substrate_name: (Glycerophosphate)n; CDPglycerol

sequence_variant_note: Resolved canonical sequence from UniProtKB:P13485 direct accession lookup on 2026-06-15 and applied mutation signature E639A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CDP-glycerol glycerophosphotransferase(Enzyme) mutant E639A

enzyme: teichoic acid poly(glycerol phosphate) polymerase

substrate: (Glycerophosphate)n; CDPglycerol


enzyme_display_name: teichoic acid poly(glycerol phosphate) polymerase

organism: Bacillus subtilis

substrate_name: CDPglycerol; (Glycerophosphate)n

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

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

km_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB:P13485 direct accession lookup on 2026-06-15 and applied mutation signature D630A to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: SABIO-RK modifier species: CDP-glycerol glycerophosphotransferase(Enzyme) mutant D630A

substrate: CDPglycerol; (Glycerophosphate)n


enzyme_display_name: propionate kinase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: acetate

source_db: oed

verification_status: unverified

mutation_signature: Unknown

kcat_over_km_origin: calculated

source_license: CC BY 4.0

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

smiles: CC(=O)O

data_origin: experimental

enzyme: propionate kinase

substrate: acetate

status: unverified

source: oed


organism: Salmonella typhimurium

substrate_name: Propanoate; ATP

assay_conditions_summary: cofactor ATP

substrate: Propanoate; ATP


substrate_name: Propanoate

smiles: CCC(=O)O

substrate: Propanoate


substrate_name: Acetate

substrate: Acetate


enzyme_display_name: 2'-5' oligoadenylate synthase

organism: Homo sapiens

substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D408A/D410A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

enzyme: 2'-5' oligoadenylate synthase

substrate: ATP


substrate_name: P1,P3-Bis(5'-adenosyl) triphosphate

substrate: P1,P3-Bis(5'-adenosyl) triphosphate


substrate_name: CDPglycerol

substrate: CDPglycerol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E639A to reconstruct the assayed variant sequence.


kcat_display: Not reported

km_display: Not reported

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H474A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CDP-glycerol glycerophosphotransferase(Enzyme) mutant H474A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D645A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: CDP-glycerol glycerophosphotransferase(Enzyme) mutant D645A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E604A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D630A to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: CDP-glycerol glycerophosphotransferase(Enzyme) mutant E604A


enzyme_display_name: dimethylallylcistransferase

organism: Solanum lycopersicum

substrate_name: isopentenyl diphosphate

source_db: uniprot

enzyme: dimethylallylcistransferase

substrate: isopentenyl diphosphate

source: uniprot


enzyme_display_name: inositol 3-kinase

organism: Zea mays

substrate_name: myo-inositol

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

enzyme: inositol 3-kinase

substrate: myo-inositol


enzyme_display_name: allose kinase

organism: Klebsiella aerogenes

substrate_name: D-allose

source_db: brenda

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

enzyme: allose kinase

substrate: D-allose

source: brenda


organism: Bacillus licheniformis

substrate_name: CDP-glycerol

substrate: CDP-glycerol


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


enzyme_display_name: sedoheptulose-bisphosphatase

organism: Cyberlindnera jadinii

substrate_name: sedoheptulose 1,7-bisphosphate

assay_conditions_summary: pH 6

enzyme: sedoheptulose-bisphosphatase

substrate: sedoheptulose 1,7-bisphosphate


organism: Lathyrus oleraceus


organism: Spinacia oleracea

substrate_name: sedoheptulose 1,7-diphosphate

proof_lines:
reduced enzyme
oxidized enzyme

substrate: sedoheptulose 1,7-diphosphate


organism: Triticum aestivum

proof_lines:
at pH 8.2, in presence of 10 mM Mg2+
with 5 mM phosphate
with 10 mM phosphate


organism: Escherichia coli (strain K12)

substrate_name: D-allose (at 25 degrees Celsius and pH 7.6)

assay_conditions_summary: pH 7.6; cofactor ATP

proof_lines: Catalytic efficiency with D-allose as substrate is 735-fold higher than that with D-glucose.


organism: Mus musculus

proof_lines: kcat is 0.39 sec(-1) with ATP as substrate.


organism: Bacillus subtilis (strain 168)

proof_lines: kcat for CDP-glycerol is 14 min(-1) (PubMed:16141206). kcat for lipid III analog is 26 sec(-1) (PubMed:18465758).


substrate_name: Fructose 1,6-bisphosphate; H2O

sequence_source: UniProtKB:O20252 FASTA direct lookup

substrate: Fructose 1,6-bisphosphate; H2O


organism: Synechococcus elongatus

substrate_name: Sedoheptulose 1,7-bisphosphate; H2O

sequence_source: UniProtKB:Q31QY2 FASTA direct lookup

substrate: Sedoheptulose 1,7-bisphosphate; H2O


organism: Synechocystis sp.

sequence_source: UniProtKB:P73922 FASTA direct lookup

assay_conditions_summary: pH 8

proof_lines: in 50 mM Tris/HCl, pH 8.0, 15 mM MgCl2, 10 mM dithiothreitol, at 289°C


sequence_source: UniProtKB:P46285 FASTA direct lookup


organism: Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)

substrate_name: L-glytamate

substrate: L-glytamate


enzyme_display_name: 3-hydroxyisobutyryl-CoA hydrolase

organism: Rattus norvegicus

assay_conditions_summary: cofactor CoA

enzyme: 3-hydroxyisobutyryl-CoA hydrolase


enzyme_display_name: N-acetylneuraminate synthase

organism: Campylobacter jejuni

substrate_name: N-Acetyl-D-mannosamine; H2O; Phosphoenolpyruvate; N-Acetyl-D-mannosamine; H2O; Phosphoenolpyruvate; N-Acetylneuraminate; Phosphate; N-Propanoylmannosamine; Phosphoenolpyruvate; H2O; N-Propanoylmannosamine; N-Propanoylneuraminate; Phosphoenolpyruvate; H2O; N-Butanoylmannosamine; N-Butanoylmannosamine; N-Butanoylneuraminate

enzyme: N-acetylneuraminate synthase


substrate_name: N-Propanoylmannosamine

substrate: N-Propanoylmannosamine


substrate_name: N-Butanoylmannosamine

substrate: N-Butanoylmannosamine


substrate_name: N-Acetyl-D-mannosamine

substrate: N-Acetyl-D-mannosamine


substrate_name: N-Pentanoylmannosamine

substrate: N-Pentanoylmannosamine


substrate_name: Phosphoenolpyruvate

substrate: Phosphoenolpyruvate


organism: Moritella viscosa


organism: Neisseria meningitidis

substrate_name: phosphoenolpyruvate

proof_lines: 37°C, 100 mM Tris-HCl buffer, pH 7.0, 1 mM MnCl2, 50 microM to 1 mM phosphoenolpyruvate, His-tagged enzyme, purine nucleoside phosphorylase, 200 mircoM 2-amino-6-mercapto-7-methylpurine ribonucleoside

proof_lines: 4.5/1 mixture of 2S-inhibitor/2R-inhibitor, a 1.2/1 mixture of 2S-inhibitor/2R-inhibitor requires a 2.5-fold lower total inhibitor concentration, 37°C, 100 mM Tris-HCl buffer, pH 7.0, 1 mM MnCl2, 50 microM to 1 mM phosphoenolpyruvate, His-t

substrate: phosphoenolpyruvate


organism: Halomonas elongata

substrate_name: L-2,4-diaminobutanoate; 2-oxoglutarate

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature D180V to reconstruct the assayed variant sequence.

substrate: L-2,4-diaminobutanoate; 2-oxoglutarate


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature D180V/F320Y/Q325R to reconstruct the assayed variant sequence.

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


substrate_name: 2-oxoglutarate; L-2,4-diaminobutanoate

substrate: 2-oxoglutarate; L-2,4-diaminobutanoate


substrate_name: N-butanoyl-D-mannosamine

substrate: N-butanoyl-D-mannosamine


organism: Escherichia coli


substrate_name: N-acetyl-D-mannosamine

assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM Tris-acetate

proof_lines: the reaction mixture contains 1 mM MgCl2 in 50 mM Tris-acetate buffer, pH 7.5, at 37°C

substrate: N-acetyl-D-mannosamine


organism: Homo sapiens

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA


organism: Pseudomonas aeruginosa


proof_lines: wild-type enzyme, a deuterium isotope of the substrate is used


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprotkb_O52250_D180V and applied mutation signature D180V to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9I168 direct lookup, release 2026_02


substrate_name: L-2,4-Diaminobutanoate; 2-Oxoglutarate

substrate: L-2,4-Diaminobutanoate; 2-Oxoglutarate


organism: Arabidopsis thaliana

substrate_name: H2O; 3-Hydroxy-2-methylpropanoyl-CoA

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

sequence_source: UniProtKB Q9LKJ1 direct lookup, release 2026_02

assay_conditions_summary: pH 7; 303.15 K; buffer 50 mM Tris/HCl; cofactor CoA

proof_lines: at 30°C, in 50 mM Tris/HCl buffer, pH 7.0

substrate: H2O; 3-Hydroxy-2-methylpropanoyl-CoA


substrate_name: H2O; (S)-3-Hydroxyisobutyryl-CoA

sequence_source: UniProtKB Q6NVY1 direct lookup, release 2026_02

substrate: H2O; (S)-3-Hydroxyisobutyryl-CoA


substrate_name: 3-Hydroxypropanoyl-CoA; H2O

sequence_source: UniProtKB Q5XIE6 direct lookup, release 2026_02

substrate: 3-Hydroxypropanoyl-CoA; H2O


enzyme_display_name: pantoate kinase

organism: Thermococcus kodakaraensis

substrate_name: D-Pantoate

sequence_source: UniProtKB Q5JHF1 direct accession lookup

enzyme: pantoate kinase

substrate: D-Pantoate


substrate_name: ATP

assay_conditions_summary: pH 8; 315.15 K; cofactor ATP

substrate: ATP


organism: Thermococcus kodakarensis

substrate_name: GTP

assay_conditions_summary: pH 7.5; 315.15 K; cofactor ATP

substrate: GTP


substrate_name: CTP

substrate: CTP


substrate_name: UTP

substrate: UTP


enzyme_display_name: guanidinobutyrase

organism: Arthrobacter sp. (strain KUJ 8602)

enzyme: guanidinobutyrase


organism: Aspergillus niger


organism: Brevibacterium helvolum


organism: Candida parapsilosis

proof_lines: 4-guanidinobutyrase activity, pH and temperature not specified in the publication


organism: Gallus sp.


sequence_source: UniProtKB reviewed accession Q9I3S3/GBUA_PSEAE; EC evidence cites PubMed 12029055; sequence fetched 2026-06-15.

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


sequence_source: UniProtKB reviewed accession Q9I3S3/GBUA_PSEAE; EC evidence cites PubMed 21600989; sequence fetched 2026-06-15.


organism: Pseudomonas putida

assay_conditions_summary: pH 9

proof_lines:
at pH 10
at pH 11
at pH 9


organism: Pseudomonas sp.


organism: Tinca tinca

substrate_name: 4-Guanidinobutanoate; H2O

substrate: 4-Guanidinobutanoate; H2O


substrate_name: H2O; 4-Guanidinobutanoate

sequence_source: UniProtKB reviewed entry Q9I3S3 / GBUA_PSEAE FASTA and REST accession check

substrate: H2O; 4-Guanidinobutanoate


smiles: NC(N)=NCCCC(=O)O


enzyme_display_name: coniferyl-alcohol glucosyltransferase

substrate_name: sinapate

enzyme: coniferyl-alcohol glucosyltransferase

substrate: sinapate


substrate_name: coniferyl aldehyde

substrate: coniferyl aldehyde


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


organism: Mus musculus


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

substrate_name: inositol hexakisphosphate

substrate: inositol hexakisphosphate


enzyme_display_name: molybdenum cofactor guanylyltransferase

organism: Escherichia coli (strain K12)

enzyme: molybdenum cofactor guanylyltransferase


enzyme_display_name: carbon disulfide hydrolase

organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

substrate_name: carbon disulfide

enzyme: carbon disulfide hydrolase

substrate: carbon disulfide


enzyme_display_name: inositol-1,4-bisphosphate 1-phosphatase

substrate_name: adenosine 3',5'-bisphosphate

enzyme: inositol-1,4-bisphosphate 1-phosphatase

substrate: adenosine 3',5'-bisphosphate


organism: Bos taurus

substrate_name: 1D-myo-inositol 1,4-bisphosphate

substrate: 1D-myo-inositol 1,4-bisphosphate


enzyme_display_name: pterin deaminase

organism: Unknown prokaryotic organism

substrate_name: isoxanthopterin

enzyme: pterin deaminase

substrate: isoxanthopterin


enzyme_display_name: 4-hydroxyphenylacetate decarboxylase

organism: Clostridium scatologenes

substrate_name: H+; 4-Hydroxyphenylacetate

enzyme: 4-hydroxyphenylacetate decarboxylase

substrate: H+; 4-Hydroxyphenylacetate


organism: Tractidigestivibacter scatoligenes

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: 5-dehydro-4-deoxyglucarate dehydratase

organism: Acinetobacter baylyi

sequence_source: UniProtKB:Q6FFQ1 direct REST lookup on 2026-06-15

enzyme: 5-dehydro-4-deoxyglucarate dehydratase


enzyme_display_name: isomaltose glucohydrolase

organism: Kribbella flavida

substrate_name: isomaltotriose

sequence_source: UniProtKB REST direct accession lookup, checked 2026-06-15

enzyme: isomaltose glucohydrolase

substrate: isomaltotriose


substrate_name: panose

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

proof_lines:
pH 6.0, 35°C
Raw SKiD Env: Temp=35°C, pH=6

source_databases_merged: brenda skid

substrate: panose


substrate_name: isomaltose

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup, checked 2026-06-15 and applied mutation signature W350A to reconstruct the assayed variant sequence.

substrate: isomaltose


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup, checked 2026-06-15 and applied mutation signature F290Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup, checked 2026-06-15 and applied mutation signature W354A to reconstruct the assayed variant sequence.


organism: Agrobacterium tumefaciens

substrate_name: 6-Formylpterin; H2O

substrate: 6-Formylpterin; H2O


organism: unidentified prokaryotic organism


organism: unknown prokaryotic organism

substrate_name: 2-Amino-4,7-dihydroxypteridine; H2O

substrate: 2-Amino-4,7-dihydroxypteridine; H2O


organism: Clostridium difficile


enzyme_display_name: S-methyl-5'-thioinosine phosphorylase

organism: Pseudomonas aeruginosa

substrate_name: Inosine

sequence_source: UniProtKB direct lookup Q9HZK1

enzyme: S-methyl-5'-thioinosine phosphorylase

substrate: Inosine


substrate_name: adenine

substrate: adenine


enzyme_display_name: AMP phosphorylase

organism: Thermococcus kodakarensis

substrate_name: CMP

sequence_source: UniProtKB direct lookup Q5JCX3

enzyme: AMP phosphorylase

substrate: CMP


substrate_name: UMP

substrate: UMP


substrate_name: phosphate

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

proof_lines:
pH 7.5, 85°C
pH 7.5, 85°C, cosubstrate: AMP
Raw SKiD Env: Temp=85°C, pH=7.5

substrate: phosphate


substrate_name: GMP

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

substrate: GMP


smiles: O=P(O)(O)O


organism: Halomonas elongata

sequence_source: UniProtKB direct lookup O52250

sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup O52250 and applied mutation signature D180V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup O52250 and applied mutation signature D180V/F320Y/Q325R to reconstruct the assayed variant sequence.


substrate_name: L-aspartate 4-semialdehyde

substrate: L-aspartate 4-semialdehyde


organism: Paenibacillus lautus


organism: Thermococcus kodakaraensis

substrate_name: ATP; D-Pantoate

sequence_source: UniProtKB direct lookup Q5JHF1

substrate: ATP; D-Pantoate


substrate_name: pantothenate

substrate: pantothenate


organism: Homo sapiens

substrate_name: 5-PP-InsP5; ATP

sequence_source: UniProtKB direct lookup Q6PFW1

assay_conditions_summary: pH 6.2; 310.15 K; cofactor ATP

substrate: 5-PP-InsP5; ATP


sequence_source: UniProtKB direct lookup O43314

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines: isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C

proof_lines: isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 m MKCl, at 37°C


organism: Arabidopsis thaliana

substrate_name: Sinapyl alcohol; UDPglucose

sequence_source: UniProtKB:O81498 direct REST/FASTA lookup

substrate: Sinapyl alcohol; UDPglucose


substrate_name: Coniferaldehyde

verification_status: verified

sequence_source: UniProtKB:Q9LVR1 direct REST/FASTA lookup

column_label: Table label: Table Table 2. Summary of the steady-state kinetic parameters of UGTs 72E1 and 72E2. Row: Coniferyl aldehyde. Enzyme column group: 72E2. Columns read: K m (mM) cell 0.02, k cat (s^-1) cell 1.37, k cat/K m (mM^-1 s^-1) cell 68.50. metric: kcat; raw value: 1.37; raw unit: s^-1; normalized value: 1.37 s^(-1); metric: Km; raw value: 0.02; raw unit: mM; normalized value: 0.02 mM; metric: kcat/Km; raw value: 68.50; raw unit: mM^-1 s^-1; normalized value: 68.5 s^-1 mM^-1; assay condition: Steady-state kinetic parameters of UGT72E2 (UDP-glycosyltransferase 72E2, UniProt Q9LVR1, Arabidopsis thaliana) from Table 2 of the primary article, PMID 15907484. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: 7200 columns of Table 2 row Coniferyl aldehyde: Km 0.02 mM = 0.02 mM (export unit); kcat 1.37 s^-1 = 1.37 s^(-1); kcat/Km 68.50 mM^-1 s^-1 corresponds to 68.5 s^-1 mM^-1. In the table asset the superscript minus one renders as −, so the header cell `k cat (s−1)` is the paper's k cat (s^-1) and `k cat/K m (mM−1 s−1)` is the paper's k cat/K m (mM^-1 s^-1); absent UGT720 cells render as – dashes. mM^-1 s^-1 and the export unit s^(-1)*mM^(-1) are the same unit written in either order, so no numeric conversion is applied; the paper's K m is already in mM.

raw_value_unit_evidence: Table Table 2. Summary of the steady-state kinetic parameters of UGTs 72E1 and 72E2 | column group header row of Table 2: 72E1	72E2 | metric header row: K m (mM)	k cat (s−1)	k cat/K m (mM−1 s−1)	K m (mM)	k cat (s−1)	k cat/K m (mM−1 s−1) | row: Coniferyl aldehyde	0.27	1.22	4.52	0.02	1.37	68.50 | 72E2 cells read: K m = 0.02 mM; k cat = 1.37 s^-1; k cat/K m = 68.50 mM^-1 s^-1

row_label: 72E2 | Coniferyl aldehyde

substrate: Coniferaldehyde

status: verified


substrate_name: coniferyl alcohol

column_label: Table label: Table Table 2. Summary of the steady-state kinetic parameters of UGTs 72E1 and 72E2. Row: Coniferyl alcohol. Enzyme column group: 72E2. Columns read: K m (mM) cell 0.06, k cat (s^-1) cell 3.17, k cat/K m (mM^-1 s^-1) cell 52.83. metric: kcat; raw value: 3.17; raw unit: s^-1; normalized value: 3.17 s^(-1); metric: Km; raw value: 0.06; raw unit: mM; normalized value: 0.06 mM; metric: kcat/Km; raw value: 52.83; raw unit: mM^-1 s^-1; normalized value: 52.833333333333336 s^-1 mM^-1; assay condition: Steady-state kinetic parameters of UGT72E2 (UDP-glycosyltransferase 72E2, UniProt Q9LVR1, Arabidopsis thaliana) from Table 2 of the primary article, PMID 15907484. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: 7200 columns of Table 2 row Coniferyl alcohol: Km 0.06 mM = 0.06 mM (export unit); kcat 3.17 s^-1 = 3.17 s^(-1); kcat/Km 52.83 mM^-1 s^-1 corresponds to 52.833333333333336 s^-1 mM^-1. In the table asset the superscript minus one renders as −, so the header cell `k cat (s−1)` is the paper's k cat (s^-1) and `k cat/K m (mM−1 s−1)` is the paper's k cat/K m (mM^-1 s^-1); absent UGT720 cells render as – dashes. mM^-1 s^-1 and the export unit s^(-1)*mM^(-1) are the same unit written in either order, so no numeric conversion is applied; the paper's K m is already in mM. The printed Table 2 7200 kcat/Km cell 52.83 mM^-1 s^-1 is this same row's own quotient stated at two decimal places: 3.17 s^-1 / 0.06 mM = 52.833333333333336 s^-1 mM^-1, which is the export's stored value. The quotient rounds to the printed cell at the printed cell's own precision, so the printed cell and the exported value agree and the difference is printed precision only.

raw_value_unit_evidence: Table Table 2. Summary of the steady-state kinetic parameters of UGTs 72E1 and 72E2 | column group header row of Table 2: 72E1	72E2 | metric header row: K m (mM)	k cat (s−1)	k cat/K m (mM−1 s−1)	K m (mM)	k cat (s−1)	k cat/K m (mM−1 s−1) | row: Coniferyl alcohol	–	–	–	0.06	3.17	52.83 | 72E2 cells read: K m = 0.06 mM; k cat = 3.17 s^-1; k cat/K m = 52.83 mM^-1 s^-1

row_label: 72E2 | Coniferyl alcohol

substrate: coniferyl alcohol


substrate_name: Sinapoyl aldehyde

substrate: Sinapoyl aldehyde


substrate_name: UDPglucose; Coniferaldehyde

substrate: UDPglucose; Coniferaldehyde


substrate_name: sinapyl alcohol

column_label: Table label: Table Table 2. Summary of the steady-state kinetic parameters of UGTs 72E1 and 72E2. Row: Sinapyl alcohol. Enzyme column group: 72E2. Columns read: K m (mM) cell 0.15, k cat (s^-1) cell 4.52, k cat/K m (mM^-1 s^-1) cell 30.13. metric: kcat; raw value: 4.52; raw unit: s^-1; normalized value: 4.52 s^(-1); metric: Km; raw value: 0.15; raw unit: mM; normalized value: 0.15 mM; metric: kcat/Km; raw value: 30.13; raw unit: mM^-1 s^-1; normalized value: 30.133333333333333 s^-1 mM^-1; assay condition: Steady-state kinetic parameters of UGT72E2 (UDP-glycosyltransferase 72E2, UniProt Q9LVR1, Arabidopsis thaliana) from Table 2 of the primary article, PMID 15907484. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: 7200 columns of Table 2 row Sinapyl alcohol: Km 0.15 mM = 0.15 mM (export unit); kcat 4.52 s^-1 = 4.52 s^(-1); kcat/Km 30.13 mM^-1 s^-1 corresponds to 30.133333333333333 s^-1 mM^-1. In the table asset the superscript minus one renders as −, so the header cell `k cat (s−1)` is the paper's k cat (s^-1) and `k cat/K m (mM−1 s−1)` is the paper's k cat/K m (mM^-1 s^-1); absent UGT720 cells render as – dashes. mM^-1 s^-1 and the export unit s^(-1)*mM^(-1) are the same unit written in either order, so no numeric conversion is applied; the paper's K m is already in mM. The printed Table 2 7200 kcat/Km cell 30.13 mM^-1 s^-1 is this same row's own quotient stated at two decimal places: 4.52 s^-1 / 0.15 mM = 30.133333333333333 s^-1 mM^-1, which is the export's stored value. The quotient rounds to the printed cell at the printed cell's own precision, so the printed cell and the exported value agree and the difference is printed precision only.

raw_value_unit_evidence: Table Table 2. Summary of the steady-state kinetic parameters of UGTs 72E1 and 72E2 | column group header row of Table 2: 72E1	72E2 | metric header row: K m (mM)	k cat (s−1)	k cat/K m (mM−1 s−1)	K m (mM)	k cat (s−1)	k cat/K m (mM−1 s−1) | row: Sinapyl alcohol	–	–	–	0.15	4.52	30.13 | 72E2 cells read: K m = 0.15 mM; k cat = 4.52 s^-1; k cat/K m = 30.13 mM^-1 s^-1

row_label: 72E2 | Sinapyl alcohol

substrate: sinapyl alcohol


enzyme_display_name: aklavinone 7-L-rhodosaminyltransferase

organism: Streptomyces galilaeus

substrate_name: dTDP-2-deoxyfucose; Aklavinone

enzyme: aklavinone 7-L-rhodosaminyltransferase

substrate: dTDP-2-deoxyfucose; Aklavinone


substrate_name: Aklavinone; dTDP-2-deoxyfucose

sequence_source: UniProtKB:Q9L4U6 direct REST/FASTA lookup

substrate: Aklavinone; dTDP-2-deoxyfucose


substrate_name: aklavinone

substrate: aklavinone


substrate_name: epsilon-Rhodomycinone

substrate: epsilon-Rhodomycinone


substrate_name: 5'-Methylthioinosine; Phosphate

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

sequence_source: UniProtKB:Q9HZK1 direct REST/FASTA lookup

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

source_databases_merged: sabio_rk brenda skid

substrate: 5'-Methylthioinosine; Phosphate


organism: Escherichia coli

substrate_name: GTP

sequence_source: UniProtKB REST exact accession P32173, accessed 2026-06-15

proof_lines: pH 7.2, temperature not specified in the publication, wild-type

substrate: GTP


organism: Acidianus sp.

substrate_name: H2O; Carbon disulfide

sequence_source: UniProtKB REST exact accession G0WXL9, accessed 2026-06-15

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

mutation_type: truncation

proof_lines: SABIO-RK modifier species: carbon disulfide hydrolase(Enzyme) mutant Gly199Stop

substrate: H2O; Carbon disulfide


substrate_name: Carbon disulfide; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession G0WXL9, accessed 2026-06-15 and applied mutation signature F77A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: carbon disulfide hydrolase(Enzyme) mutant Phe77Ala

substrate: Carbon disulfide; H2O


substrate_name: Carbonyl sulfide

smiles: O=C=S

substrate: Carbonyl sulfide


substrate_name: Carbon disulfide

smiles: S=C=S

substrate: Carbon disulfide


sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession G0WXL9, accessed 2026-06-15 and applied mutation signature F96S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: carbon disulfide hydrolase(Enzyme) mutant Phe96Ser


organism: Acidithiobacillus thiooxidans

substrate_name: carbonyl sulfide

sequence_source: UniProtKB REST exact accession S5FT07, accessed 2026-06-15

substrate: carbonyl sulfide


sequence_source: UniProtKB REST exact accession S5FU55, accessed 2026-06-15


organism: Sulfolobus solfataricus

sequence_source: UniProtKB REST exact accession Q97YU3, accessed 2026-06-15


organism: Bos taurus

substrate_name: 1D-myo-Inositol 1,4-bisphosphate; H2O

sequence_source: UniProtKB REST exact accession P21327, accessed 2026-06-15

substrate: 1D-myo-Inositol 1,4-bisphosphate; H2O


substrate_name: inositol 1,3,4-trisphosphate

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

substrate: inositol 1,3,4-trisphosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession P21327, accessed 2026-06-15 and applied mutation signature D54A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D54A, pH and temperature not specified in the publication


organism: Rattus norvegicus

substrate_name: inositol 1,4-bisphosphate

sequence_source: UniProtKB REST exact accession Q9Z1N4, accessed 2026-06-15

substrate: inositol 1,4-bisphosphate


organism: Kribbella flavida

substrate_name: isomaltose

sequence_source: UniProtKB REST exact accession D2PPM8, accessed 2026-06-15

substrate: isomaltose


substrate_name: panose

substrate: panose


sequence_source: UniProt REST accession lookup for O43314


substrate_name: TorD; MobA-M1-M2

substrate: TorD; MobA-M1-M2


sequence_variant_note: Resolved canonical sequence from P32173 UniProt canonical sequence with explicit mutation reconstruction from the selected BRENDA note and applied mutation signature P79L/A81T/G82S to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, temperature not specified in the publication, mutant P79L/A81T/G82S


sequence_source: UniProt REST accession lookup for P32173


substrate_name: Mo-Molybdopterin; GTP

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

proof_lines: SABIO-RK modifier species: molybdenum cofactor guanylyltransferase(Enzyme) mutant fusion of N-terminal MobA domain and C-terminal MocA domain

substrate: Mo-Molybdopterin; GTP


substrate_name: apoTorA; MobA-M1

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

substrate: apoTorA; MobA-M1


substrate_name: apoTorA; MobA-M1-M2

substrate: apoTorA; MobA-M1-M2


substrate_name: TorD; MobA-M2

substrate: TorD; MobA-M2


sequence_variant_note: Resolved canonical sequence from P32173 UniProt canonical sequence with explicit mutation reconstruction from the selected BRENDA note and applied mutation signature L12T/G14A/P79L/A81T/G82S to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, temperature not specified in the publication, mutant L12T/G14A/P79L/A81T/G82S


substrate_name: PaoD; N-MobA-C-MocA

substrate: PaoD; N-MobA-C-MocA


substrate_name: Mo-Molybdopterin; CTP

proof_lines: SABIO-RK modifier species: molybdenum cofactor guanylyltransferase(Enzyme) mutant MobA with M1 and M2 motifs of MocA

proof_lines: SABIO-RK modifier species: molybdenum cofactor guanylyltransferase(Enzyme) mutant MobA with M1 motif of MocA

proof_lines: SABIO-RK modifier species: molybdenum cofactor guanylyltransferase(Enzyme) mutant MobA with M2 motif of MocA

substrate: Mo-Molybdopterin; CTP


substrate_name: N-MobA-C-MocA; GTP

substrate: N-MobA-C-MocA; GTP


substrate_name: GTP

sequence_variant_note: Resolved canonical sequence from P32173 UniProt canonical sequence with explicit mutation reconstruction from the selected BRENDA note and applied mutation signature L12T/G14A to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, temperature not specified in the publication, mutant L12T/G14A

substrate: GTP


enzyme_display_name: Pro-Pro endopeptidase

organism: Clostridioides difficile

substrate_name: Dabcyl-Lys-EVNPPPPD-EdansGlu

sequence_source: UniProtKB reviewed entry Q183R7, fetched 2026-06-15

enzyme: Pro-Pro endopeptidase

substrate: Dabcyl-Lys-EVNPPPPD-EdansGlu


organism: Paenibacillus alvei

substrate_name: YPSSKPLPPVPPVQPLPPVPKLETS; H2O

sequence_source: UniProtKB reviewed entry K4ZRC1, fetched 2026-06-15

substrate: YPSSKPLPPVPPVQPLPPVPKLETS; H2O


substrate_name: H2O; YPSSKPLPPVPPVQPLPPVPKLETS

sequence_source: Reconstructed from UniProtKB K4ZRC1 canonical sequence plus UniProtKB mutagenesis feature SERV112-115GGST supported by PMID 29794027

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

proof_lines: SABIO-RK modifier species: Pro-Pro endopeptidase(Enzyme) mutant PPEP-2-GGST

substrate: H2O; YPSSKPLPPVPPVQPLPPVPKLETS


substrate_name: YPSSKPLPPVPPVQPLPPVPKLETS

proof_lines: wild type enzyme PPEP-2, at pH 7.0 and 37°C

proof_lines: recombinant enzyme PPEP-2GGST, where residues 112-115 of the wild type enzyme (SERV) are replaced by residues 91-94 of Pro-Pro endopeptidase-1 (GGST), at pH 7.0 and 37°C

substrate: YPSSKPLPPVPPVQPLPPVPKLETS


enzyme_display_name: isoleucine N-monooxygenase

organism: Lotus japonicus

substrate_name: isoleucine

proof_lines: kcat is 120 min(-1) with isoleucine as substrate (PubMed:15122013). kcat is 44 min(-1) with valine as substrate (PubMed:15122013).

enzyme: isoleucine N-monooxygenase

substrate: isoleucine


proof_lines: kcat is 220 min(-1) with isoleucine as substrate (PubMed:15122013). kcat is 50 min(-1) with valine as substrate (PubMed:15122013).


organism: Manihot esculenta

substrate_name: valine

proof_lines: kcat is 2.3 min(-1) with isoleucine as substrate (PubMed:10636899). kcat is 4.3 min(-1) with valine as substrate (PubMed:10636899).

substrate: valine


enzyme_display_name: tryptophan 7-halogenase

organism: Kutzneria sp. (strain 744)

substrate_name: Unknown

proof_lines: kcat is 0.19 min(-1) with L-Trp as substrate (PubMed:18828589). kcat is 0.07 min(-1) with 6-chloro-L-tryptophan as substrate (PubMed:18828589).

enzyme: tryptophan 7-halogenase

substrate: Unknown


organism: Lentzea aerocolonigenes

substrate_name: tryptophan (with FAD)

assay_conditions_summary: cofactor FAD

substrate: tryptophan (with FAD)


enzyme_display_name: nicotinate N-methyltransferase

substrate_name: nicotinate

proof_lines: kcat is 3.52 sec(-1) with nicotinate as substrate (PubMed:28533213). kcat is 3.01 sec(-1) with S-adenosyl-L-methionine as substrate (PubMed:28533213).

enzyme: nicotinate N-methyltransferase

substrate: nicotinate


organism: Glycine max

proof_lines: kcat is 4.81 sec(-1) with nicotinate as substrate (PubMed:28533213). kcat is 4.14 sec(-1) with S-adenosyl-L-methionine as substrate (PubMed:28533213).


organism: Oryza sativa subsp. japonica

proof_lines: kcat is 2.25 sec(-1) with nicotinate as substrate (PubMed:28533213). kcat is 2.07 sec(-1) with S-adenosyl-L-methionine as substrate (PubMed:28533213).


substrate_name: aklavinone (with dTDP-4-amino-2-deoxyrhamnose as sugar donor)

proof_lines: kcat is 9.6 sec(-1) for glycosyltransferase activity with aklavinone as sugar acceptor and TDP-L-rhodosamine as sugar donor. kcat is 0.05 sec(-1) for glycosyltransferase activity without AknT and with aklavinone as sugar acceptor and TDP-L-


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: inosine (at 25 degrees Celsius and pH 7.5)

proof_lines: kcat is 1.7 sec(-1) with inosine as substrate (PubMed:14982926, PubMed:24416224). kcat is 2.63 sec(-1) with inosine as substrate (PubMed:29440412). kcat is 1.1 sec(-1) with guanosine as substrate (PubMed:19575810). kcat is 1.5 sec(-1) with

proof_lines: kcat is 0.34 sec(-1) with inosine as substrate (PubMed:11707439). kcat is 0.14 sec(-1) with guanosine as substrate (PubMed:11707439). kcat is 0.64 sec(-1) with 2'-deoxyinosine as substrate (PubMed:11707439). kcat is 0.2 sec(-1) with 2'-deox


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

proof_lines: kcat is 4.8 sec(-1) with S-methyl-5'-thioinosine as substrate (PubMed:21197954). kcat is 0.57 sec(-1) with inosine as substrate (PubMed:21197954). kcat is 0.0549 sec(-1) with adenosine as substrate (PubMed:21197954).


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

substrate_name: CMP (in the presence of AMP, at 85 degrees Celsius)

proof_lines: kcat is 39.1 sec(-1), 15.0 sec(-1), 10.5 sec(-1) and 2.7 sec(-1), with CMP, AMP, UMP, and GMP as substrate, respectively (at 85 degrees Celsius). KM for AMP was not determined because the reaction does not follow Michaelis-Menten kinetics.


enzyme_display_name: N-acetylneuraminate synthase

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

substrate_name: ManNAc

enzyme: N-acetylneuraminate synthase

substrate: ManNAc


organism: Homo sapiens

proof_lines: The catalytic efficiency is 80 folds higher for 5-PP-InsP5 (InsP7) compared to InsP6.


enzyme_display_name: 3-sulfinopropanoyl-CoA desulfinase

organism: Advenella mimigardefordensis (strain DSM 17166 / LMG 22922 / DPN7)

enzyme: 3-sulfinopropanoyl-CoA desulfinase


organism: Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)


organism: Paraburkholderia xenovorans (strain LB400)


organism: Variovorax paradoxus


organism: Acidianus sp. (strain A1-3)

substrate_name: carbon disulfide

proof_lines: kcat is 952 sec(-1) with carbon disulfide as substrate. kcat is 1800 sec(-1) with the intermediate carbonyl sulfide as substrate.

substrate: carbon disulfide


organism: Acidithiobacillus thiooxidans

proof_lines: kcat is 780 sec(-1) with carbon disulfide as substrate. kcat is 814 sec(-1) with the intermediate carbonyl sulfide as substrate.


proof_lines: kcat is 3000 sec(-1) with carbon disulfide as substrate. kcat is 22400 sec(-1) with the intermediate carbonyl sulfide as substrate.


enzyme_display_name: 3-hydroxyisobutyryl-CoA hydrolase

organism: Arabidopsis thaliana

proof_lines: Can also use 3-hydroxy-3-phenoylpropionoyl-CoA and p-coumaroyl-CoA as substrates, but not benzoyl-CoA.

enzyme: 3-hydroxyisobutyryl-CoA hydrolase


substrate_name: 1D-myo-inositol 1,4-bisphosphate

proof_lines: KM for adenosine 3',5'-bisphosphate is between 2 and 10 uM.

substrate: 1D-myo-inositol 1,4-bisphosphate


proof_lines: KM for adenosine 3',5'-bisphosphate is below 1 uM.


substrate_name: Nicotinate; S-Adenosyl-L-methionine

sequence_source: UniProtKB:I1M2U5; sequence_version=1

substrate: Nicotinate; S-Adenosyl-L-methionine


organism: Oryza sativa

substrate_name: S-Adenosyl-L-methionine; Nicotinate

sequence_source: UniProtKB:Q6K9X3; sequence_version=1

substrate: S-Adenosyl-L-methionine; Nicotinate


organism: Advenella mimigardefordensis

sequence_source: UniProtKB:K4L7X3; sequence_version=1

sequence_variant_note: Resolved canonical sequence from UniProtKB:K4L7X3; sequence_version=1 and applied mutation signature Q246E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA

proof_lines: recombinant His6-tagged mutant Q246E, pH 7.4, 30°C


proof_lines: recombinant His6-tagged wild-type enzyme, pH 7.4, 30°C


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Clostridioides difficile

sequence_source: UniProtKB:Q183R7; sequence_version=1


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q183R7; sequence_version=1 and applied mutation signature E184A to reconstruct the assayed variant sequence.


organism: Mus musculus

substrate_name: adenosine 3',5'-bisphosphate (PAP)

proof_lines: The different methodology used for determination of the hydrolysis of inositol-1,4-bisphosphate might account for the discrepancy obtained with protein homologs from human and rat, which show much more efficiency with this substrate.

substrate: adenosine 3',5'-bisphosphate (PAP)


organism: Rattus norvegicus

substrate_name: 3'-phosphoadenylyl sulfate

proof_lines: KM for adenosine 3',5'-bisphosphate is below 2 uM.

substrate: 3'-phosphoadenylyl sulfate


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

proof_lines: KM for adenosine 3',5'-bisphosphate is below 10 uM.


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

substrate_name: panose

proof_lines: kcat is 11.4 sec(-1) for isomaltose as substrate. kcat is 1.17 sec(-1) for panose as substrate. kcat is 1.07 sec(-1) for isomaltotriose as substrate.

substrate: panose


organism: Clostridioides difficile (strain 630)

proof_lines: kcat is 19 sec(-1) with synthetic FRET peptide DabcylLys-EVNPPPPD-EdansGlu as substrate.


organism: Paenibacillus alvei (strain ATCC 6344 / DSM 29 / NBRC 3343 / NCIMB 9371 / NCTC 6352)

substrate_name: a FRET peptide containing PLPPVP

proof_lines: kcat is 8 sec(-1) with a FRET peptide containing PLPPVP as substrate. kcat is 3 sec(-1) with a FRET peptide containing VLPPVP as substrate.

substrate: a FRET peptide containing PLPPVP


enzyme_display_name: guanidinobutyrase

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

enzyme: guanidinobutyrase


organism: Rhizobium rhizogenes (strain K84 / ATCC BAA-868)

substrate_name: formylpterin

proof_lines: kcat is 64 sec(-1) with formylpterin as substrate. kcat is 110 sec(-1) with pterin-6-carboxylate as substrate. kcat is 48 sec(-1) with pterin-7-carboxylate as substrate. kcat is 131 sec(-1) with pterin as substrate. kcat is 28 sec(-1) with

substrate: formylpterin


proof_lines: kcat is 110 sec(-1) for the decarboxylation of 4-hydroxyphenylacetate. kcat is 65 sec(-1) for the decarboxylation of 3,4-hydroxyphenylacetate.


organism: Clostridium scatologenes

proof_lines: kcat is 135 sec(-1) for the decarboxylation of 4-hydroxyphenylacetate. kcat is 67 sec(-1) for the decarboxylation of 3,4-hydroxyphenylacetate.


organism: Lotus japonicus

substrate_name: NADPH; O2; L-Isoleucine; H+

sequence_source: UniProtKB reviewed accession Q6J541

assay_conditions_summary: pH 7.5; 301.15 K; cofactor NADPH

substrate: NADPH; O2; L-Isoleucine; H+


substrate_name: L-Isoleucine

substrate: L-Isoleucine


substrate_name: O2; H+; NADPH; L-Isoleucine

sequence_source: UniProtKB reviewed accession Q6J540

substrate: O2; H+; NADPH; L-Isoleucine


substrate_name: L-Valine

substrate: L-Valine


organism: Kutzneria sp. 744

sequence_source: UniProtKB reviewed accession A8CF75

assay_conditions_summary: pH 7

proof_lines: about, pH 7.0, temperature not specified in the publication, recombinant His-tagged enzyme


organism: Lentzea aerocolonigenes

substrate_name: L-tryptophan

sequence_source: UniProtKB reviewed accession Q8KHZ8

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

substrate: L-tryptophan


organism: Pseudomonas fluorescens

substrate_name: O2; Cl-; FADH2; L-Tryptophan; H+

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P95480 with row-specific mutation reconstruction and applied mutation signature S347A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tryptophan 7-halogenase(Enzyme) mutant S347A

substrate: O2; Cl-; FADH2; L-Tryptophan; H+


substrate_name: FADH2; O2; Cl-; H+; L-Tryptophan

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P95480 with row-specific mutation reconstruction and applied mutation signature W272A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tryptophan 7-halogenase(Enzyme) mutant W272A

substrate: FADH2; O2; Cl-; H+; L-Tryptophan


substrate_name: L-Tryptophan; H+; O2; Cl-; FADH2

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P95480 with row-specific mutation reconstruction and applied mutation signature W272F/W274F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tryptophan 7-halogenase(Enzyme) mutant W272F_W274F

substrate: L-Tryptophan; H+; O2; Cl-; FADH2


substrate_name: FADH2; H+; Cl-; O2; L-Tryptophan

sequence_source: UniProtKB reviewed accession P95480

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

substrate: FADH2; H+; Cl-; O2; L-Tryptophan


substrate_name: L-Tryptophan; FADH2; Cl-; O2; H+

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P95480 with row-specific mutation reconstruction and applied mutation signature W274F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tryptophan 7-halogenase(Enzyme) mutant W274F

substrate: L-Tryptophan; FADH2; Cl-; O2; H+


substrate_name: FADH2; L-Tryptophan; H+; O2; Cl-

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P95480 with row-specific mutation reconstruction and applied mutation signature W272F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tryptophan 7-halogenase(Enzyme) mutant W272F

substrate: FADH2; L-Tryptophan; H+; O2; Cl-


enzyme_display_name: carminomycin 4-O-methyltransferase

organism: Streptomyces peucetius

sequence_source: UniProtKB reviewed accession Q06528

enzyme: carminomycin 4-O-methyltransferase


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


proof_lines:
pH 8.0, 37°C
Raw SKiD Env: Temp=37°C, pH=8


substrate_name: tryptophan

sequence_source: UniProtKB Q8KHZ8 official REST lookup on 2026-06-15

proof_lines: ranges from 0.02 s-1 to 0.05 s-1 for different preparations, 25°C

substrate: tryptophan


sequence_variant_note: Resolved canonical sequence from UniProtKB P95480 official REST lookup on 2026-06-15 plus direct 1-indexed H101A substitution reconstruction and applied mutation signature H101A to reconstruct the assayed variant sequence.

proof_lines: His-tagged recombinant mutant enzyme H101A, at 30°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P95480 official REST lookup on 2026-06-15 plus direct 1-indexed W455A substitution reconstruction and applied mutation signature W455A to reconstruct the assayed variant sequence.

proof_lines: His-tagged recombinant mutant enzyme W455A, at 30°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P95480 official REST lookup on 2026-06-15 plus direct 1-indexed F103A substitution reconstruction and applied mutation signature F103A to reconstruct the assayed variant sequence.

proof_lines: His-tagged recombinant mutant enzyme F103A, at 30°C, pH not specified in the publication


sequence_source: UniProtKB P95480 official REST lookup on 2026-06-15

proof_lines: His-tagged recombinant wild type enzyme, at 30°C, pH not specified in the publication


proof_lines: pH 7.2, 30°C, in vitro two-component system of enzyme and flavin reductase to provide FADH2


sequence_source: UniProtKB Q06528 official REST lookup on 2026-06-15


organism: Lathyrus oleraceus

substrate_name: nicotinate

substrate: nicotinate


organism: Lemna aequinoctialis


enzyme_display_name: coniferyl-alcohol glucosyltransferase

organism: Forsythia ovata

substrate_name: UDPglucose

enzyme: coniferyl-alcohol glucosyltransferase

substrate: UDPglucose


substrate_name: tryptophan (with FAD at pH 7.2 and 30 degrees Celsius)

verification_status: corrected

assay_conditions_summary: pH 7.2; cofactor FAD

status: corrected


organism: Picea abies

substrate_name: coniferyl alcohol

substrate: coniferyl alcohol


organism: Pinus strobus

substrate_name: sinapyl alcohol

substrate: sinapyl alcohol


organism: Rosa sp.


organism: Streptomyces galilaeus

substrate_name: dTDP-beta-L-rhodosamine

sequence_source: UniProtKB REST reviewed accession Q9L4U6

proof_lines: with dTDP-L-2-deoxyfucose as cosubstrate, in 75 mM Tris (pH 7.5), 10 mM MgCl2, at 25°C

proof_lines: with aklavinone as cosubstrate, in 75 mM Tris (pH 7.5), 10 mM MgCl2, at 25°C

substrate: dTDP-beta-L-rhodosamine


organism: Acinetobacter baumannii

substrate_name: L-2,4-diaminobutyric acid

substrate: L-2,4-diaminobutyric acid


organism: Rattus norvegicus

substrate_name: diphosphoinositol pentakisphosphate

assay_conditions_summary: pH 6.8; 310.15 K; cofactor ATP

substrate: diphosphoinositol pentakisphosphate


organism: Advenella mimigardefordensis

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: pH 7.4, 37°C, with a Vmax of 4.19 micromol/min*mg


organism: Cupriavidus necator

proof_lines: pH 7.4, 37°C, with a Vmax of 6.1 micromol/min*mg


organism: Paraburkholderia xenovorans

proof_lines: pH 7.4, 37°C, with a Vmax of 1.58 micromol/min*mg


organism: Variovorax paradoxus

proof_lines: pH 7.4, 37°C, with a Vmax of 3.47 micromol/min*mg


enzyme_display_name: carbon disulfide hydrolase

organism: Acidianus sp.

substrate_name: carbon disulfide

proof_lines: pH and temperature not specified in the publication, mutant enzyme G199stop

enzyme: carbon disulfide hydrolase

substrate: carbon disulfide


sequence_source: UniProtKB REST reviewed accession G0WXL9

proof_lines: pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:G0WXL9 plus row-specific F77A reconstruction and applied mutation signature F77A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme F77A


sequence_variant_note: Resolved canonical sequence from UniProtKB:G0WXL9 plus row-specific F96S reconstruction and applied mutation signature F96S to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme F96S


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


enzyme_display_name: inositol-1,4-bisphosphate 1-phosphatase

organism: Bos taurus

substrate_name: inositol 1,4-bisphosphate

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

enzyme: inositol-1,4-bisphosphate 1-phosphatase

substrate: inositol 1,4-bisphosphate


substrate_name: H2O; 1D-myo-Inositol 1,4-bisphosphate

substrate: H2O; 1D-myo-Inositol 1,4-bisphosphate


enzyme_display_name: pterin deaminase

organism: Priestia megaterium

enzyme: pterin deaminase


organism: unknown prokaryotic organism

substrate_name: 2-Amino-4,7-dihydroxypteridine; H2O

substrate: 2-Amino-4,7-dihydroxypteridine; H2O


enzyme_display_name: 4-hydroxyphenylacetate decarboxylase

organism: Clostridioides difficile

proof_lines: in 100 mM Tris-HCl, pH 7.5, 40 mM NaCl, 5 mM MgCl2, 5 mM (NH4)2SO4, 5 mM cysteine, 25 mM substrate, and 5 mM dithiothreitol, at 30°C

enzyme: 4-hydroxyphenylacetate decarboxylase


organism: Clostridium scatologenes


organism: Streptomyces sp. (strain C5)

substrate_name: carminomycin

sequence_source: source_record; UniProt Q55216 direct sequence check

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

substrate: carminomycin


organism: Streptomyces peucetius


organism: Arabidopsis thaliana


organism: Bacillus subtilis


enzyme_display_name: benzoyl-CoA reductase

organism: Pseudomonas sp.

substrate_name: benzoyl-CoA

enzyme: benzoyl-CoA reductase

substrate: benzoyl-CoA


organism: Thauera aromatica

assay_conditions_summary: cofactor ATP


sequence_source: UniProtKB reviewed accession P27620 FASTA and metadata; TAGA_BACSU, Bacillus subtilis strain 168 TagA, EC 2.4.1.187, with PMID 16953575 evidence.

proof_lines:
apparent Kcat at 600 microM UDP-ManNAc
apparent Km at 600 microM UDP-ManNAc


organism: Escherichia coli

substrate_name: 7,8-dihydroneopterin 3'-triphosphate

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

substrate: 7,8-dihydroneopterin 3'-triphosphate


organism: Bacillus subtilis (strain 168)

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

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


enzyme_display_name: sucrose-phosphate phosphatase

organism: Unknown

substrate_name: sucrose 6-phosphate

enzyme: sucrose-phosphate phosphatase

substrate: sucrose 6-phosphate


organism: Daucus carota

substrate_name: sucrose phosphate

substrate: sucrose phosphate


organism: Lathyrus oleraceus


organism: Methylobacillus flagellatus


organism: Oryza sativa


organism: Spinacia oleracea

substrate_name: Sucrose 6-phosphate; H2O

substrate: Sucrose 6-phosphate; H2O


organism: Synechocystis sp.

substrate_name: Unknown

ki_unit: mM

substrate: Unknown


substrate_name: Benzoyl-CoA; H2O; ATP; Reduced acceptor

substrate: Benzoyl-CoA; H2O; ATP; Reduced acceptor


substrate_name: ATP

assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: Benzoyl-CoA

assay_conditions_summary: pH 7.3; 310.15 K; cofactor CoA

substrate: Benzoyl-CoA


substrate_name: Benzoyl-CoA; Reduced acceptor; ATP

substrate: Benzoyl-CoA; Reduced acceptor; ATP


sequence_source: UniProtKB:Q9CA40 direct accession lookup on 2026-06-15

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


sequence_source: UniProtKB:P0AFC0 direct accession lookup on 2026-06-15

proof_lines:
pH 8.5, 37°C
Raw SKiD Env: Temp=37°C, pH=8.5
Raw SKiD Env: Temp=42°C, pH=8.5


substrate_name: dATP

substrate: dATP


organism: Lactococcus lactis

sequence_source: UniProtKB:D8KIT5 direct accession lookup on 2026-06-15


enzyme_display_name: acetate CoA-transferase

substrate_name: Acetoacetyl-CoA; Acetate

assay_conditions_summary: cofactor CoA

enzyme: acetate CoA-transferase

substrate: Acetoacetyl-CoA; Acetate


enzyme_display_name: hydroquinone glucosyltransferase

enzyme: hydroquinone glucosyltransferase


organism: Escherichia coli (strain K12)

substrate_name: acetyl-CoA (for acetoacetyl-CoA formation)


substrate: acetyl-CoA (for acetoacetyl-CoA formation)


organism: Oryza sativa subsp. japonica

substrate_name: sucrose 6(F)-phosphate

substrate: sucrose 6(F)-phosphate


organism: Zea mays


organism: Arabidopsis thaliana

substrate_name: NADH (in the presence of 5 mM of manganese)

assay_conditions_summary: cofactor NADH


substrate_name: dihydroneopterin triphosphate

substrate: dihydroneopterin triphosphate


substrate_name: 3,4-Dichlorophenol; UDPglucose

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

proof_lines: SABIO-RK modifier species: hydroquinone glucosyltransferase(Enzyme) mutant Y315F N-terminal streptactin-tagged

substrate: 3,4-Dichlorophenol; UDPglucose


proof_lines: SABIO-RK modifier species: hydroquinone glucosyltransferase(Enzyme) mutant H19Q N-terminal streptactin-tagged


proof_lines: SABIO-RK modifier species: hydroquinone glucosyltransferase(Enzyme) mutant N312D-Y315F N-terminal streptactin-tagged


organism: Brassica napus

proof_lines: SABIO-RK modifier species: hydroquinone glucosyltransferase(Enzyme) mutant F317Y N-terminal streptactin-tagged


substrate_name: UDPglucose; 3,4-Dichlorophenol

proof_lines: SABIO-RK modifier species: hydroquinone glucosyltransferase(Enzyme) mutant D314N-F317Y N-terminal streptactin-tagged

substrate: UDPglucose; 3,4-Dichlorophenol


organism: Rauvolfia serpentina

substrate_name: hydroquinone

substrate: hydroquinone


organism: Acetobacter aceti

substrate_name: acetyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot:B3EY95:direct_reconstructed_variant and applied mutation signature N347A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines: mutant enzyme N347A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C

substrate: acetyl-CoA


substrate_name: acetate

column_label: AarC acetate saturation, decoded plain-numeral measurement-bound row: kcat = 290 s^-1; Km = 110 mM; kcat/Km = 2.6 x 10^3 M^-1 s^-1; Ki = 1600 mM. The article prints these four constants for the one acetate-saturation measurement in running prose, and prints no kcat column and no Km column for any enzyme form anywhere in the article body.

normalized_value_unit_evidence: kcat: printed value 290 s^-1; the printed unit is already s^-1, so no unit conversion applies and the exported value is 290.0 s^(-1). Km: printed value 110 mM; the printed unit is already mM, so no unit conversion applies and the exported value is 110.0 mM. kcat/Km: printed value 2.6 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.6 x 10^3 x 0.001 = 2.6 s^-1 mM^-1; the export row holds no kcat_over_km value, so this converted figure is kept as typed provenance only and no ratio metric is written.

raw_value_unit_evidence: AarC acetate saturation, decoded plain-numeral measurement-bound row: kcat = 290 s^-1; Km = 110 mM; printed kcat/Km = 2.6 x 10^3 M^-1 s^-1; printed Ki = 1600 mM.

row_label: AarC acetate saturation, decoded plain-numeral measurement-bound row, substrate acetate, enzyme form wild-type AarC

table_label: Results, 'Protein Production, Isolation, and Biophysical Characterization', journal page 8424: the AarC acetate-saturation steady-state constants stated in running prose

substrate: acetate


substrate_name: succinate

proof_lines: mutant enzyme R228E, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C

substrate: succinate


substrate_name: succinyl-CoA

proof_lines: mutant enzyme E435D, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C

substrate: succinyl-CoA


proof_lines: mutant enzyme S71A, in 50 mM potassium phosphate (pH 8.0), 100 mM potassium chloride, at 30°C


organism: Anabaena sp.

substrate_name: sucrose 6-phosphate

substrate: sucrose 6-phosphate


sequence_source: UniProtKB reviewed direct accession lookup Q9SJ66


sequence_source: UniProtKB reviewed direct accession lookup Q93XN8


substrate_name: Sucrose 6-phosphate; H2O

sequence_source: UniProtKB reviewed direct accession lookup Q6YXW6

substrate: Sucrose 6-phosphate; H2O


organism: Saccharum officinarum

sequence_source: UniProtKB TrEMBL direct accession lookup Q4FCW1


enzyme_display_name: D(-)-tartrate dehydratase

organism: Bradyrhizobium diazoefficiens

substrate_name: D-Tartrate

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q89FH0 canonical FASTA plus selected mutation_signature H322Q; residue check performed 2026-06-15 and applied mutation signature H322Q to reconstruct the assayed variant sequence.

enzyme: D(-)-tartrate dehydratase

substrate: D-Tartrate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q89FH0 canonical FASTA plus selected mutation_signature K184R; residue check performed 2026-06-15 and applied mutation signature K184R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q89FH0 canonical FASTA plus selected mutation_signature H322N; residue check performed 2026-06-15 and applied mutation signature H322N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D(-)-tartrate dehydratase(Enzyme) mutant H322N


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q89FH0 canonical FASTA plus selected mutation_signature H322A; residue check performed 2026-06-15 and applied mutation signature H322A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D(-)-tartrate dehydratase(Enzyme) mutant H322A


substrate_name: D-tartrate

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

substrate: D-tartrate


organism: Bradyrhizobium japonicum

substrate_name: (S,S)-Tartrate

sequence_source: RCSB 2DW7 / UniProt Q89FH0

sequence_variant_note: Resolved canonical sequence from RCSB 2DW7 / UniProt Q89FH0 and applied mutation signature H322Q to reconstruct the assayed variant sequence.

substrate: (S,S)-Tartrate


sequence_variant_note: Resolved canonical sequence from RCSB 2DW7 / UniProt Q89FH0 and applied mutation signature H322A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB 2DW7 / UniProt Q89FH0 and applied mutation signature H322N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB 2DW7 / UniProt Q89FH0 and applied mutation signature K184R to reconstruct the assayed variant sequence.


organism: Cereibacter sphaeroides


organism: Pseudomonas sp.

proof_lines:
strain Ch
strain G2


sequence_variant_note: Resolved canonical sequence from UniProtKB Q89FH0 direct lookup plus selected mutation_signature H322N reconstruction and applied mutation signature H322N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q89FH0 direct lookup plus selected mutation_signature H322A reconstruction and applied mutation signature H322A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q89FH0 direct lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB Q89FH0 direct lookup plus selected mutation_signature K184R reconstruction and applied mutation signature K184R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D(-)-tartrate dehydratase(Enzyme) mutant K184R


sequence_variant_note: Resolved canonical sequence from UniProtKB Q89FH0 direct lookup plus selected mutation_signature H322Q reconstruction and applied mutation signature H322Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D(-)-tartrate dehydratase(Enzyme) mutant H322Q


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


organism: Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110)

sequence_source: source_record; direct UniProt Q89FH0 check


substrate_name: Vanillin

sequence_source: UniProtKB/Swiss-Prot Q9AR73 (HQGT_RAUSE), linked to PMID 11937332 and DOI 10.1016/S0968-0896(02)00029-9

substrate: Vanillin


enzyme_display_name: 5-dehydro-4-deoxyglucarate dehydratase

organism: Acinetobacter baylyi

sequence_source: UniProtKB REST direct lookup on 2026-06-15 for accession Q6FFQ1

enzyme: 5-dehydro-4-deoxyglucarate dehydratase


organism: Agrobacterium fabrum

sequence_source: UniProtKB REST direct lookup on 2026-06-15 for accession Q8UB77

proof_lines:
pH 7.5, 22°C
Raw SKiD Env: Temp=22°C, pH=7.5


organism: Comamonas testosteroni

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


assay_conditions_summary: pH 7; 310.15 K; buffer 25 mM potassium phosphate

proof_lines: in 25 mM potassium phosphate buffer, at pH 7.0 and 37°C


organism: Polaromonas naphthalenivorans

sequence_source: UniProtKB REST direct lookup on 2026-06-15 for accession A1VMN2


organism: Polaromonas naphthalenivorans CJ2


enzyme_display_name: acetylornithine transaminase

organism: Burkholderia cepacia

substrate_name: L-ornithine

enzyme: acetylornithine transaminase

substrate: L-ornithine


organism: Escherichia coli

proof_lines: cosubstrate 2-oxoglutarate, arginine inducible and arginine repressible enzyme


organism: Klebsiella aerogenes


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Escherichia coli (strain K12)

substrate_name: N-acetylornithine

substrate: N-acetylornithine


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

substrate_name: N(2)-succinyl-L-ornithine (at 15 mM 2-ketoglutarate and pH 9.0)

assay_conditions_summary: pH 9


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: acetylornithine

substrate: acetylornithine


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

substrate_name: N-acetylornithine (at pH 9.5 and 25 degrees Celsius)


enzyme_display_name: hydroxyisourate hydrolase

organism: Glycine max

proof_lines: pH 7.5, 37°C, recombinant enzyme lacking the signal peptide

enzyme: hydroxyisourate hydrolase


enzyme_display_name: 2-dehydro-3-deoxyglucarate aldolase

enzyme: 2-dehydro-3-deoxyglucarate aldolase


organism: Picrophilus oshimae

assay_conditions_summary: pH 6.2; 333.15 K; buffer 50 mM sodium phosphate

proof_lines: at 60°C in 50 mM sodium phosphate buffer (pH 6.2)


enzyme_display_name: 2-hydroxyethylphosphonate dioxygenase

organism: Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494)

enzyme: 2-hydroxyethylphosphonate dioxygenase


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

proof_lines: kcat is 2.31 sec(-1) with N-acetylornithine as substrate. kcat is 0.16 sec(-1) with ornithine as substrate. kcat is 0.14 sec(-1) with gamma-aminobutyric acid as substrate. kcat is 2.50 sec(-1) with 2-oxoglutarate as substrate (in the presen


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

substrate_name: KDG (at 70 degrees Celsius and pH 7.2)

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: kcat is 3.8 sec(-1) for ATP, 5 sec(-1) for KDG and 5.4 sec(-1) for KDGal (at 60 degrees Celsius and pH 7.5).

substrate: KDG (at 70 degrees Celsius and pH 7.2)


substrate_name: 5-Hydroxyisourate; H2O

sequence_source: UniProt Q8S3J3 chain 32-560; signal peptide 1-31 removed

substrate: 5-Hydroxyisourate; H2O


organism: Klebsiella pneumoniae

sequence_variant_note: Resolved canonical sequence from UniProt A6T926 canonical sequence with R41K reconstructed after residue check and applied mutation signature R41K to reconstruct the assayed variant sequence.

proof_lines: mutant R41K, pH 7.6, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt A6T926 canonical sequence with S108A reconstructed after residue check and applied mutation signature S108A to reconstruct the assayed variant sequence.

proof_lines: mutant S108A, pH 7.6, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt A6T926 canonical sequence with H7N reconstructed after residue check and applied mutation signature H7N to reconstruct the assayed variant sequence.

proof_lines: mutant H7N, pH 7.6, temperature not specified in the publication


sequence_source: UniProt A6T926 canonical sequence

proof_lines: wild-type, pH 7.6, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt A6T926 canonical sequence with H92N reconstructed after residue check and applied mutation signature H92N to reconstruct the assayed variant sequence.

proof_lines: mutant H92N, pH 7.6, temperature not specified in the publication


sequence_source: UniProt P23522 canonical chain 1-256

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

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 KDGlucA; column kcat (s^-1) = 27.3; column Km (uM) = 65; column kcat/Km (M^-1 s^-1) = 4.2 x 10^5. captured primary segment: KDGlucA | kcat 27.3 ± 0.4 s^-1 | Km 65 ± 3 uM | kcat/Km 4.2 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 27.3 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 27.3 s^(-1); the exported value is 27.3 s^(-1). Km: printed Table 1 cell 65 uM; 1 uM is 1/1000 mM, so 65 / 1000 = 0.065 mM; the exported value is 0.065 mM. kcat/Km: printed Table 1 cell 4.2 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.2 x 10^5 / 1000 = 420.0 s^(-1)*mM^(-1); the exported value is 420.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row KDGlucA: kcat = 27.3 s^-1; Km = 65 uM; printed kcat/Km = 4.2 x 10^5 M^-1 s^-1.

row_label: Table 1, row KDGlucA


proof_lines:
data for Mg2+-activated YfaU
data for Ni2+-activated YfaU
Raw SKiD Env: Temp=-----, pH=-----


organism: Streptomyces viridochromogenes

sequence_source: UniProtKB:Q5IW40 direct accession check; reviewed 2026-06-15

smiles: O=P(O)(O)CCO


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5IW40 direct accession check; reviewed 2026-06-15 and applied mutation signature R90K to reconstruct the assayed variant sequence.


organism: Saccharomyces cerevisiae

substrate_name: 2-Oxoglutarate; N2-Acetyl-L-ornithine

sequence_source: UniProtKB:P18544 direct accession check; reviewed 2026-06-15

substrate: 2-Oxoglutarate; N2-Acetyl-L-ornithine


organism: Salmonella typhimurium

sequence_source: UniProtKB:P40732 direct accession check; reviewed 2026-06-15


substrate_name: L-Ornithine

substrate: L-Ornithine


organism: Saccharolobus solfataricus

substrate_name: ATP

sequence_source: UniProtKB:Q97U29 direct accession check; reviewed 2026-06-15

assay_conditions_summary: pH 7.5; 333.15 K; cofactor ATP

substrate: ATP


proof_lines:
pH 7.5, 60°C
pH 7.2, 60°C
Raw SKiD Env: Temp=60°C, pH=7.5


sequence_source: UniProtKB:Q8S3J3 direct accession check; reviewed 2026-06-15


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

substrate_name: KDG

substrate: KDG


substrate_name: hydroxyisourate

substrate: hydroxyisourate


enzyme_display_name: 2-oxopent-4-enoate hydratase

organism: Burkholderia xenovorans LB400

smiles: O=C([O-])C(O)=CC=CCl

enzyme: 2-oxopent-4-enoate hydratase


substrate_name: H2O; 2-Hydroxy-2,4-pentadienoate

substrate: H2O; 2-Hydroxy-2,4-pentadienoate


organism: Escherichia coli

substrate_name: 2-Hydroxy-2,4-pentadienoate; H2O

sequence_source: UniProtKB REST P77608

substrate: 2-Hydroxy-2,4-pentadienoate; H2O


organism: Escherichia coli (strain K12)

substrate_name: 2-hydroxy-pentadienoic acid (at pH 6)

assay_conditions_summary: pH 6

substrate: 2-hydroxy-pentadienoic acid (at pH 6)


organism: Spinacia oleracea

substrate_name: But-2-enoyl-[acyl-carrier protein]; H2O

substrate: But-2-enoyl-[acyl-carrier protein]; H2O


substrate_name: 2-hydroxypentadienoic acid

substrate: 2-hydroxypentadienoic acid


organism: Paraburkholderia xenovorans

proof_lines:
activated by Mg2+
activated by Mn2+


organism: Pseudomonas putida

assay_conditions_summary: pH 7


organism: Arabidopsis thaliana


organism: Homo sapiens

substrate_name: acetyl-CoA

assay_conditions_summary: cofactor NADPH

substrate: acetyl-CoA


organism: Mus musculus

substrate_name: malonyl-CoA

substrate: malonyl-CoA


organism: Rattus norvegicus

substrate_name: Unknown

substrate: Unknown


organism: Helianthus annuus

proof_lines: pH 6.8, temperature not specified in the publication, HaHAD1 wild-type protein

proof_lines: pH 6.8, temperature not specified in the publication, HaHAD2 wild-type protein


sequence_variant_note: Resolved canonical sequence from UniProtKB:F2VYC9 canonical sequence with direct F166V reconstruction and applied mutation signature F166V to reconstruct the assayed variant sequence.

proof_lines: pH 6.8, temperature not specified in the publication, HaHAD1 F166V mutant


substrate_name: crotonoyl-CoA

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

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

substrate: crotonoyl-CoA


substrate_name: H2O; Crotonoyl-CoA

proof_lines: SABIO-RK modifier species: 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase(Enzyme) mutant K1699Q DH

substrate: H2O; Crotonoyl-CoA


substrate_name: Crotonoyl-CoA; H2O

proof_lines: SABIO-RK modifier species: 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase(Enzyme) mutant K1699A DH

substrate: Crotonoyl-CoA; H2O


sequence_source: UniProtKB:P49327 canonical sequence

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

column_label: TABLE THREE beta-hydroxyacyl dehydratase block, enzyme row WT; columns kcat (min^-1), KCRT (uM) and kcat/KCRT (uM^-1 min^-1); kcat cell = 6 min^-1; KCRT cell = 7 uM; kcat/KCRT cell = 0.9; author manuscript page 15 (PDF page 15). captured primary segment: crotonyl-CoA | wild-type HFAS, recombinant human fatty-acid synthase (HFAS) expressed in Sf9 insect cells | TABLE THREE beta-hydroxyacyl dehydratase block, enzyme row WT: Km CRT 7 uM | kcat 6 min^-1 | kcat/Km CRT printed cell 0.9 under the column head kcat/KCRT (uM^-1 min^-1)

raw_value_unit_evidence: TABLE THREE beta-hydroxyacyl dehydratase block, enzyme row WT: KCRT = 7 uM; kcat = 6 min^-1; printed kcat/KCRT = 0.9 uM^-1 min^-1.

table_label: TABLE THREE (kinetic evaluation of the wild-type and Lys-1699 mutant HFAS enzymes), beta-hydroxyacyl dehydratase block; printed column heads enzyme | kcat (min^-1) | KCRT (uM) | kcat/KCRT (uM^-1 min^-1)


organism: Streptomyces coelicolor


enzyme_display_name: tryptophan transaminase

substrate_name: L-tryptophan

enzyme: tryptophan transaminase

substrate: L-tryptophan


organism: Zea mays

sequence_source: UniProtKB:B4FJJ9; NCBI Protein:NP_001136624.1; PMID:24599492 gene anchor GRMZM5G840928

assay_conditions_summary: pH 8; 295.15 K; cofactor ATP


organism: Mycobacterium tuberculosis


assay_conditions_summary: cofactor FMN


smiles: O=O


proof_lines:
flavin: FMNH2, pH 7.4, 25°C
flavin: FADH2, pH 7.4, 25°C


substrate_name: L-Tryptophan

substrate: L-Tryptophan


substrate_name: L-Tryptophan; 2-Oxoglutarate

substrate: L-Tryptophan; 2-Oxoglutarate


organism: Thermococcus litoralis

substrate_name: 2-Oxoglutarate; L-Tryptophan

substrate: 2-Oxoglutarate; L-Tryptophan


enzyme_display_name: 1-carboxybiuret hydrolase

organism: Pseudomonas sp.

substrate_name: 1-Carboxybiuret; H2O

enzyme: 1-carboxybiuret hydrolase

substrate: 1-Carboxybiuret; H2O


organism: Pseudomonas sp. ADP

assay_conditions_summary: pH 9; 295.15 K; cofactor ADP

proof_lines: pH 9, 22°C, recombinant enzyme expressed in Escherichia coli

proof_lines: pH 9.0, temperature not specified in the publication

proof_lines: pH 9, 22°C, purified from Pseudomonas sp. ADP


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


organism: Rauvolfia serpentina

substrate_name: Vanillin

substrate: Vanillin


sequence_source: UniProtKB reviewed canonical sequence Q9AR73 (HQGT_RAUSE), retrieved by direct EC 2.4.1.218 + Rauvolfia serpentina lookup


enzyme_display_name: 7-methylguanosine nucleotidase

substrate_name: m(7)GMP (at 37 degrees Celsius)

enzyme: 7-methylguanosine nucleotidase

substrate: m(7)GMP (at 37 degrees Celsius)


substrate_name: AMP

substrate: AMP


substrate_name: (S)-NADHX

assay_conditions_summary: cofactor ATP

substrate: (S)-NADHX


substrate_name: indole-3-pyruvic acid (at pH 8.5 and 37 degrees Celsius)

proof_lines: kcat is 2.5 min(-1) with indole-3-pyruvic acid as substrate. kcat is 1.9 min(-1) with L-Met as substrate. kcat is 3.16 min(-1) with L-Phe as substrate (at pH 8.5 and 37 degrees Celsius).


organism: Pseudomonas sp. (strain ADP)

assay_conditions_summary: cofactor ADP

proof_lines: kcat is 15.5 sec(-1) with 1-carboxybiuret as substrate. kcat is 9.4 sec(-1) with 1-nitrobiuret as substrate. kcat is 7 sec(-1) with 1-carboxymalonamide as substrate. kcat is 19 sec(-1) with succinamate as substrate.


sequence_source: UniProtKB reviewed accession Q9AR73; direct UniProt REST accession lookup on 2026-06-15

proof_lines: pH 7.5, 50°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9AR73; direct UniProt REST accession lookup on 2026-06-15 and applied mutation signature A204V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9AR73; direct UniProt REST accession lookup on 2026-06-15 and applied mutation signature E368D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9AR73; direct UniProt REST accession lookup on 2026-06-15 and applied mutation signature E368A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9AR73; direct UniProt REST accession lookup on 2026-06-15 and applied mutation signature L86I to reconstruct the assayed variant sequence.


substrate_name: hydroquinone

substrate: hydroquinone


organism: Drosophila melanogaster

substrate_name: 7-Methylguanosine 5'-phosphate

sequence_source: UniProtKB reviewed accession Q9W197; direct UniProt REST accession lookup on 2026-06-15

column_label: Table 2 (Steady-state kinetic parameters for CG3362), substrate row 'm7GMP'; column 'Km' unit uM = 13; column 'Vmax' unit umol/min/mg = 11; column 'kcat' unit 1/s = 6.3; column 'kcat/Km' = 0.46; the Ki cell of this row is empty.

normalized_value_unit_evidence: kcat: printed cell 6.3 1/s; the printed unit is already per second, so no unit conversion applies; 6.3 s^(-1). Km: printed cell 13 uM; 1 uM is 0.001 mM, so 13 / 1000 = 0.013 mM. kcat/Km: printed cell 0.46 1/(s*uM); 1 1/(s*uM) is 1000 s^-1 mM^-1, so 0.46 x 1000 = 460.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate row m7GMP: Km cell 13 uM; Vmax cell 11 umol/min/mg; kcat cell 6.3 1/s; kcat/Km cell 0.46 in the 1/(s*uM) units implied by the Km column head uM and the kcat column head 1/s.

row_label: Table 2, substrate row m7GMP

table_label: Table 2: Steady-state kinetic parameters for CG3362 (J. Biol. Chem. 2013, 288(4):2441-2451)

substrate: 7-Methylguanosine 5'-phosphate


substrate_name: UMP

column_label: Table 2 (Steady-state kinetic parameters for CG3362), substrate row 'UMP'; column 'Km' unit uM = 91; column 'Vmax' unit umol/min/mg = 4.0; column 'kcat' unit 1/s = 2.3; column 'kcat/Km' = 0.03; the Ki cell of this row is empty.

normalized_value_unit_evidence: kcat: printed cell 2.3 1/s; the printed unit is already per second, so no unit conversion applies; 2.3 s^(-1). Km: printed cell 91 uM; 1 uM is 0.001 mM, so 91 / 1000 = 0.091 mM. kcat/Km: printed cell 0.03 1/(s*uM); 1 1/(s*uM) is 1000 s^-1 mM^-1, so 0.03 x 1000 = 30.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate row UMP: Km cell 91 uM; Vmax cell 4.0 umol/min/mg; kcat cell 2.3 1/s; kcat/Km cell 0.03 in the 1/(s*uM) units implied by the Km column head uM and the kcat column head 1/s.

row_label: Table 2, substrate row UMP

substrate: UMP


substrate_name: CMP

column_label: Table 2 (Steady-state kinetic parameters for CG3362), substrate row 'CMP'; column 'Km' unit uM = 48; column 'Vmax' unit umol/min/mg = 21; column 'kcat' unit 1/s = 12.0; column 'kcat/Km' = 0.25; the Ki cell of this row is empty.

normalized_value_unit_evidence: kcat: printed cell 12.0 1/s; the printed unit is already per second, so no unit conversion applies; 12.0 s^(-1). Km: printed cell 48 uM; 1 uM is 0.001 mM, so 48 / 1000 = 0.048 mM. kcat/Km: printed cell 0.25 1/(s*uM); 1 1/(s*uM) is 1000 s^-1 mM^-1, so 0.25 x 1000 = 250.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate row CMP: Km cell 48 uM; Vmax cell 21 umol/min/mg; kcat cell 12.0 1/s; kcat/Km cell 0.25 in the 1/(s*uM) units implied by the Km column head uM and the kcat column head 1/s.

row_label: Table 2, substrate row CMP

substrate: CMP


substrate_name: 7-Methylguanosine 5'-phosphate; H2O

normalized_value_unit_evidence: kcat: printed cell 6.3 1/s; the printed unit is already per second, so no unit conversion applies; 6.3 s^(-1). Km: printed cell 13 uM; 1 uM is 0.001 mM, so 13 / 1000 = 0.013 mM. Vmax: printed cell 11 umol/min/mg; 1 umol/min/mg is 0.000001 mol per 60 s per 0.001 g, so 11 / 60 / 1000 = 0.0001833333333333333 mol s^(-1) g^(-1). kcat/Km: printed cell 0.46 1/(s*uM); 1 1/(s*uM) is 1000 s^-1 mM^-1, so 0.46 x 1000 = 460.0 s^(-1)*mM^(-1).

substrate: 7-Methylguanosine 5'-phosphate; H2O


sequence_source: UniProtKB reviewed accession Q9H0P0; direct UniProt REST accession lookup on 2026-06-15

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


sequence_source: UniProtKB reviewed accession Q969T7; direct UniProt REST accession lookup on 2026-06-15

column_label: Table 3 (Steady-state kinetic parameters for human cNIII-like), substrate row 'CMP'; column 'Km' unit uM = 79; column 'Vmax' unit umol/min/mg = 12.0; column 'kcat' unit 1/s = 7; column 'kcat/Km' = 0.09; Table 3 prints no Ki column.

normalized_value_unit_evidence: kcat: printed cell 7 1/s; the printed unit is already per second, so no unit conversion applies; 7.0 s^(-1). Km: printed cell 79 uM; 1 uM is 0.001 mM, so 79 / 1000 = 0.079 mM. kcat/Km: printed cell 0.09 1/(s*uM); 1 1/(s*uM) is 1000 s^-1 mM^-1, so 0.09 x 1000 = 90.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row CMP: Km cell 79 uM; Vmax cell 12.0 umol/min/mg; kcat cell 7 1/s; kcat/Km cell 0.09 in the 1/(s*uM) units implied by the Km column head uM and the kcat column head 1/s.

row_label: Table 3, substrate row CMP

table_label: Table 3: Steady-state kinetic parameters for human cNIII-like (J. Biol. Chem. 2013, 288(4):2441-2451)


column_label: Table 3 (Steady-state kinetic parameters for human cNIII-like), substrate row 'UMP'; column 'Km' unit uM = 439; column 'Vmax' unit umol/min/mg = 10.7; column 'kcat' unit 1/s = 6.2; column 'kcat/Km' = 0.01; Table 3 prints no Ki column.

normalized_value_unit_evidence: kcat: printed cell 6.2 1/s; the printed unit is already per second, so no unit conversion applies; 6.2 s^(-1). Km: printed cell 439 uM; 1 uM is 0.001 mM, so 439 / 1000 = 0.439 mM. kcat/Km: printed cell 0.01 1/(s*uM); 1 1/(s*uM) is 1000 s^-1 mM^-1, so 0.01 x 1000 = 10.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row UMP: Km cell 439 uM; Vmax cell 10.7 umol/min/mg; kcat cell 6.2 1/s; kcat/Km cell 0.01 in the 1/(s*uM) units implied by the Km column head uM and the kcat column head 1/s.

row_label: Table 3, substrate row UMP


substrate_name: H2O; 7-Methylguanosine 5'-phosphate

column_label: Table 3 (Steady-state kinetic parameters for human cNIII-like), substrate row 'm7GMP'; column 'Km' unit uM = 7.8; column 'Vmax' unit umol/min/mg = 0.41; column 'kcat' unit 1/s = 0.24; column 'kcat/Km' = 0.03; Table 3 prints no Ki column.

normalized_value_unit_evidence: kcat: printed cell 0.24 1/s; the printed unit is already per second, so no unit conversion applies; 0.24 s^(-1). Km: printed cell 7.8 uM; 1 uM is 0.001 mM, so 7.8 / 1000 = 0.0078 mM. Vmax: printed cell 0.41 umol/min/mg; 1 umol/min/mg is 0.000001 mol per 60 s per 0.001 g, so 0.41 / 60 / 1000 = 0.000006833333333333333 mol s^(-1) g^(-1). kcat/Km: printed cell 0.03 1/(s*uM); 1 1/(s*uM) is 1000 s^-1 mM^-1, so 0.03 x 1000 = 30.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row m7GMP: Km cell 7.8 uM; Vmax cell 0.41 umol/min/mg; kcat cell 0.24 1/s; kcat/Km cell 0.03 in the 1/(s*uM) units implied by the Km column head uM and the kcat column head 1/s.

row_label: Table 3, substrate row m7GMP

substrate: H2O; 7-Methylguanosine 5'-phosphate


sequence_source: UniProtKB reviewed Q936X3

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


sequence_source: UniProtKB reviewed Q94AF2

assay_conditions_summary: pH 8; 295.15 K; cofactor NADH

row_label: Arabidopsis / NADHX

table_label: Table I


assay_conditions_summary: pH 8; 295.15 K; cofactor NADPH


row_label: Arabidopsis / NADPHX


sequence_source: UniProtKB reviewed Q8IW45 with PubMed 30576410 natural variant VAR_082224

sequence_variant_note: Mutation signature G63S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: ATP-dependent NAD(P)H-hydrate dehydratase(Enzyme) mutant G63S N-terminal His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8IW45 with PubMed 30576410 natural variant VAR_082225 and applied mutation signature R308C with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ATP-dependent NAD(P)H-hydrate dehydratase(Enzyme) mutant R308C N-terminal His-tagged


sequence_source: UniProtKB reviewed Q8IW45


sequence_source: UniProtKB reviewed Q9CZ42 canonical sequence only

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

proof_lines: SABIO-RK modifier species: ATP-dependent NAD(P)H-hydrate dehydratase(Enzyme) mutant Carkd (lacking mitochondrail propeptide), N-terminal His-tag


sequence_source: UniProtKB inactive/deleted accession A0A3L6F337


substrate_name: m(7)GMP (at 25 degrees Celsius)

proof_lines: kcat is 6.3 sec(-1) with m(7)GMP. kcat is 12 sec(-1) with CMP. kcat is 0.88 sec(-1) with GMP. kcat is 0.28 sec(-1) with AMP. kcat is 2.3 sec(-1) with UMP.

substrate: m(7)GMP (at 25 degrees Celsius)


proof_lines: kcat is 0.24 sec(-1) with m(7)GMP. kcat is 7 sec(-1) with CMP. kcat is 0.07 sec(-1) with GMP. kcat is 0.04 sec(-1) with AMP. kcat is 6.2 sec(-1) with UMP.


organism: Streptomyces viridochromogenes


sequence_source: UniProt REST direct accession lookup, Q5IW40, 2026-06-15


enzyme_display_name: valine N-monooxygenase

organism: Lotus japonicus

substrate_name: L-Valine

enzyme: valine N-monooxygenase

substrate: L-Valine


organism: Manihot esculenta

substrate_name: L-Isoleucine

substrate: L-Isoleucine


sequence_source: UniProt REST direct accession lookup, Q9M7B8, 2026-06-15


organism: Escherichia coli

substrate_name: Glyceraldehyde

smiles: O=CC(O)CO

substrate: Glyceraldehyde


substrate_name: isoleucine

proof_lines: kcat is 120 min(-1) with isoleucine as substrate (PubMed:15122013). kcat is 44 min(-1) with valine as substrate (PubMed:15122013).

substrate: isoleucine


proof_lines: kcat is 220 min(-1) with isoleucine as substrate (PubMed:15122013). kcat is 50 min(-1) with valine as substrate (PubMed:15122013).


substrate_name: valine

proof_lines: kcat is 2.3 min(-1) with isoleucine as substrate (PubMed:10636899). kcat is 4.3 min(-1) with valine as substrate (PubMed:10636899).

substrate: valine


organism: Escherichia coli (strain K12)

substrate_name: dihydroxyacetone

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

proof_lines: kcat is 2.8 sec(-1). Values measured with the DhaKLM complex.

substrate: dihydroxyacetone


proof_lines: kcat is 2.8 sec(-1) with dihydroxyacetone as substrate. Values measured with the DhaKLM complex (PubMed:11350937). kcat is 290 min(-1) with dihydroxyacetone as substrate. kcat is 12.5 min(-1) with D,L-glyceraldehyde as substrate (PubMed:154


organism: Arabidopsis thaliana

proof_lines: kcat is 140 min(-1) with indole-3-acetaldoxime as substrate. kcat is 26 min(-1) with p-hydroxyphenylacetaldoxime as substrate. kcat is 25 min(-1) with phenylacetaldoxime as substrate.


enzyme_display_name: gluconate dehydratase

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

substrate_name: D-xylonate

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

enzyme: gluconate dehydratase

substrate: D-xylonate


organism: Chromohalobacter israelensis (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11)

substrate_name: Unknown

proof_lines: kcat is 0.02 sec(-1) with D-mannonate. kcat is 0.04 sec(-1) with D-gluconate.

substrate: Unknown


organism: Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)

proof_lines: kcat is 0.03 sec(-1) with D-mannonate. kcat is 0.05 sec(-1) with D-gluconate.


organism: Musicola paradisiaca (strain Ech703)

proof_lines: kcat is 0.04 sec(-1) with D-mannonate. kcat is 0.03 sec(-1) with D-gluconate.


organism: Pantoea ananatis (strain LMG 20103)


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

proof_lines: kcat is 10.4 sec(-1) for gluconate and 1.08 sec(-1) for galactonate (at 70 degrees Celsius and pH 6). kcat is 12.6 sec(-1) for gluconate (at 78 degrees Celsius and pH 7).


organism: Salmonella enteritidis PT4 (strain P125109)


organism: Salmonella virchow (strain SL491)


organism: Streptomyces bingchenggensis (strain BCW-1)


enzyme_display_name: L-fuconate dehydratase

organism: Homo sapiens

substrate_name: L-fuconate

proof_lines: kcat is 0.5 sec(-1) for L-fuconate. kcat is 0.3 sec(-1) for L-galactonate. kcat is 0.3 sec(-1) for L-arabinonate. kcat is 0.04 sec(-1) for D-arabinonate. kcat is 0.002 sec(-1) for D-ribonate.

enzyme: L-fuconate dehydratase

substrate: L-fuconate


enzyme_display_name: pseudouridylate synthase

substrate_name: pseudouridine 5'-phosphate

proof_lines: kcat is 1.41 sec(-1) with pseudouridine 5'-phosphate as substrate.

enzyme: pseudouridylate synthase

substrate: pseudouridine 5'-phosphate


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

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

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


organism: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)


organism: Mus musculus

substrate_name: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one (using iron as cofactor)

sequence_source: source_record; direct UniProt Q99JT9 check matched the selected canonical sequence

smiles: CSCCC(=O)/C(=C/O)/O

proof_lines: kcat is 114.3 sec(-1) with 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one as substrate (using iron as cofactor) (PubMed:26858196). kcat is 7.55 sec(-1) with 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one as substrate (using cobalt as cofa


substrate_name: pseudouridine 5'-phosphate (in the presence of 0.5 mM Mn(2+))

sequence_source: source_record; direct UniProt P33025 check matched the selected canonical sequence

proof_lines: kcat is 3.74 sec(-1) for the synthesis of PsiMP.


organism: Klebsiella oxytoca

substrate_name: 1,2-Dihydroxyhex-1-en-3-one; O2

substrate: 1,2-Dihydroxyhex-1-en-3-one; O2


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


proof_lines:
Fe2+ bound enzyme, pH 7.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7


organism: Oryza sativa

substrate_name: 1,2-Dihydroxy-3-ketopent-1-ene; O2

substrate: 1,2-Dihydroxy-3-ketopent-1-ene; O2


enzyme_display_name: psoralen synthase

organism: Ammi majus

substrate_name: O2; Marmesin; NADPH; H+

proof_lines: SABIO-RK modifier species: psoralen synthas(Enzyme) mutant M120V, N-terminal 37 residues replaced by corresponding 33-residue membrane anchor region of CYP73A1

enzyme: psoralen synthase

substrate: O2; Marmesin; NADPH; H+


substrate_name: Marmesin; NADPH; O2; H+

assay_conditions_summary: pH 7; 300.15 K; cofactor NADPH

proof_lines: pH 7.0, 27°C, recombinant enzyme in microsomes

substrate: Marmesin; NADPH; O2; H+


organism: Apium graveolens

substrate_name: Marmesin; H+; NADPH; O2

substrate: Marmesin; H+; NADPH; O2


organism: Pastinaca sativa

substrate_name: O2; NADPH; Marmesin; H+

substrate: O2; NADPH; Marmesin; H+


organism: Arabidopsis thaliana

substrate_name: 3-Indoleacetaldoxime; O2; H+; NADPH; L-Cysteine

assay_conditions_summary: pH 8.1; 302.15 K; cofactor NADPH

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


organism: Oryza sativa subsp. indica

substrate_name: 1,2-dihydroxy-3-ketopent-1-ene (DHKP) (using iron as cofactor)


organism: Dictyostelium discoideum

substrate_name: S-adenosylmethionine

substrate: S-adenosylmethionine


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

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


enzyme_display_name: cis-zeatin O-beta-D-glucosyltransferase

organism: Zea mays

substrate_name: cis-zeatin

enzyme: cis-zeatin O-beta-D-glucosyltransferase

substrate: cis-zeatin


enzyme_display_name: phosphonopyruvate hydrolase

organism: Variovorax sp. (strain Pal2)

substrate_name: phosphonopyruvate (at 37 degrees Celsius, pH 7.0, with 5 umol CoCl(2))

enzyme: phosphonopyruvate hydrolase


enzyme_display_name: ADP-ribose 1''-phosphate phosphatase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: ADP-ribose 1''-phosphate

enzyme: ADP-ribose 1''-phosphate phosphatase

substrate: ADP-ribose 1''-phosphate


organism: Sulfolobus solfataricus

substrate_name: D-Gluconate

sequence_source: UniProt REST accession lookup Q97U27

substrate: D-Gluconate


organism: Aspergillus niger

substrate_name: L-fuconate

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

proof_lines: recombinant enzyme, pH 7.0, temperature not specified in the publication


organism: Xanthomonas campestris

substrate_name: D-Arabinonate

sequence_source: UniProt REST accession lookup Q8P3K2

substrate: D-Arabinonate


substrate_name: L-Fuconate

substrate: L-Fuconate


substrate_name: L-Galactonate

substrate: L-Galactonate


organism: Escherichia coli

substrate_name: H2O; Pseudouridine 5'-phosphate

sequence_source: UniProt REST accession lookup P33025

proof_lines:
pH 7.1, 30°C
Raw SKiD Env: Temp=30°C, pH=7.1

substrate: H2O; Pseudouridine 5'-phosphate


substrate_name: Uracil; D-Ribose 5-phosphate

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt P33025 canonical sequence and applied mutation signature E31A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pseudouridylate synthase(Enzyme) mutant E31A

substrate: Uracil; D-Ribose 5-phosphate


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt P33025 canonical sequence and applied mutation signature K166A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pseudouridylate synthase(Enzyme) mutant K166A


substrate_name: D-Ribose 5-phosphate; Uracil

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt P33025 canonical sequence and applied mutation signature N289A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pseudouridylate synthase(Enzyme) mutant N289A

substrate: D-Ribose 5-phosphate; Uracil


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt P33025 canonical sequence and applied mutation signature K93A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pseudouridylate synthase(Enzyme) mutant K93A


substrate_name: (E)-phenylacetaldoxime

sequence_source: UniProtKB:P48421 direct accession lookup

substrate: (E)-phenylacetaldoxime


enzyme_display_name: glutathione amide reductase

organism: Chromatium gracile

substrate_name: Glutathione amide disulfide

sequence_source: UniProtKB:D0VWY5 direct accession lookup

enzyme: glutathione amide reductase

substrate: Glutathione amide disulfide


substrate_name: NADH; Glutathione amide disulfide; H+

assay_conditions_summary: cofactor NADH

substrate: NADH; Glutathione amide disulfide; H+


substrate_name: NADH

assay_conditions_summary: pH 7.1; 298.15 K; cofactor NADH

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 7.1; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: Oxidized glutathione

substrate: Oxidized glutathione


organism: Thermus thermophilus

substrate_name: S-Adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GBB2 direct accession lookup plus Y194A reconstruction and applied mutation signature Y194A to reconstruct the assayed variant sequence.

substrate: S-Adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GBB2 direct accession lookup plus D170A reconstruction and applied mutation signature D170A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GBB2 direct accession lookup plus Y78A reconstruction and applied mutation signature Y78A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q8GBB2 direct accession lookup

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


organism: Oryza sativa Japonica Group

substrate_name: cis-zeatin


sequence_source: UniProtKB accession Q7XU02


sequence_source: UniProtKB accession Q7XU03


substrate_name: UDP-D-glucose; cis-Zeatin

sequence_source: UniProtKB accession Q8RXA5

substrate: UDP-D-glucose; cis-Zeatin


sequence_source: UniProtKB accession Q93XP7


substrate_name: Unknown

sequence_source: UniProtKB accession Q9S7N2

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


organism: Malassezia furfur

substrate_name: L-tryptophan

sequence_source: UniProtKB accession S4UF58

substrate: L-tryptophan


organism: Variovorax sp.

sequence_source: UniProtKB accession Q84G06

proof_lines:
37°C
25°C, pH 7.5
Raw SKiD Env: Temp=25°C, pH=7.5


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB accession Q84G06 by applying R188A and applied mutation signature R188A to reconstruct the assayed variant sequence.


organism: Saccharomyces cerevisiae

substrate_name: ADP-ribose 1''-phosphate

sequence_source: UniProtKB accession P38218

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ADP

substrate: ADP-ribose 1''-phosphate


proof_lines: Ki above 10 mM, in 20 mM Tris-HCl, pH 7.5, 5 mM MgCl2, 2.5 mM spermidine, 100 mM dithiothreitol, 0.4% (v/v) Triton X-100, at 30°C


organism: Haloferax volcanii

substrate_name: D-gluconate

sequence_source: UniProtKB accession D4GYD4

substrate: D-gluconate


organism: Picrophilus oshimae

substrate_name: D-galactonate

substrate: D-galactonate


substrate_name: D-Gluconate

sequence_source: UniProtKB accession Q97U27

substrate: D-Gluconate


organism: Oryza sativa


organism: Petroselinum crispum

assay_conditions_summary: pH 7; 293.15 K; cofactor NADPH


organism: Zea mays

substrate: cis-zeatin


organism: Bacteria


organism: Clostridium sporogenes

proof_lines: cosubstrate phenylalanine , pH 8.4, 22°C approximately

proof_lines: cosubstrate tryptophan, pH 8.4, 22°C approximately


organism: Sus scrofa

proof_lines:
pH 8.0, 37°C
cosubstrate phenylalanine, pH 8.0, 37°C


organism: Burkholderia cepacia


substrate_name: 3-Phosphonopyruvate; H2O

substrate: 3-Phosphonopyruvate; H2O


organism: Severe acute respiratory syndrome-related coronavirus

assay_conditions_summary: pH 7.5; cofactor ADP

proof_lines: in 50 mM Tris (pH 7.5), 1 mM MgCl2, 0.1 mM sodium azide, temperature not specified in the publication


organism: Alcaligenes sp.


organism: Clostridium pasteurianum


organism: Penicillium citrinum


organism: Saccharolobus solfataricus

sequence_source: UniProtKB reviewed accession Q97U27, FASTA direct check


organism: Sulfolobus solfataricus


organism: Thermoplasma acidophilum


organism: Aureobasidium pullulans

substrate_name: L-fuconate

substrate: L-fuconate


substrate_name: L-arabonate

substrate: L-arabonate


organism: Xanthomonas campestris


organism: Agrobacterium tumefaciens

substrate_name: Uracil

substrate: Uracil


organism: Saccharomyces cerevisiae

substrate_name: tRNAVal

proof_lines: substrate from yeast, in absence of Mg2+

proof_lines: substrate from yeast, intronless, limiting

substrate: tRNAVal


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Tetrahymena pyriformis

substrate_name: ribose 5-phosphate

substrate: ribose 5-phosphate


organism: Escherichia coli (strain K12)

substrate_name: succinyl-CoA (at pH 7.4)

assay_conditions_summary: pH 7.4; cofactor CoA

substrate: succinyl-CoA (at pH 7.4)


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


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: ppGpp (at 30 degrees Celsius and pH 8)

assay_conditions_summary: pH 8

substrate: ppGpp (at 30 degrees Celsius and pH 8)


organism: Streptococcus dysgalactiae subsp. equisimilis

substrate_name: GTP

substrate: GTP


organism: Escherichia coli

sequence_source: UniProt REST direct lookup P0A9D8

assay_conditions_summary: cofactor CoA


organism: Pseudomonas amygdali pv. tabaci

substrate_name: succinyl-CoA

sequence_source: UniProt REST direct lookup P31852

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

substrate: succinyl-CoA


substrate_name: DhaK; Dihydroxyacetone

sequence_source: UniProt REST direct lookup P76015

substrate: DhaK; Dihydroxyacetone


substrate_name: Phosphoenolpyruvate; Dihydroxyacetone

substrate: Phosphoenolpyruvate; Dihydroxyacetone


substrate_name: Dihydroxyacetone; Phosphoenolpyruvate

substrate: Dihydroxyacetone; Phosphoenolpyruvate


substrate_name: Glycerone

sequence_source: UniProt REST direct lookup P76014

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

substrate: Glycerone