardiolipin synthase (CMP-forming)

substrate: egg yolk phosphatidylglycerol


enzyme_display_name: thiosulfate--thiol sulfurtransferase

organism: Acinetobacter calcoaceticus

substrate_name: cyanide

enzyme: thiosulfate--thiol sulfurtransferase

substrate: cyanide


organism: Saccharomyces cerevisiae

substrate_name: glutathione

proof_lines: pH 8.1, 37°C, with benzenethiosulfonate as the other substrate

proof_lines: pH 8.1, 37°C, with thiosulfate as the other substrate

substrate: glutathione


organism: squid

substrate_name: 3'-phosphoadenylyl sulfate

substrate: 3'-phosphoadenylyl sulfate


organism: Paenibacillus sp.


organism: Rhodococcus erythropolis

proof_lines:
pH 7.0, 28°C
pH 7.4, 35°C
pH 7.0, 28°C, recombinant enzyme


enzyme_display_name: retinoid isomerohydrolase

organism: Bos taurus

substrate_name: all-trans-retinyl palmitate

proof_lines: pH and temperature not specified in the publication

enzyme: retinoid isomerohydrolase

substrate: all-trans-retinyl palmitate


organism: Gallus gallus

assay_conditions_summary: pH 8; 310.15 K; buffer 10 mM BTP

proof_lines: purified enzyme, in 10 mM BTP buffer, pH 8.0, 100 mM NaCl, at 37°C


organism: Homo sapiens

substrate_name: an all-trans-retinyl ester

substrate: an all-trans-retinyl ester


organism: Sus scrofa


organism: Aspergillus nidulans

substrate_name: mannitol 1-phosphate

proof_lines: at 2 mM mannitol 1-phosphate the maximal activity was underestimated, additional information

substrate: mannitol 1-phosphate


organism: Caloglossa continua

substrate_name: D-mannitol 1-phosphate

substrate: D-mannitol 1-phosphate


organism: Ectocarpus siliculosus


organism: Eimeria tenella


organism: Pyricularia oryzae


organism: Escherichia coli (strain K12)

substrate_name: fructose-1-P (with magnesium ions as cofactor and at pH 9)

assay_conditions_summary: pH 9

proof_lines: kcat is 3.7 sec(-1) with fructose-1-P as substrate. kcat is 2.7 sec(-1) with ribose-5-P as substrate. kcat is 13 sec(-1) with glucose-6-P as substrate. kcat is 3.1 sec(-1) with fructose-6-P as substrate. kcat is 7.5 sec(-1) with beta-D-gluc


substrate_name: 2-deoxyglucose-6-P (with manganese ions as cofactor and at pH 9)

proof_lines: kcat is 33 sec(-1) with 2-deoxyglucose-6-P as substrate. kcat is 11 sec(-1) with mannose-6-P as substrate. kcat is 9.4 sec(-1) with 2-deoxyribose-5-P as substrate. kcat is 2.8 sec(-1) with ribose-5-P as substrate. kcat is 25 sec(-1) with gl


enzyme_display_name: pseudouridine 5'-phosphatase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: XMP

proof_lines: kcat is 1.9 sec(-1) with XMP as substrate.

enzyme: pseudouridine 5'-phosphatase

substrate: XMP


organism: Bacillus subtilis (strain 168)

proof_lines: kcat is 15.0 min(-1) with 2',3'-cAMP as substrate. kcat is 22.1 min(-1) with 2',3'-cGMP as substrate. kcat is 9.2 min(-1) with 3',5'-cAMP as substrate. kcat is 7.7 min(-1) with 3',5'-cGMP as substrate.


substrate_name: Unknown

proof_lines: The 2',3'-cyclic phosphodiesterase activity is higher than that of the 5'-nucleotidase with the four major nucleotides used as substrates.

substrate: Unknown


organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

substrate_name: PEP (at pH 6.5)

proof_lines: kcat is 0.18 sec(-1) with PEP as substrate. kcat is 0.38 sec(-1) with 2',3'-cAMP as substrate. kcat is 0.32 sec(-1) with 2',3'-cCMP as substrate. kcat is 0.42 sec(-1) with 2',3'-cGMP as substrate. kcat is 0.20 sec(-1) with pNPP as substrate

substrate: PEP (at pH 6.5)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 2.8 sec(-1) with 2',3'-cAMP as substrate. kcat is 0.55 sec(-1) with pNPP as substrate. kcat is 12.4 sec(-1) with bis(pNPP) as substrate.


organism: Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b)

proof_lines: kcat is 2.0 sec(-1) with beta-Ara2. kcat is 0.013 sec(-1) with Ara-Hyp. kcat is 6.3 sec(-1) with Ara(2)-Hyp.


organism: Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399)

substrate_name: cyclobis-(1-6)-alpha-nigerosyl (CNN)

proof_lines: kcat is 22.3 sec(-1) for cyclobis-(1-6)-alpha-nigerosyl (CNN) as substrate.

substrate: cyclobis-(1-6)-alpha-nigerosyl (CNN)


enzyme_display_name: exo beta-1,2-glucooligosaccharide sophorohydrolase (non-reducing end)

organism: Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152)

proof_lines: kcat is 54 sec(-1) with beta-1,2-glucotetrasaccharide as substrate. kcat is 29 sec(-1) with beta-1,2-glucopentasaccharide as substrate. kcat is 0.48 sec(-1) with beta-1,2-glucan (with an average DP of 77) as substrate.


enzyme_display_name: arylformamidase

organism: Bacillus anthracis

substrate_name: N-formyl-L-kynurenine

proof_lines: kcat is 50.56 sec(-1) for N-formyl-L-kynurenine as substrate.

enzyme: arylformamidase

substrate: N-formyl-L-kynurenine


organism: Streptococcus bovis

substrate_name: H2O; D-Mannitol 1-phosphate

substrate: H2O; D-Mannitol 1-phosphate


organism: Homo sapiens

substrate_name: pseudouridine 5'-phosphate

substrate: pseudouridine 5'-phosphate


organism: Bacillus sp. (in: firmicutes)

substrate_name: bis(p-nitrophenyl)phosphate

substrate: bis(p-nitrophenyl)phosphate


organism: Bacillus subtilis


organism: Escherichia coli


organism: Fusarium culmorum

substrate_name: cyclic 2',3'-GMP

substrate: cyclic 2',3'-GMP


organism: Haemophilus influenzae


organism: Mycobacterium tuberculosis

substrate_name: p-nitrophenyl phosphate

assay_conditions_summary: pH 8.5; buffer Tris-HCl

proof_lines: wild type enzyme, in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2

substrate: p-nitrophenyl phosphate


organism: Myxococcus xanthus

substrate_name: cyclic 2',3'-AMP

assay_conditions_summary: pH 8

substrate: cyclic 2',3'-AMP


organism: Proteus mirabilis


organism: Proteus vulgaris


organism: Shigella sonnei


organism: Vibrio alginolyticus

proof_lines:
with 200 mM NaCl
without NaCl


organism: Bacteroides thetaiotaomicron


organism: Bifidobacterium longum


enzyme_display_name: C5a peptidase

organism: Streptococcus pyogenes

substrate_name: SQLRANISHKDMQLGR

proof_lines:
pH 7.4, 25°C
pH 7.4, 25°C, Km above 2 mM

enzyme: C5a peptidase

substrate: SQLRANISHKDMQLGR


enzyme_display_name: complement subcomponent C1r

substrate_name: N-acetyl-Arg methyl ester

enzyme: complement subcomponent C1r

substrate: N-acetyl-Arg methyl ester


organism: Elizabethkingia meningoseptica

substrate_name: Fetuin glycopeptide

substrate: Fetuin glycopeptide


organism: Mus musculus


organism: Prunus amygdalus var. dulcis

substrate_name: bromelain undecapeptide

proof_lines: stem bromelain undecapeptide, glycopeptidase group C

substrate: bromelain undecapeptide


organism: Saccharomyces cerevisiae

substrate_name: asialo fetuin glycopeptide I

substrate: asialo fetuin glycopeptide I


organism: Sus scrofa

substrate_name: Beta-aspartylglycosylamine

substrate: Beta-aspartylglycosylamine


organism: Bos taurus


organism: Drosophila melanogaster

proof_lines:
formamidase I
formamidase II


organism: Gallus gallus


organism: Neurospora crassa


organism: Ogataea henricii

proof_lines:
formamidase II
formamidase I


organism: Oncorhynchus mykiss

substrate_name: N-formyl-DL-kynurenine

substrate: N-formyl-DL-kynurenine


organism: Rattus sp.


organism: Streptomyces parvulus


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: N-substituted formamide deformylase

organism: Arthrobacter pascens

substrate_name: N-benzylformamide

proof_lines:
25°C, pH 7.5, recombinant enzyme
pH 7.0, 25°C
pH 7.5, 25°C

enzyme: N-substituted formamide deformylase

substrate: N-benzylformamide


enzyme_display_name: cyanoalanine nitrilase

organism: Brassica rapa

proof_lines: in 50 mM sodium phosphate (pH 8.0) containing 0.2% (w/v) BSA with 5 mM substrate, at 35°C

enzyme: cyanoalanine nitrilase


organism: Pseudomonas sp.


organism: Zea mays


enzyme_display_name: ADP-sugar diphosphatase

organism: Escherichia coli

substrate_name: ADP-ribose

assay_conditions_summary: pH 7.5; cofactor ADP

enzyme: ADP-sugar diphosphatase

substrate: ADP-ribose


organism: Rattus norvegicus

substrate_name: ADP-Rib

assay_conditions_summary: cofactor ADP

substrate: ADP-Rib


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: ADP-glucose

substrate: ADP-glucose


enzyme_display_name: adenylylsulfatase

substrate_name: Adenosine 5'-phosphosulfate; H2O

assay_conditions_summary: cofactor ATP

enzyme: adenylylsulfatase

substrate: Adenosine 5'-phosphosulfate; H2O


organism: Comamonas terrigena

substrate_name: adenosine 5'-phosphosulfate

substrate: adenosine 5'-phosphosulfate


enzyme_display_name: carboxynorspermidine decarboxylase

organism: Campylobacter jejuni

substrate_name: carboxyspermidine

proof_lines: pH and temperature not specified in the publication

enzyme: carboxynorspermidine decarboxylase

substrate: carboxyspermidine


organism: Eshraghiella crossota


organism: Vibrio alginolyticus

substrate_name: carboxynorspermidine

substrate: carboxynorspermidine


organism: Vibrio vulnificus


enzyme_display_name: porphobilinogen synthase

organism: Bos taurus

enzyme: porphobilinogen synthase


organism: Cereibacter sphaeroides


organism: Coturnix japonica

proof_lines:
liver enzyme
shell gland enzyme


organism: Drosophila melanogaster


assay_conditions_summary: pH 6

proof_lines:
at pH 6 and pH 8.5
at pH 6.8


organism: Homo sapiens


organism: Ictalurus punctatus


organism: Lathyrus oleraceus

proof_lines:
at pH 7.5
at pH 9


organism: Mus musculus

proof_lines:
pH 7.5
pH 6.4 and 37°C


organism: Mycolicibacterium phlei


organism: Neurospora crassa


organism: Plasmodium falciparum


organism: Pseudomonas aeruginosa

assay_conditions_summary: pH 8.6; buffer Na-Hepes


organism: Pyrobaculum calidifontis

proof_lines: presence of zinc and 2-mercaptoethanol, pH 6.8, 70°C


organism: Rattus sp.

substrate_name: 5-aminolevulinic acid

proof_lines: expressed from expression vector pET28a+, His-tag removed

substrate: 5-aminolevulinic acid


organism: Rhodobacter capsulatus

proof_lines:
in absence of 2-mercaptoethanol
in presence of 2-mercaptoethanol


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:P05373 reviewed HEM2_YEAST; PMID 2204246 names yeast structural gene HEM2; PubChem CID 137 for substrate SMILES


organism: Tetradesmus obliquus


organism: Toxoplasma gondii


organism: Zea mays

proof_lines: in the presence of Hg2+, at pH 8.2 and 37°C

proof_lines: in the absence of Hg2+, at pH 8.2 and 37°C


organism: Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)

substrate_name: N-formyl-L-kynurenine

proof_lines: kcat is 43.94 sec(-1) for N-formyl-L-kynurenine as substrate.

substrate: N-formyl-L-kynurenine


organism: Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)

proof_lines: kcat is 0.77 sec(-1) for N-formyl-L-kynurenine as substrate.


organism: Drosophila melanogaster

proof_lines: kcat is 1584 min(-1) with N-formyl-L-kynurenine as substrate.


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

proof_lines: kcat is 114.21 sec(-1) for N-formyl-L-kynurenine as substrate.


enzyme_display_name: UDP-2,3-diacylglucosamine diphosphatase

organism: Escherichia coli (strain K12)

enzyme: UDP-2,3-diacylglucosamine diphosphatase


enzyme_display_name: inosine/xanthosine triphosphatase

substrate_name: ITP

proof_lines: kcat is 573.3 sec(-1) with ITP as substrate. kcat is 2625 sec(-1) with XTP as substrate. kcat is 119 sec(-1) with GDP as substrate. kcat is 616.5 sec(-1) with dITP as substrate. kcat is 22.3 sec(-1) with GTP as substrate.

enzyme: inosine/xanthosine triphosphatase

substrate: ITP


enzyme_display_name: D-ornithine/D-lysine decarboxylase

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

proof_lines: kcat is 1.8 sec(-1) with D-ornithine as substrate. kcat is 4.4 sec(-1) with D-lysine as substrate.

enzyme: D-ornithine/D-lysine decarboxylase


organism: Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828)

proof_lines: KM values are given with the protein sequence containing Glu instead of Lys at position 184, the effect of the variation on activity is unclear.


organism: Pisum sativum


organism: Lathyrus oleraceus

proof_lines:
pH 7.5, 30°C
isoform HMM2, 30°C
isoform HMM1, 30°C


organism: Glycyrrhiza echinata


organism: Medicago truncatula


organism: Methanosarcina barkeri

substrate_name: methyl-CoM

substrate: methyl-CoM


sequence_source: UniProtKB reviewed entry Q48924, exact accession lookup on 2026-06-29


substrate_name: methylmercaptopropionate

sequence_source: UniProtKB reviewed Q48924 direct accession follow-up

proof_lines:
pH 7.0, 37°C
recombinant enzyme, pH 7.0, 37°C

substrate: methylmercaptopropionate


enzyme_display_name: 2-deoxystreptamine glucosyltransferase

organism: Streptomyces kanamyceticus

substrate_name: UDP-D-glucose

proof_lines: using UDP-D-glucose as donor, in 100 mM Tris-HCl (pH 7.6), 10 mM MgCl2, 6 mM 2-mercaptoethanol, and 1 mM phenylmethylsulfonyl fluoride, at 30°C

proof_lines: using UDP-N-acetyl-alpha-D-glucosamine as donor, in 100 mM Tris-HCl (pH 7.6), 10 mM MgCl2, 6 mM 2-mercaptoethanol, and 1 mM phenylmethylsulfonyl fluoride, at 30°C

enzyme: 2-deoxystreptamine glucosyltransferase

substrate: UDP-D-glucose


organism: Rhodothermus marinus

substrate_name: CTP

substrate: CTP


substrate_name: 2-Deoxystreptamine; UDP-D-glucose

sequence_source: UniProtKB reviewed accession Q65CC1 via exact accession lookup on 2026-06-29

substrate: 2-Deoxystreptamine; UDP-D-glucose


organism: Archaeoglobus fulgidus

substrate_name: 1L-myo-inositol 1-phosphate

sequence_source: UniProtKB reviewed accession O29976 via exact accession lookup on 2026-06-29

proof_lines: 90°C, pH 7.0, cytoplasmic CTP:inositol-1-phosphate cytidylyltransferase domain of the bifunctional enzyme (EC 2.7.7.74/EC 2.7.8.34)

proof_lines: pH and temperature not specified in the publication

substrate: 1L-myo-inositol 1-phosphate


substrate_name: UDP-N-acetyl-alpha-D-glucosamine

substrate: UDP-N-acetyl-alpha-D-glucosamine


organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

substrate_name: CTP (at pH 7 and 90 degrees Celsius)

substrate: CTP (at pH 7 and 90 degrees Celsius)


enzyme_display_name: type I site-specific deoxyribonuclease

organism: Escherichia coli

substrate_name: ATP

assay_conditions_summary: 310.15 K; cofactor ATP

enzyme: type I site-specific deoxyribonuclease

substrate: ATP


organism: Micrococcus luteus

substrate_name: DNA; ATP; H2O

assay_conditions_summary: pH 9.4; 303.15 K; cofactor ATP

substrate: DNA; ATP; H2O


organism: Pseudomonas sp. (strain ADP)

substrate_name: hydroxyatrazine

assay_conditions_summary: pH 7; buffer 50 mM phosphate; cofactor ADP

substrate: hydroxyatrazine


organism: Pseudomonas sp.

substrate_name: Hydroxyatrazine

sequence_source: UniProtKB reviewed accession P95442/ATZB_PSESD FASTA, checked 2026-06-29; entry cites PMID 17660279 for EC 3.5.4.43 and AtzB function.

assay_conditions_summary: pH 7; 296.15 K; cofactor ADP

column_label: Table 2 (Kinetic values for substrate hydrolysis by AtzB) prints one kinetic-measure label column followed by five substrate columns whose heads are IEOT, IMOT and IIOT under the Deamination block and CIOT and CEOT under the Dechlorination block, and three kinetic-measure rows whose labels are Km (uM), kcat (s-1) and kcat/Km (mM-1 s-1) in that printed order. The cited cell set is the substrate column IEOT of the deamination block: row Km (uM) = 20; row kcat (s-1) = 3.2; row kcat/Km (mM-1 s-1) = 160. Captured primary segment: Table 2, substrate column IEOT (deamination block) | construct AtzB wild type | substrate IEOT, 2-(N-Ethylamino)-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine, hydroxyatrazine | condition pH 7.0 at 23 C | Km 20 uM | kcat 3.2 s-1 | kcat/Km 160 mM-1 s-1

normalized_value_unit_evidence: Km: printed Table 2 cell 20 uM; 1 uM is 1/1000 mM, so 20 / 1000 = 0.02 mM. kcat: printed Table 2 cell 3.2 s-1; the printed turnover row of this table is already per second, so no unit conversion applies and the paper value is 3.2 s^(-1). kcat/Km: printed Table 2 cell 160 mM-1 s-1; the printed efficiency row is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 160.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate column IEOT (deamination block), AtzB wild type: Km = 20 uM; kcat = 3.2 s-1; printed kcat/Km = 160 mM-1 s-1.

table_label: Table 2: Kinetic values for substrate hydrolysis by AtzB (Journal of Bacteriology 2007, 189(19):6989-6997)

substrate: Hydroxyatrazine


column_label: Table 2 (Kinetic values for substrate hydrolysis by AtzB) prints one kinetic-measure label column followed by five substrate columns whose heads are IEOT, IMOT and IIOT under the Deamination block and CIOT and CEOT under the Dechlorination block, and three kinetic-measure rows whose labels are Km (uM), kcat (s-1) and kcat/Km (mM-1 s-1) in that printed order. The cited cell set is the substrate column CIOT of the dechlorination block: row Km (uM) = 120; row kcat (s-1) = 1.9; row kcat/Km (mM-1 s-1) = 16. Captured primary segment: Table 2, substrate column CIOT (dechlorination block) | construct AtzB wild type | substrate CIOT, 2-Chloro-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine | condition pH 7.0 at 23 C | Km 120 uM | kcat 1.9 s-1 | kcat/Km 16 mM-1 s-1

normalized_value_unit_evidence: Km: printed Table 2 cell 120 uM; 1 uM is 1/1000 mM, so 120 / 1000 = 0.12 mM. kcat: printed Table 2 cell 1.9 s-1; the printed turnover row of this table is already per second, so no unit conversion applies and the paper value is 1.9 s^(-1). kcat/Km: printed Table 2 cell 16 mM-1 s-1; the printed efficiency row is already in s^-1 mM^-1, so no unit conversion applies and the printed cell reads 16.0 s^(-1)*mM^(-1). Quotient disclosure for this column: 1.9 / 0.12 = 15.833333333333334 s^-1 mM^-1, against the printed catalytic-efficiency cell 16 mM-1 s-1, which is that same quantity written to the precision the table uses.

raw_value_unit_evidence: Table 2, substrate column CIOT (dechlorination block), AtzB wild type: Km = 120 uM; kcat = 1.9 s-1; printed kcat/Km = 16 mM-1 s-1.


column_label: Table 2 (Kinetic values for substrate hydrolysis by AtzB) prints one kinetic-measure label column followed by five substrate columns whose heads are IEOT, IMOT and IIOT under the Deamination block and CIOT and CEOT under the Dechlorination block, and three kinetic-measure rows whose labels are Km (uM), kcat (s-1) and kcat/Km (mM-1 s-1) in that printed order. The cited cell set is the substrate column IIOT of the deamination block: row Km (uM) = 29; row kcat (s-1) = 0.8; row kcat/Km (mM-1 s-1) = 28. Captured primary segment: Table 2, substrate column IIOT (deamination block) | construct AtzB wild type | substrate IIOT, 2,4-Diisopropylamino-6-hydroxy-1,3,5-triazine | condition pH 7.0 at 23 C | Km 29 uM | kcat 0.8 s-1 | kcat/Km 28 mM-1 s-1

normalized_value_unit_evidence: Km: printed Table 2 cell 29 uM; 1 uM is 1/1000 mM, so 29 / 1000 = 0.029 mM. kcat: printed Table 2 cell 0.8 s-1; the printed turnover row of this table is already per second, so no unit conversion applies and the paper value is 0.8 s^(-1). kcat/Km: printed Table 2 cell 28 mM-1 s-1; the printed efficiency row is already in s^-1 mM^-1, so no unit conversion applies and the printed cell reads 28.0 s^(-1)*mM^(-1). Quotient disclosure for this column: 0.8 / 0.029 = 27.586206896551726 s^-1 mM^-1, against the printed catalytic-efficiency cell 28 mM-1 s-1, which is that same quantity written to the precision the table uses.

raw_value_unit_evidence: Table 2, substrate column IIOT (deamination block), AtzB wild type: Km = 29 uM; kcat = 0.8 s-1; printed kcat/Km = 28 mM-1 s-1.


column_label: Table 2 (Kinetic values for substrate hydrolysis by AtzB) prints one kinetic-measure label column followed by five substrate columns whose heads are IEOT, IMOT and IIOT under the Deamination block and CIOT and CEOT under the Dechlorination block, and three kinetic-measure rows whose labels are Km (uM), kcat (s-1) and kcat/Km (mM-1 s-1) in that printed order. The cited cell set is the substrate column IMOT of the deamination block: row Km (uM) = 40; row kcat (s-1) = 1.4; row kcat/Km (mM-1 s-1) = 35. Captured primary segment: Table 2, substrate column IMOT (deamination block) | construct AtzB wild type | substrate IMOT, 6-Hydroxy-4-(N-isopropylamino)-2-(N-methylamino)-1,3,5-triazine | condition pH 7.0 at 23 C | Km 40 uM | kcat 1.4 s-1 | kcat/Km 35 mM-1 s-1

normalized_value_unit_evidence: Km: printed Table 2 cell 40 uM; 1 uM is 1/1000 mM, so 40 / 1000 = 0.04 mM. kcat: printed Table 2 cell 1.4 s-1; the printed turnover row of this table is already per second, so no unit conversion applies and the paper value is 1.4 s^(-1). kcat/Km: printed Table 2 cell 35 mM-1 s-1; the printed efficiency row is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 35.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate column IMOT (deamination block), AtzB wild type: Km = 40 uM; kcat = 1.4 s-1; printed kcat/Km = 35 mM-1 s-1.


column_label: Table 2 (Kinetic values for substrate hydrolysis by AtzB) prints one kinetic-measure label column followed by five substrate columns whose heads are IEOT, IMOT and IIOT under the Deamination block and CIOT and CEOT under the Dechlorination block, and three kinetic-measure rows whose labels are Km (uM), kcat (s-1) and kcat/Km (mM-1 s-1) in that printed order. The cited cell set is the substrate column CEOT of the dechlorination block: row Km (uM) = 230; row kcat (s-1) = 1.6; row kcat/Km (mM-1 s-1) = 7. Captured primary segment: Table 2, substrate column CEOT (dechlorination block) | construct AtzB wild type | substrate CEOT, 2-Chloro-4-(N-ethylamino)-6-hydroxy-1,3,5-triazine | condition pH 7.0 at 23 C | Km 230 uM | kcat 1.6 s-1 | kcat/Km 7 mM-1 s-1

normalized_value_unit_evidence: Km: printed Table 2 cell 230 uM; 1 uM is 1/1000 mM, so 230 / 1000 = 0.23 mM. kcat: printed Table 2 cell 1.6 s-1; the printed turnover row of this table is already per second, so no unit conversion applies and the paper value is 1.6 s^(-1). kcat/Km: printed Table 2 cell 7 mM-1 s-1; the printed efficiency row is already in s^-1 mM^-1, so no unit conversion applies and the printed cell reads 7.0 s^(-1)*mM^(-1). Quotient disclosure for this column: 1.6 / 0.23 = 6.956521739130435 s^-1 mM^-1, against the printed catalytic-efficiency cell 7 mM-1 s-1, which is that same quantity written to the precision the table uses.

raw_value_unit_evidence: Table 2, substrate column CEOT (dechlorination block), AtzB wild type: Km = 230 uM; kcat = 1.6 s-1; printed kcat/Km = 7 mM-1 s-1.


substrate_name: H2O; Hydroxyatrazine

sequence_source: UniProtKB reviewed accession P95442/ATZB_PSESD FASTA, checked 2026-06-29; selected SABIO accession text '(P95442)*2' was interpreted only as identity context and not as a clean source tuple.

normalized_value_unit_evidence: Km: printed Table 2 cell 20 uM; 1 uM is 1/1000 mM, so 20 / 1000 = 0.02 mM. kcat: printed Table 2 cell 3.2 s-1; the printed turnover row of this table is already per second, so no unit conversion applies and the paper value is 3.2 s^(-1). kcat/Km: printed Table 2 cell 160 mM-1 s-1; the printed efficiency row is already in s^-1 mM^-1, so no unit conversion applies and the printed cell reads 160.0 s^(-1)*mM^(-1). The live export row holds no kcat_over_km for this measurement and this pass adds none.

row_label: Table 2, substrate column IEOT (deamination block), AtzB wild type

substrate: H2O; Hydroxyatrazine


organism: Streptococcus pneumoniae

proof_lines: Km-value is determined using purified membranes from Escherichia coli expressing Streptococcus pneumoniae, pH 7.4, 37°C


enzyme_display_name: D-amino-acid N-acetyltransferase

organism: Saccharomyces cerevisiae

substrate_name: D-serine

sequence_source: UniProtKB reviewed accession P39979 (HPA3_YEAST), queried from the PMID 15375647 HPA3/Hpa3p paper anchor

assay_conditions_summary: 303.15 K; cofactor CoA

enzyme: D-amino-acid N-acetyltransferase

substrate: D-serine


organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

substrate_name: glycerol-3-phosphate (at 37 degrees Celsius and at pH 7.4)


substrate_name: Acetyl-CoA; D-Serine

sequence_source: UniProtKB reviewed accession P39979 (HPA3_YEAST), checked by direct UniProt REST/flat-file lookup on 2026-06-29

assay_conditions_summary: cofactor CoA

substrate: Acetyl-CoA; D-Serine


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: D-Serine

substrate: D-Serine


organism: Homo sapiens

substrate_name: glucosylceramide

substrate: glucosylceramide


substrate_name: UDP-D-galactose; Glucosylceramide

sequence_source: UniProtKB reviewed accession Q9UBX8 (B4GT6_HUMAN), fetched 2026-06-29

substrate: UDP-D-galactose; Glucosylceramide


organism: Catharanthus roseus

substrate_name: UDP-alpha-D-glucose

sequence_source: UniProtKB reviewed accession U3U992 (UGT8_CATRO), fetched 2026-06-29

substrate: UDP-alpha-D-glucose


substrate_name: 7-deoxyloganetic acid

proof_lines: kcat is 0.130 sec(-1) for 7-deoxyloganetic acid. kcat is 0.325 sec(-1) for UPD-glucose.

substrate: 7-deoxyloganetic acid


proof_lines: kcat is 0.130 sec(-1) with 7-deoxyloganetic acid as substrate. kcat is 0.325 sec(-1) with UDP-glucose as substrate (PubMed:24104568). kcat is 1.25 sec(-1) with 7-deoxyloganetic acid as substrate (PubMed:24710322).


substrate_name: UDP-galactose

substrate: UDP-galactose


organism: Rattus norvegicus


organism: Unknown

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


organism: Azospirillum brasilense

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+


organism: Rhodospirillum rubrum

substrate_name: NAD

substrate: NAD


organism: Bacillus subtilis (strain 168)

substrate_name: Unknown

proof_lines: The Km value for methylglucuronoxylan from sweetgum is 1.63 mg/ml. The activity is directly correlated to the degree of substitution of the glucuronosyl moiety on the xylan chain.

substrate: Unknown


organism: Dickeya chrysanthemi


enzyme_display_name: Glucuronoxylanase XynC

organism: Bacillus subtilis

substrate_name: H2O; 4-O-Methyl-D-glucuronoxylan

sequence_source: UniProtKB reviewed accession Q45070 direct lookup

enzyme: Glucuronoxylanase XynC

substrate: H2O; 4-O-Methyl-D-glucuronoxylan


enzyme_display_name: albendazole monooxygenase

substrate_name: trimethylamine (at pH 8.5)

enzyme: albendazole monooxygenase

substrate: trimethylamine (at pH 8.5)


organism: Dicrocoelium dendriticum

substrate_name: albendazole S-oxide

proof_lines: mitochondrial fraction in vitro, pH 7.4, 37°C

proof_lines: microsomal fraction in vitro, pH 7.4, 37°C

substrate: albendazole S-oxide


organism: Ictalurus punctatus

substrate_name: H+; NADPH; O2; Albendazole

assay_conditions_summary: cofactor NADPH

substrate: H+; NADPH; O2; Albendazole


organism: Oncorhynchus mykiss


organism: Oreochromis sp.


organism: Escherichia coli

substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: UDPglucose

substrate: UDPglucose


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: lipopolysaccharide

proof_lines: in presence of optimal concentrations of phosphatidylethanolamine

substrate: lipopolysaccharide


organism: Salmonella typhimurium

substrate_name: UDPglucose; Lipopolysaccharide

sequence_source: UniProtKB:P19817 canonical FASTA, direct exact-accession lookup on 2026-06-29

substrate: UDPglucose; Lipopolysaccharide


substrate_name: beta-Alanine

sequence_source: UniProtKB:P50554 linked from PMID 10989446

proof_lines: competitive to beta-alanine, pH 8.8, 37°C

proof_lines: uncompetitive against 2-oxoglutarate, pH 8.8, 37°C

substrate: beta-Alanine


substrate_name: 2-Oxoglutarate; L-3-Amino-isobutanoate

sequence_source: UniProtKB:P50554 direct accession lookup

substrate: 2-Oxoglutarate; L-3-Amino-isobutanoate


proof_lines: pH 7.5, 30°C, Fe protein as the acceptor of ADP-ribose, in the presence of MgADP-


enzyme_display_name: [pyruvate, phosphate dikinase] kinase

organism: Arabidopsis thaliana

substrate_name: Pyruvate, phosphate dikinase; ADP

enzyme: [pyruvate, phosphate dikinase] kinase

substrate: Pyruvate, phosphate dikinase; ADP


enzyme_display_name: molybdenum cofactor sulfurtransferase

substrate_name: L-Cysteine; 1,4-Dithiothreitol

proof_lines: for the L-cysteine desulfurase domain, 2 mM DTT, pH 9.3, 37°C

enzyme: molybdenum cofactor sulfurtransferase

substrate: L-Cysteine; 1,4-Dithiothreitol


organism: Homo sapiens

substrate_name: Benzamidoxime; NADH; H+

substrate: Benzamidoxime; NADH; H+


organism: Sus scrofa


enzyme_display_name: CoA:oxalate CoA-transferase

substrate_name: acetyl-CoA

assay_conditions_summary: pH 6.7; 298.15 K; cofactor CoA

enzyme: CoA:oxalate CoA-transferase

substrate: acetyl-CoA


substrate_name: oxalate

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

substrate: oxalate


substrate_name: NAD+

proof_lines: cosubstrate native ADP-D-ribosyl-[dinitrogen reductase], in the presence of MgADP-

proof_lines: cosubstrate ADP-D-ribosyl-[dinitrogen reductase] from Klebsiella pneumoniae, in the absence of MgADP-

proof_lines: cosubstrate ADP-D-ribosyl-[dinitrogen reductase] from Azotobacter vinelandii, in the absence of MgADP-

substrate: NAD+


organism: Zea mays

substrate_name: ADP

assay_conditions_summary: pH 8.3; 303.15 K; cofactor ADP

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

proof_lines: pyruvate,Pi dikinase phosphorylated at a His residue, pH 8.3, temperature not specified in the publication

substrate: ADP


enzyme_display_name: carbonic anhydrase

proof_lines: pH 6.28, MES buffer, carbonic anhydrase I mutant V62N,H67N,H200T

proof_lines: pH 8.98, TAPS buffer, carbonic anhydrase I mutant V62N,H67N,H200T

proof_lines: pH 7.23, 1-methylimidazolebuffer, carbonic anhydrase I mutant V62N,H67N,H200T

enzyme: carbonic anhydrase


substrate_name: ADP (at pH 6.8)

assay_conditions_summary: pH 6.8; cofactor ADP

substrate: ADP (at pH 6.8)


substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: benzamidoxime

substrate: benzamidoxime


organism: Acetobacter aceti

substrate_name: oxalate (at pH 6.7 and 25 degrees Celsius)

sequence_source: source_record; UniProtKB:A9X6P9

assay_conditions_summary: pH 6.7; cofactor CoA

proof_lines: kcat is 1.8 sec(-1) for the CoA-transferase activity with oxalate as substrate (at pH 6.7 and 25 degrees Celsius). kcat is 2 sec(-1) for the CoA-transferase activity with acetyl-CoA as substrate (at pH 6.7 and 25 degrees Celsius).


organism: Escherichia coli (strain K12)

substrate_name: acetyl-CoA (at pH 6.7 and 25 degrees Celsius)

sequence_source: source_record; UniProtKB:P76518

proof_lines: kcat is 11 sec(-1) for the CoA-transferase activity with acetyl-CoA as substrate (at pH 6.7 and 25 degrees Celsius). kcat is 15 sec(-1) for the CoA-transferase activity with oxalate as substrate (at pH 6.7 and 25 degrees Celsius).


enzyme_display_name: mannosyl-3-phosphoglycerate phosphatase

organism: Pyrococcus horikoshii

sequence_source: UniProtKB REST canonical sequence for O58690 (MPGP_PYRHO), queried 2026-06-29; MD5=7F432BF84DD27642FF31B20A7399BDAD

enzyme: mannosyl-3-phosphoglycerate phosphatase


organism: Thermus thermophilus

sequence_source: UniProtKB REST canonical sequence for Q84B23 (Q84B23_THETH), queried 2026-06-29; MD5=4A54F9943D4012189CAC75E5918BA5E4


organism: Bacteroides thetaiotaomicron

sequence_source: UniProtKB REST canonical sequence for Q8AAI7 (GMHBA_BACTN), queried 2026-06-29; MD5=B66102C560A5B5E75D6F57A4B1790364


enzyme_display_name: N(1)-aminopropylagmatine ureohydrolase

organism: Thermococcus kodakarensis

sequence_source: UniProtKB REST canonical sequence for Q5JI38 (APAUH_THEKO), queried 2026-06-29; MD5=35228BD9D101E7D36A16160659A45C80

smiles: N=C(N)NCCCCNCCCN

enzyme: N(1)-aminopropylagmatine ureohydrolase


substrate_name: agmatine

smiles: N=C(N)NCCCCN

substrate: agmatine


enzyme_display_name: prephenate decarboxylase

organism: Bacillus subtilis

substrate_name: prephenate

sequence_source: UniProtKB REST canonical sequence for P39638 (BACA_BACSU), queried 2026-06-29; MD5=33BE7A58F2127EF6C2CF88A017EC4144

enzyme: prephenate decarboxylase

substrate: prephenate


organism: Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)

substrate_name: GPG (at 30 degrees Celsius)

substrate: GPG (at 30 degrees Celsius)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: glucosyl-3-phosphoglycerate (at 37 degrees Celsius)


organism: Persephonella marina (strain DSM 14350 / EX-H1)

substrate_name: GPG (at 70 degrees Celsius)

substrate: GPG (at 70 degrees Celsius)


sequence_source: UniProtKB reviewed accession O58690 (MPGP_PYRHO)


enzyme_display_name: coccolysin

organism: Enterococcus faecalis

substrate_name: Substance P

proof_lines:
scissile bond Gln6-Phe7
scissile bond Phe7-Phe8
scissile bond Gly9-Leu10

enzyme: coccolysin

substrate: Substance P


organism: Enterococcus faecalis subsp. liquefaciens

substrate_name: Insulin B chain; H2O

substrate: Insulin B chain; H2O


organism: Planktothrix agardhii

sequence_source: UniProtKB reviewed accession A0A073CEA3 (AERD_PLAA1)

proof_lines: pH and temperature not specified in the publication


organism: Salinispora tropica


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

substrate_name: alpha-HBP (at pH 7.5 and 25 degrees Celsius)

proof_lines: kcat is 29 sec(-1) and 13 sec(-1) with alpha-HBP and beta-HBP as substrate, respectively. Thus, the enzyme displays 6-fold more efficiency towards the alpha- than the beta-anomer (PubMed:20050615).


organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

substrate_name: D-glycero-alpha-D-manno-heptose 1,7-bisphosphate (at pH 7.4)

proof_lines: kcat is 0.12 sec(-1) for D-glycero-alpha-D-manno-heptose 1,7-bisphosphate.


organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)

substrate_name: APA

proof_lines: kcat is 70.8 sec(-1) with APA as substrate.

substrate: APA


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

substrate_name: N(1)-aminopropylagmatine (at pH 7.5 and 70 degrees Celsius)

proof_lines: kcat is 1.86 sec(-1) for ureohydrolase activity with agmatine as substrate (at pH 7.5 and 70 degrees Celsius). kcat is 1.01 sec(-1) for ureohydrolase activity with N(1)-aminopropylagmatine as substrate (at pH 7.5 and 70 degrees Celsius).


organism: Bacillus subtilis (strain 168)

proof_lines: kcat is 190 min(-1) for decarboxylase activity with prephenate as substrate.


organism: Planktothrix agardhii (strain NIVA-CYA 126/8)

proof_lines: kcat is 245 min(-1) for decarboxylase activity with prephenate as substrate.


enzyme_display_name: xylonate dehydratase

organism: Pseudomonas sp.

substrate_name: D-gluconate

enzyme: xylonate dehydratase

substrate: D-gluconate


organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)

substrate_name: xylonate

substrate: xylonate


organism: Escherichia coli

substrate_name: D-xylonate

sequence_source: UniProtKB:P39358 REST lookup on 2026-06-29

substrate: D-xylonate


organism: Haloferax volcanii

substrate_name: D-Gluconate; D-Xylonate

sequence_source: UniProtKB:D4GP40 REST lookup on 2026-06-29

substrate: D-Gluconate; D-Xylonate


substrate_name: D-xylonate; D-gluconate

assay_conditions_summary: pH 7.5; 315.15 K; buffer 0.1 M Tris-HCl

proof_lines: at 42°C, in 0.1 M Tris-HCl buffer, pH 7.5, 2.5 M KCl, 50 mM MgCl2

substrate: D-xylonate; D-gluconate


organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15)

proof_lines: kcat is 1406 min(-1) with D-xylonate as substrate. kcat is 2626 min(-1) with D-gluconate as substrate. kcat is 46 min(-1) with L-arabinonate as substrate. kcat is 218 min(-1) with D-galactonate as substrate. kcat is 196 min(-1) with D-fucon


organism: Escherichia coli (strain K12)


enzyme_display_name: 3-methyl-L-tyrosine peroxygenase

organism: Streptomyces lavendulae

proof_lines: kcat is 17.8 min(-1) with 3-methyl-L-tyrosine as substrate. kcat is 12.3 min(-1) with L-tyrosine as substrate.

enzyme: 3-methyl-L-tyrosine peroxygenase


substrate_name: L-tyrosine

sequence_source: UniProtKB B0CN28 direct FASTA/JSON lookup

substrate: L-tyrosine


enzyme_display_name: 9beta-pimara-7,15-diene oxidase

organism: Oryza sativa subsp. japonica

substrate_name: syn-pimaradiene

proof_lines: kcat is 46 sec(-1) with syn-pimaradiene as substrate and 49 sec(-1) with syn-stemodene as substrate.

enzyme: 9beta-pimara-7,15-diene oxidase

substrate: syn-pimaradiene


organism: Oryza sativa

substrate_name: 9beta-Pimara-7,15-diene; NADPH; O2

sequence_source: UniProtKB reviewed accession Q0JF01 (C99A3_ORYSJ)

substrate: 9beta-Pimara-7,15-diene; NADPH; O2


organism: Arabidopsis thaliana

sequence_source: UniProtKB Q42569 canonical sequence from direct REST lookup


proof_lines: kcat is 0.74 min(-1) for (22S)-22-hydroxycampesterol (PubMed:22822057). kcat is 0.11 min(-1) for (22R,23R)-22,23-dihydroxycampesterol (PubMed:22822057).


enzyme_display_name: gibberellin A9 O-methyltransferase

substrate_name: gibberellin a4

sequence_source: UniProtKB:F4JUY5 (GAMT1_ARATH, UniProtKB reviewed (Swiss-Prot))

enzyme: gibberellin A9 O-methyltransferase

substrate: gibberellin a4


substrate_name: gibberellin a9

substrate: gibberellin a9


enzyme_display_name: gibberellin A4 carboxyl methyltransferase

sequence_source: UniProtKB:Q5XF78 (GAMT2_ARATH, UniProtKB reviewed (Swiss-Prot))


enzyme: gibberellin A4 carboxyl methyltransferase


proof_lines: kcat is 0.01 sec(-1) for GA4. kcat is 0.026 sec(-1) for GA9.


proof_lines: kcat is 0.0015 sec(-1) for GA4. kcat is 0.0018 sec(-1) for GA9.


enzyme_display_name: 10-deoxymethynolide syntase

organism: Streptomyces venezuelae

enzyme: 10-deoxymethynolide syntase


proof_lines: pH 7.2, 30°C, kcat for activity with the polyketide synthase PikAIII/polyketide synthase PikAIV complex in formation of 10-deoxymethynolide

proof_lines: pH 7.2, 30°C, KM-value for activity with the polyketide synthase PikAIII/polyketide synthase PikAIV complex in formation of 10-deoxymethynolide

proof_lines: pH 7.2, 30°C, kcat/Km-value for activity with the polyketide synthase PikAIII/polyketide synthase PikAIV complex in formation of 10-deoxymethynolide


enzyme_display_name: narbonolide synthase

enzyme: narbonolide synthase


proof_lines: pH 7.2, 30°C, kcat for activity with the polyketide synthase PikAIII/polyketide synthase PikAIV complex in formation of narbonolide

proof_lines: pH 7.2, 30°C, Km-valkue for activity with the polyketide synthase PikAIII/polyketide synthase PikAIV complex in formation of narbonolide

proof_lines: pH 7.2, 30°C, kcat/Km-value for activity with the polyketide synthase PikAIII/polyketide synthase PikAIV complex in formation of narbonolide


sequence_source: source_record; UniProt Q9ZGI2 FASTA match checked 2026-06-30

proof_lines: kcat is 56 min(-1) for thioesterase activity with 2-methyl-3-ketopentanoyl-SNAC as substrate. kcat is 7.9 min(-1) for thioesterase activity with (2S,3R)-2-methyl-3-hydroxyacyl-SNAC as substrate. kcat is 4.3 min(-1) for thioesterase activity


enzyme_display_name: baicalein 7-O-glucuronosyltransferase

organism: Scutellaria baicalensis

substrate_name: baicalein

enzyme: baicalein 7-O-glucuronosyltransferase

substrate: baicalein


substrate_name: UDP-D-glucuronate; Baicalein

sequence_source: UniProtKB reviewed Swiss-Prot Q76MR7 direct accession lookup; canonical sequence for UBGAT_SCUBA.

substrate: UDP-D-glucuronate; Baicalein


substrate_name: scutellarein

substrate: scutellarein


enzyme_display_name: soyasapogenol B glucuronide galactosyltransferase

organism: Glycine max

substrate_name: UDP-D-galactose; Soyasapogenol B monoglucuronide

sequence_source: UniProtKB reviewed accession D4Q9Z4


substrate_name: soyasapogenol B 3-O-beta-D-glucuronide

enzyme: soyasapogenol B glucuronide galactosyltransferase

substrate: soyasapogenol B 3-O-beta-D-glucuronide


enzyme_display_name: [amino group carrier protein]-gamma-(L-lysyl)-L-glutamate

organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

proof_lines: kcat is 1.0 sec(-1) with N(2)-acetyl-L-ornithine as substrate. kcat is 0.8 sec(-1) with N(2)-acetyl-L-lysine as substrate.


organism: Thermus thermophilus

sequence_source: UniProtKB reviewed accession Q93R93

enzyme: [amino group carrier protein]-gamma-(L-lysyl)-L-glutamate


enzyme_display_name: taurine--pyruvate aminotransferase

organism: Bilophila wadsworthia

substrate_name: taurine

enzyme: taurine--pyruvate aminotransferase

substrate: taurine


sequence_source: UniProtKB FASTA Q9APM5


substrate_name: Pyruvate; Taurine

substrate: Pyruvate; Taurine


organism: Geobacillus thermodenitrificans subsp. thermodenitrificans

sequence_source: UniProtKB FASTA A0A0S2VC96


substrate_name: glycyrrhetinic acid-3-O-monoglucoside

sequence_source: UniProtKB reviewed accession D4Q9Z4 direct REST lookup on 2026-06-30

substrate: glycyrrhetinic acid-3-O-monoglucoside


organism: Campylobacter jejuni subsp. jejuni serotype O:2

sequence_source: UniProtKB reviewed accession Q0P8J8 direct REST lookup on 2026-06-30


substrate_name: CTP

substrate: CTP


organism: Pseudomonas denitrificans

sequence_source: UniProtKB reviewed accession P29936 direct REST lookup on 2026-06-30; sequence kept as context only because of taxonomy caveat


organism: Pseudomonas denitrificans (nom. rej.)

substrate_name: adenosylcobinamide-GDP

substrate: adenosylcobinamide-GDP


organism: Sinorhizobium sp

substrate_name: alpha-ribazole 5'-phosphate

substrate: alpha-ribazole 5'-phosphate


organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

substrate_name: L-glutamine phosphate

proof_lines: kcat is 57 min(-1) with L-glutamine phosphate as substrate (in the presence of MgCTP) (PubMed:29023101). kcat is 0.35 min(-1) with L-glutamine phosphate as substrate (in the presence of MnCTP). kcat is 0.6 min(-1) with phosphoramidate as su

substrate: L-glutamine phosphate


organism: Salmonella enterica

substrate_name: alpha-ribazole

substrate: alpha-ribazole


enzyme_display_name: phosphoribosyl 1,2-cyclic phosphate 1,2-diphosphodiesterase

organism: Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B)

proof_lines: kcat is 2.0 sec(-1) for 5-phospho-alpha-D-ribose 1,2-cyclic phosphate. kcat is 7.4 sec(-1) for D-ribofuranose 2,5-bisphosphate.


enzyme_display_name: Phosphoribosyl 1,2-cyclic phosphate 1,2-diphosphodiesterase

enzyme_name_source: UniProtKB C8WJZ5

organism: Eggerthella lenta

sequence_source: UniProtKB C8WJZ5 FASTA


substrate_name: D-ribofuranose 2,5-bisphosphate

enzyme: Phosphoribosyl 1,2-cyclic phosphate 1,2-diphosphodiesterase

substrate: D-ribofuranose 2,5-bisphosphate


enzyme_display_name: linear primary-alkylsulfatase

organism: Pseudomonas aeruginosa

substrate_name: SDS

sequence_source: UniProtKB direct accession lookup: Q9I5I9

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

enzyme: linear primary-alkylsulfatase

substrate: SDS


organism: Pseudomonas sp. S9

sequence_source: UniProtKB direct accession lookup: F2WP51

proof_lines:
at pH 7.1 and 25°C
at pH 9.0 and 70°C
Raw SKiD Env: Temp=25°C, pH=7.1


enzyme_display_name: chorismatase

organism: Actinoplanes sp. N902-109

substrate_name: chorismate

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

enzyme: chorismatase

substrate: chorismate


organism: Streptomyces hygroscopicus subsp. ascomyceticus

sequence_source: UniProtKB direct accession lookup: Q9KID9

proof_lines: wild type enzyme, in 100 mM Tris-HCl (pH 7.0), at 25°C


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

proof_lines: kcat is 337 min(-1) with 1-octyl sulfate as substrate. kcat is 5.4 min(-1) with (R)-2-octyl sulfate as substrate.


organism: Pseudomonas sp

proof_lines: kcat is 4.88 sec(-1) with SDS as substrate.


organism: Streptomyces hygroscopicus

proof_lines: kcat is 17.6 sec(-1) for chorismatase activity with chorismate as substrate.


assay_conditions_summary: pH 7; 293.15 K; buffer deuterated potassium phosphate

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


enzyme_display_name: [amino group carrier protein]-lysine hydrolase

organism: Thermus thermophilus

sequence_source: UniProtKB reviewed accession Q5SHH3; direct REST check on 2026-06-30


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8VUS5; direct REST check on 2026-06-30 and applied mutation signature R282E to reconstruct the assayed variant sequence.

enzyme: [amino group carrier protein]-lysine hydrolase


sequence_source: UniProtKB reviewed accession Q8VUS5; direct REST check on 2026-06-30


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8VUS5; direct REST check on 2026-06-30 and applied mutation signature R286E to reconstruct the assayed variant sequence.


organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

proof_lines: kcat is 51.8 sec(-1) with N(2)-acetyl-L-lysine. kcat is 28.1 sec(-1) with N(2)-acetyl-L-ornithine.


enzyme_display_name: barbiturase

organism: Nocardioides sp.

substrate_name: H2O; Barbituric acid

sequence_source: UniProtKB A1SPN2 reviewed entry fetched 2026-06-30

enzyme: barbiturase

substrate: H2O; Barbituric acid


sequence_source: UniProtKB A1SGT4 reviewed entry fetched 2026-06-30


organism: Rhodococcus erythropolis

substrate_name: Barbiturate

sequence_source: UniProtKB Q8RSQ2 reviewed entry fetched 2026-06-30

substrate: Barbiturate


organism: Mycobacterium sp.


substrate_name: barbituric acid

proof_lines: kcat is 115 sec(-1) with barbituric acid as substrate.

substrate: barbituric acid


enzyme_display_name: spore photoproduct lyase

organism: Bacillus subtilis (strain 168)

substrate_name: SPTpT

proof_lines: SPTpT is the spore photoproduct of the TpT dinucleoside.

enzyme: spore photoproduct lyase

substrate: SPTpT


organism: Bacillus subtilis

sequence_source: UniProtKB reviewed entry P37956


organism: Geobacillus thermodenitrificans

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


proof_lines: mutant C140A, pH and temperature not specified in the publication


proof_lines: mutant Y98F, pH and temperature not specified in the publication


enzyme_display_name: 3-cyanoalanine hydratase

organism: Lupinus angustifolius

substrate_name: Beta-cyano-L-alanine

enzyme: 3-cyanoalanine hydratase

substrate: Beta-cyano-L-alanine


organism: Pseudomonas sp.


substrate_name: H2O; 3-Cyano-L-alanine

sequence_source: UniProtKB reviewed exact accession Q3LRV4

substrate: H2O; 3-Cyano-L-alanine


sequence_source: UniProtKB reviewed exact accession Q5QGZ8


organism: Arabidopsis thaliana

substrate_name: Ala(CN) (for the nitrilase activity)

substrate: Ala(CN) (for the nitrilase activity)


substrate_name: Ala(CN)

substrate: Ala(CN)


enzyme_display_name: (S)-scoulerine 9-O-methyltransferase

organism: Berberis wilsoniae

substrate_name: S-adenosyl-L-methionine

enzyme: (S)-scoulerine 9-O-methyltransferase

substrate: S-adenosyl-L-methionine


organism: Papaver somniferum

substrate_name: (S)-scoulerine

substrate: (S)-scoulerine


organism: Eschscholzia californica subsp. californica

substrate_name: (S)-reticuline

sequence_source: UniProtKB A0A224ALZ8 FASTA/JSON, direct exact-accession lookup

proof_lines: cosubstrate (S)-reticuline, product norlaudanine, pH 8.4, 35°C

proof_lines: cosubstrate (S)-scoulerine, product (S)-tetrahydrocolumbamine, pH 8.4, 35°C

substrate: (S)-reticuline


substrate_name: (S)-norreticuline

substrate: (S)-norreticuline


sequence_source: UniProtKB I3PLQ7 FASTA/JSON, direct exact-accession lookup

proof_lines: pH 7.5, 37°C, recombinant detagged enzyme


organism: Stephania intermedia

sequence_source: UniProtKB A0A5P9PAM0 FASTA/JSON, direct exact-accession lookup; UniProt entry is flagged as Fragment


enzyme_display_name: aspartate racemase

organism: Acropora millepora

substrate_name: D-Aspartate

proof_lines: recombinant His-tagged mutant P150S, pH 8.0, 30°C

enzyme: aspartate racemase

substrate: D-Aspartate


substrate_name: L-aspartate

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

substrate: L-aspartate


organism: Anadara broughtonii

assay_conditions_summary: pH 5.53; 303.15 K; cofactor ATP

proof_lines:
pH 5.53, 1 mM ATP
pH 5.53, 2 mM ATP
pH 8.0, 30°C


organism: Anneissia japonica


organism: Aplysia californica


organism: Bifidobacterium bifidum

substrate_name: D-Asp

substrate: D-Asp


organism: Enterococcus faecalis

substrate_name: L-Asp

substrate: L-Asp


organism: Macrostomum lignano


organism: Manihot esculenta

substrate_name: D-glutamic acid

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication

substrate: D-glutamic acid


organism: Mus musculus


organism: Saccoglossus kowalevskii

substrate_name: D-glutamate

proof_lines: wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme

proof_lines: pH 8.0, temperature not specified in the publication, wild-type enzyme, Asp/GluR enzyme

proof_lines: pH 8.0, temperature not specified in the publication, wild-type enzyme, AspR enzyme

substrate: D-glutamate


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme S156A, AspR enzyme


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme AS56A, AspR enzyme


proof_lines: mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme A156S, Asp/GluR enzyme


organism: Sphagnum girgensohnii


organism: Spirogyra pratensis


organism: Streptococcus thermophilus

proof_lines: recombinant enzyme, pH 8.3, 37°C, coupling method assay


organism: Magallana gigas


proof_lines: recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C


organism: Microcystis aeruginosa

sequence_source: UniProtKB REST exact accession Q9RNB4


sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession Q9RNB4 plus C195S reconstruction and applied mutation signature C195S to reconstruct the assayed variant sequence.


organism: Penaeus monodon


organism: Picrophilus oshimae


organism: Pyrococcus horikoshii

sequence_source: UniProtKB REST exact accession O58403


organism: Solanum lycopersicum

substrate_name: D-serine

sequence_source: UniProtKB REST exact accession A0A3Q7FTJ5

substrate: D-serine


organism: Thermococcus litoralis

sequence_source: UniProtKB REST exact accession H3ZNI2


enzyme_display_name: isocitrate dehydrogenase (NADP(+))

organism: Aeropyrum pernix

substrate_name: NADP+

sequence_source: UniProtKB exact accession Q9YE81 via rest.uniprot.org/uniprotkb/Q9YE81

assay_conditions_summary: pH 8; 343.15 K; cofactor NADP+

enzyme: isocitrate dehydrogenase (NADP(+))

substrate: NADP+


organism: Archaeoglobus fulgidus

substrate_name: NAD+

sequence_source: UniProtKB exact accession O29610 via rest.uniprot.org/uniprotkb/O29610

assay_conditions_summary: pH 8; 333.15 K; cofactor NADP+

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=60°C, pH=8

substrate: NAD+


organism: Bos taurus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+


organism: Desulfotalea psychrophila

sequence_source: UniProtKB exact accession Q6AQ66 via rest.uniprot.org/uniprotkb/Q6AQ66

assay_conditions_summary: 278.15 K; cofactor NADP+

proof_lines:
Raw SKiD Env: Temp=5°C, pH=-----
Raw SKiD Env: Temp=25°C, pH=-----


organism: Escherichia coli

substrate_name: isocitrate

sequence_source: UniProtKB exact accession P08200 via rest.uniprot.org/uniprotkb/P08200

substrate: isocitrate


organism: Homo sapiens

sequence_source: UniProtKB exact accession O75874 via rest.uniprot.org/uniprotkb/O75874

assay_conditions_summary: pH 6.8; 310.15 K; cofactor NADP+

proof_lines:
Raw SKiD Env: Temp=37°C, pH=6.8
Raw SKiD Env: Temp=21°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.2


sequence_source: UniProtKB exact accession P48735 via rest.uniprot.org/uniprotkb/P48735

assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8
Raw SKiD Env: Temp=-----, pH=-----


organism: Mus musculus

sequence_source: UniProtKB exact accession P54071 via rest.uniprot.org/uniprotkb/P54071

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=7.5


sequence_source: UniProtKB exact accession O88844 via rest.uniprot.org/uniprotkb/O88844


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB exact accession P9WKL1 via rest.uniprot.org/uniprotkb/P9WKL1

assay_conditions_summary: pH 7.5; cofactor NADP+


organism: Saccharomyces cerevisiae

substrate_name: NADPH

sequence_source: UniProtKB exact accession P21954 via rest.uniprot.org/uniprotkb/P21954

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7.5

substrate: NADPH


organism: Sus scrofa

sequence_source: UniProtKB exact accession P33198 via rest.uniprot.org/uniprotkb/P33198

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


organism: Trypanosoma cruzi

sequence_source: UniProtKB exact accession Q4E4L7 via rest.uniprot.org/uniprotkb/Q4E4L7

assay_conditions_summary: cofactor NADP+


enzyme_display_name: pyranose dehydrogenase (acceptor)

organism: Leucoagaricus meleagris

substrate_name: ferricenium ion

sequence_source: UniProtKB Q3L245 reviewed Swiss-Prot entry PDH1_MACME

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8.5
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=2

enzyme: pyranose dehydrogenase (acceptor)

substrate: ferricenium ion


enzyme_display_name: carboxylesterase

organism: Actinidia eriantha

substrate_name: 4-methylumbelliferyl heptanoate

enzyme: carboxylesterase

substrate: 4-methylumbelliferyl heptanoate


substrate_name: 4-nitrophenyl dodecanoate

proof_lines:
Raw SKiD Env: Temp=60°C, pH=8
Raw SKiD Env: Temp=70°C, pH=7

substrate: 4-nitrophenyl dodecanoate


substrate_name: 4-nitrophenyl propionate

substrate: 4-nitrophenyl propionate


substrate_name: 4-nitrophenyl palmitate

substrate: 4-nitrophenyl palmitate


organism: Bacillus subtilis

substrate_name: p-nitrophenyl acetate

substrate: p-nitrophenyl acetate


substrate_name: 4-nitrophenyl laurate

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

substrate: 4-nitrophenyl laurate


organism: Ferroplasma acidiphilum

substrate_name: 4-nitrophenyl butyrate

proof_lines:
Raw SKiD Env: Temp=50°C, pH=2
Raw SKiD Env: Temp=35°C, pH=6

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl acetate

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=-----

substrate: 4-nitrophenyl acetate


organism: Oryctolagus cuniculus

substrate_name: irinotecan

substrate: irinotecan