substrate_name: Arsenate; Mycothiol

sequence_source: UniProtKB direct lookup for P0DKS5; matches accession reuse cache accession_2fb3d14c44b4d48b

substrate: Arsenate; Mycothiol


enzyme_display_name: arsenate-mycothiol transferase

organism: Corynebacterium glutamicum

substrate_name: arsenate

source_db: oed

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_source: UniProtKB direct lookup for P0DKS7; matches accession reuse cache accession_2293b723b69248b3

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

data_origin: experimental

enzyme: arsenate-mycothiol transferase

substrate: arsenate

status: unverified

source: oed


kcat_over_km_display: Not reported

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

proof_lines: isoform ArsC1, pH and temperature not specified in the publication

proof_lines: isoform ArsC2, pH and temperature not specified in the publication

source_databases_merged: sabio_rk brenda skid

source_db: brenda


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

source_db: uniprot

verification_status: corrected

assay_conditions_summary: pH 8; buffer 50 mM Hepes; cofactor mycoredoxin 1; mycothiol; mycothione reductase; NADPH

status: corrected

source: uniprot


enzyme_display_name: 6-oxocamphor hydrolase

organism: Rhodococcus sp.

sequence_variant_note: Resolved canonical sequence from uniprot_exact_accession:Q93TU6 and applied mutation signature H45A to reconstruct the assayed variant sequence.

mutation_type: substitution

enzyme: 6-oxocamphor hydrolase


sequence_variant_note: Resolved canonical sequence from uniprot_exact_accession:Q93TU6 and applied mutation signature H145A to reconstruct the assayed variant sequence.


substrate_name: 6-Oxocamphor; H2O

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

sequence_variant_note: Resolved canonical sequence from uniprot_exact_accession:Q93TU6 and applied mutation signature D154N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6-oxocamphor hydrolase(Enzyme) mutant D154N

substrate: 6-Oxocamphor; H2O


substrate_name: H2O; 6-Oxocamphor

sequence_variant_note: Resolved canonical sequence from uniprot_exact_accession:Q93TU6 and applied mutation signature H122A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6-oxocamphor hydrolase(Enzyme) mutant H122A

substrate: H2O; 6-Oxocamphor


proof_lines: SABIO-RK modifier species: 6-oxocamphor hydrolase(Enzyme) mutant H145A


proof_lines: SABIO-RK modifier species: 6-oxocamphor hydrolase(Enzyme) mutant H45A


organism: Rhodococcus sp


sequence_variant_note: Resolved canonical sequence from UniProtKB Q93TU6 canonical sequence checked directly; D154N reconstructed after confirming canonical residue D154. and applied mutation signature D154N to reconstruct the assayed variant sequence.


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

sequence_source: UniProtKB Q93TU6 FASTA checked directly for the canonical wild-type sequence.

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


sequence_variant_note: Resolved canonical sequence from UniProtKB Q93TU6 canonical sequence checked directly; E244Q reconstructed after confirming canonical residue E244. and applied mutation signature E244Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q93TU6 canonical sequence checked directly; E244Q reconstructed after confirming canonical residue E244.

proof_lines: SABIO-RK modifier species: 6-oxocamphor hydrolase(Enzyme) mutant E244Q


organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)

source: brenda


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


organism: Escherichia coli

substrate_name: UDP-GlcUA

kcat_display: Not reported

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

substrate: UDP-GlcUA


organism: Bos taurus

substrate_name: UDP-N-acetyl-beta-D-galactosamine

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

substrate: UDP-N-acetyl-beta-D-galactosamine


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

sequence_source: UniProtKB Q8L0V4, direct REST check on 2026-06-01

proof_lines: wild type enzyme, in 25 mM HEPES (pH 7.5), 100 mM NaCl, 20 mM MnCl2, 1 mM CaCl2, at 30°C

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


organism: Avibacterium paragallinarum

substrate_name: UDP-GalNAc

sequence_source: UniProtKB direct accession lookup for D0QYM5 on 2026-06-01

substrate: UDP-GalNAc


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

sequence_source: UniProtKB direct accession lookup for Q8L0V4 on 2026-06-01

source_databases_merged: brenda skid


organism: Homo sapiens

substrate_name: Chondroitin sulfate; UDPglucuronate

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

sequence_source: UniProtKB direct accession lookup for Q70JA7 on 2026-06-01

substrate: Chondroitin sulfate; UDPglucuronate


sequence_source: UniProtKB direct accession lookup for Q86X52 on 2026-06-01


organism: Sphingobium sp. (strain NBRC 103272 / SYK-6)

substrate_name: vanillate

verification_status: verified

assay_conditions_summary: pH 8

proof_lines: kcat is 5.76 sec(-1) with vanillate as substrate.

substrate: vanillate

status: verified


organism: Neomoorella thermoacetica

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


organism: Sphingobium sp.

sequence_source: UniProtKB reviewed accession G2IQS7, direct lookup 2026-06-01


organism: Sphingomonas paucimobilis

sequence_source: UniProtKB accession Q60FX1 redirected to reviewed primary accession G2IQS7, direct lookup 2026-06-01


substrate_name: Vanillate; 5,6,7,8-Tetrahydrofolate

substrate: Vanillate; 5,6,7,8-Tetrahydrofolate


proof_lines: substrate tetrahydrofolate, pH 8.0, 30°C


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB reviewed accession P9WKL5 fetched by direct accession lookup

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


organism: Mycobacteroides abscessus

sequence_source: UniProtKB reviewed accession B1MCE2 fetched by direct accession lookup


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: HQNO

proof_lines: kcat is 0.8 sec(-1) with HQNO as substrate (PubMed:33064871). kcat is 0.074 min(-1) with compound 14 as substrate (PubMed:27432954).

substrate: HQNO


organism: Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948)

proof_lines: kcat is 2.0 sec(-1) with HQNO as substrate.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P9WKL5:S140A and applied mutation signature S140A to reconstruct the assayed variant sequence.


organism: Arabidopsis thaliana

substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Humulus lupulus

substrate_name: AMP

substrate: AMP


substrate_name: Dimethylallyl diphosphate; ATP

sequence_source: UniProtKB reviewed direct accession lookup for Q9SB60

substrate: Dimethylallyl diphosphate; ATP


substrate_name: ADP

sequence_source: UniProtKB reviewed direct accession lookup for Q5GHF7

assay_conditions_summary: pH 7; 298.15 K; buffer or raw SKiD pH/temperature notes; cofactor ATP

proof_lines: in HEPES (20mM, pH 7.0; 150 mM NaCl, 3 mM dithiothreitol), at 25°C

substrate: ADP


organism: Morus alba

sequence_source: UniProtKB TrEMBL direct accession lookup for Q08ET4

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP


assay_conditions_summary: pH 7; 298.15 K; buffer 100 mM Tris-HCl; cofactor ATP

proof_lines: in 100 mM Tris-HCl buffer, pH 7.0, containing 50 mM KCl, 2 mM MnCl2, 1 mg/ml bovine serum albumin, and 1 mM dithiohtreitol, at 25°C


substrate_name: dimethylallyl diphosphate

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

substrate: dimethylallyl diphosphate


sequence_source: UniProtKB Q9SB60 reviewed Swiss-Prot entry IPT4_ARATH; PMID 11479373 reference covers catalytic activity and the source cache records sequence_source=source_record with confidence 1.0.

assay_conditions_summary: pH 7.5; 297.15 K; cofactor ATP

proof_lines: in 25 mM Tris-HCl, pH 7.5, 10 mM MgCl2+, 5 mM 2-mercaptoethanol at 24°C


sequence_source: UniProtKB Q5GHF7 reviewed Swiss-Prot entry IPT_HUMLU; PMID 15381407 reference covers catalytic activity and the source cache records sequence_source=source_record with confidence 1.0.

assay_conditions_summary: pH 8; 298.15 K; buffer 100 mM Tris-HCl; cofactor ATP

proof_lines: in 100 mM Tris-HCl buffer, pH 8.0, containing 50 mM KCl, 10 mM MgCl2, 1 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 25°C

proof_lines: in 100 mM Tris–HCl buffer, pH 8.0, containing 50 mM KCl, 10 mM MgCl2, 1 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 25°C


enzyme_display_name: homocysteine S-methyltransferase

organism: Brassica oleracea var. italica

substrate_name: DL-homocysteine

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

enzyme: homocysteine S-methyltransferase

substrate: DL-homocysteine


substrate_name: S-Methyl-L-methionine; L-Homocysteine

proof_lines: pH 7.5, 30°C, cosubstrate: S-adenosyl-L-methionine

proof_lines: pH 7.5, 30°C, cosubstrate: S-methyl-L-methionine

substrate: S-Methyl-L-methionine; L-Homocysteine


substrate_name: L-Homocysteine; S-Methyl-L-methionine

substrate: L-Homocysteine; S-Methyl-L-methionine


proof_lines: pH 7.5, 25°C, cosubstrate: S-methyl-L-methionine

proof_lines: pH 7.5, 25°C, cosubstrate: S-adenosyl-L-methionine


organism: Escherichia coli (strain K12)

substrate_name: L-Homocysteine

substrate: L-Homocysteine


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

proof_lines: pH 6, 30°C, cosubstrate: S-adenosyl-L-methionine

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


substrate_name: S-methyl-L-methionine

proof_lines: final concentrations of S-methyl-L-methionine ranging from 0.1 mM to 9 mM, lower value than obtained for BHMT (EC 2.1.1.5)

substrate: S-methyl-L-methionine


enzyme_display_name: carnosine N-methyltransferase

organism: Gallus gallus

substrate_name: S-adenosyl-L-methionine

enzyme: carnosine N-methyltransferase

substrate: S-adenosyl-L-methionine


organism: Oryctolagus cuniculus

substrate_name: Actin peptide H

substrate: Actin peptide H


substrate_name: carnosine

proof_lines: kcat is 0.034 sec(-1) for carnosine. kcat is 0.519 sec(-1) for S-adenosyl-L-methionine.

substrate: carnosine


proof_lines: kcat is 0.14 min(-1) for carnosine. kcat is 2.51 min(-1) for S-adenosyl-L-methionine.


proof_lines: kcat is 0.09 min(-1) for carnosine. kcat is 3.57 min(-1) for S-adenosyl-L-methionine.


organism: Rattus norvegicus

proof_lines: kcat is 0.15 min(-1) for carnosine. kcat is 4.69 min(-1) for S-adenosyl-L-methionine.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 0.38 min(-1) for carnosine. kcat is 0.74 min(-1) for S-adenosyl-L-methionine.


substrate_name: S-Adenosyl-L-methionine

sequence_source: UniProt REST FASTA accession F1N9S8; matched identity reuse cache accession:F1N9S8

substrate: S-Adenosyl-L-methionine


substrate_name: S-Adenosyl-L-methionine; Carnosine

substrate: S-Adenosyl-L-methionine; Carnosine


organism: Homo sapiens

sequence_source: UniProt REST FASTA accession Q8N4J0; matched identity reuse cache accession:Q8N4J0


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


sequence_source: UniProt REST FASTA accession Q5BJZ6; matched identity reuse cache accession:Q5BJZ6


substrate_name: Carnosine; S-Adenosyl-L-methionine

sequence_source: UniProtKB Q5BJZ6 direct accession lookup; sequence matched the accession reuse cache.

substrate: Carnosine; S-Adenosyl-L-methionine


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB P53934 direct accession lookup; sequence matched the accession reuse cache.


enzyme_display_name: sulfoquinovosidase

organism: Agrobacterium tumefaciens

substrate_name: 4-nitrophenyl alpha-sulfoquinovoside

sequence_source: UniProt A9CEZ0 canonical sequence with K245Q reconstructed during review from PMID 30276262 UniProt mutagenesis evidence.

sequence_variant_note: Mutation signature K245Q matches the mutant residue at offset +0 and the reference residue at offset +11; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: mutant K245Q, pH not specified in the publication, temperature not specified in the publication

enzyme: sulfoquinovosidase

substrate: 4-nitrophenyl alpha-sulfoquinovoside


sequence_source: UniProt A9CEZ0 canonical AtSQase/SmoI sequence linked to PMID 30276262.

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


proof_lines: mutantK245Q/ E270Q, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant E270Q, pH not specified in the publication, temperature not specified in the publication


substrate_name: para-nitrophenyl alpha-sulfoquinovoside

proof_lines: kcat is 14.3 sec(-1) with para-nitrophenyl alpha-sulfoquinovoside as substrate.

substrate: para-nitrophenyl alpha-sulfoquinovoside


organism: Escherichia coli

km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProt P32138 REST direct check; variant sequence reconstructed from the P32138 canonical sequence when mutation_signature is present. and applied mutation signature R301K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: sulfoquinovosidase(Enzyme) mutant R301K His-tagged


sequence_variant_note: Resolved canonical sequence from UniProt P32138 REST direct check; variant sequence reconstructed from the P32138 canonical sequence when mutation_signature is present. and applied mutation signature R301Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: sulfoquinovosidase(Enzyme) mutant R301Q His-tagged


sequence_source: UniProt P32138 REST direct check; variant sequence reconstructed from the P32138 canonical sequence when mutation_signature is present.

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


sequence_variant_note: Resolved canonical sequence from UniProt P32138 REST direct check; variant sequence reconstructed from the P32138 canonical sequence when mutation_signature is present. and applied mutation signature Q288E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: sulfoquinovosidase(Enzyme) mutant Q288E His-tagged

proof_lines: mutant Q288E, pH not specified in the publication, temperature not specified in the publication


substrate_name: p-Nitrophenol alpha-D-glucopyranoside

substrate: p-Nitrophenol alpha-D-glucopyranoside


sequence_variant_note: Resolved canonical sequence from UniProt P32138 REST direct check; variant sequence reconstructed from the P32138 canonical sequence when mutation_signature is present. and applied mutation signature Q262K/Q288E to reconstruct the assayed variant sequence.

proof_lines: mutant Q262K/Q288E, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt P32138 REST direct check; variant sequence reconstructed from the P32138 canonical sequence when mutation_signature is present. and applied mutation signature Q262K to reconstruct the assayed variant sequence.

proof_lines: mutant Q262K, pH not specified in the publication, temperature not specified in the publication


organism: Marinobacter adhaerens (strain DSM 23420 / HP15)

substrate_name: 2-O-(alpha-D-glucopyranosyl)glycerol (at pH 6.5 and 37 degrees Celsius)

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

proof_lines: kcat is 14 sec(-1) towards 2-O-(alpha-D-glucopyranosyl)glycerol for the phosphorolytic direction (at pH 6.5 and 37 degrees Celsius). kcat is 14 sec(-1) towards phosphate for the phosphorolytic direction (at pH 6.5 and 37 degrees Celsius). k


organism: Marinobacter adhaerens


proof_lines:
pH 6.5, 37°C
recombinant enzyme, pH 6.5, 37°C
Raw SKiD Env: Temp=37°C, pH=6.5


substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


substrate_name: glycerol

smiles: OCC(O)CO

substrate: glycerol


substrate_name: phosphate

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

substrate: phosphate


enzyme_display_name: cyanohydrin beta-glucosyltransferase

organism: Sorghum bicolor

substrate_name: mandelonitrile

proof_lines: kcat is 10.6 sec(-1) with mandelonitrile as substrate. kcat is 0.10 sec(-1) with geraniol as substrate. kcat is 0.09 sec(-1) with beta-citronellol as substrate. kcat is 0.06 sec(-1) with nerol as substrate. kcat is 0.06 sec(-1) with 1-hexan

enzyme: cyanohydrin beta-glucosyltransferase

substrate: mandelonitrile


substrate_name: geraniol

substrate: geraniol


substrate_name: Prenol

sequence_source: UniProtKB Q9SBL1 direct lookup; matches accession reuse cache accession_f5a28182a913b775

smiles: CC(C)=CCO

substrate: Prenol


substrate_name: Leaf alcohol

smiles: CCC=CCCO

substrate: Leaf alcohol


substrate_name: Mandelonitrile; UDPglucose

proof_lines: pH 7.5, 30°C, cosubstrate: mandelonitrile

substrate: Mandelonitrile; UDPglucose


organism: Prunus dulcis

substrate_name: benzyl alcohol

substrate: benzyl alcohol


sequence_source: UniProtKB:Q9SBL1 direct accession lookup

smiles: C=C(C)CCO


smiles: CCCCCCO


substrate_name: beta-Citronellol

smiles: CC(C)=CCCC(C)CCO

substrate: beta-Citronellol


substrate_name: Mandelonitrile

substrate: Mandelonitrile


substrate_name: Nerol

smiles: CC(C)=CCC/C(C)=C\CO

substrate: Nerol


substrate_name: Geraniol

smiles: CC(C)=CCC/C(C)=C/CO

substrate: Geraniol


substrate_name: 2-Hydroxy-3-methoxybenzyl alcohol

substrate: 2-Hydroxy-3-methoxybenzyl alcohol


enzyme_display_name: GDP-mannose 4,6-dehydratase

organism: Pseudomonas aeruginosa

substrate_name: GDP-mannose

enzyme: GDP-mannose 4,6-dehydratase

substrate: GDP-mannose


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


substrate_name: GDP-alpha-D-mannose

ki_unit: mM

sequence_source: multiple

source_databases_merged: brenda uniprot

substrate: GDP-alpha-D-mannose


organism: Phaseolus vulgaris


substrate_name: GDPmannose

substrate: GDPmannose


organism: Sus scrofa


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


organism: Burkholderia cenocepacia J2315


sequence_source: UniProtKB O60547; reviewed GMDS_HUMAN; PMID 9525924 citation; REST check 2026-06-02


organism: Mortierella alpina

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


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

proof_lines: mutant S156A, 37°C, pH not specified in the publication


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


organism: Burkholderia cepacia

proof_lines: at pH 7.4 and 25°C, in the presence of 1 mol MgCl2 per mol of protein


proof_lines:
pH 8, M-GMD and L-GMD
pH 8, isoenzyme M-GMD
pH 8, isoenzyme L-GMD

source_databases_merged: brenda skid uniprot


substrate_name: GDP-D-mannose

proof_lines: Table 1 reports BceN from B. cenocepacia J2315 using GDP-D-mannose as substrate.

substrate: GDP-D-mannose


substrate_name: Unknown

substrate: Unknown


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

substrate_name: UDP-N-acetylbacillosamine

substrate: UDP-N-acetylbacillosamine


organism: Bacillus subtilis (strain 168)


organism: Acinetobacter baumannii

source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Bacillus subtilis

substrate_name: Acetyl-CoA; UDP-N-acetylbacillosamine

sequence_source: UniProtKB P71063 direct lookup; accession reuse cache canonical sequence from source_record

assay_conditions_summary: cofactor CoA

substrate: Acetyl-CoA; UDP-N-acetylbacillosamine


organism: Neisseria gonorrhoeae

sequence_source: UniProtKB Q5FAE1 direct lookup plus validated Q370A substitution reconstruction

sequence_variant_note: Mutation signature Q370A matches the mutant residue at offset +0 and the reference residue at offset -1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB Q5FAE1 direct lookup plus validated Q369A substitution reconstruction

sequence_variant_note: Mutation signature Q369A matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB Q5FAE1 direct lookup plus validated H210F substitution reconstruction


sequence_source: UniProtKB Q5FAE1 direct lookup plus validated D332A substitution reconstruction


sequence_source: UniProtKB Q5FAE1 direct lookup; RCSB 4M98/4M99 SIFTS accession support


sequence_source: UniProtKB reviewed accession Q0P9D1 (PGLD_CAMJE)


enzyme_display_name: ureidoglycolate amidohydrolase

organism: Arabidopsis thaliana

substrate_name: (S)-ureidoglycolate

sequence_source: source_record; UniProt REST direct check Q8VXY9

proof_lines: kcat is 1.43 sec(-1) with (S)-ureidoglycolate as substrate (at pH 8.5 and 30 degrees Celsius) (PubMed:25020232). kcat is 7.9 sec(-1) for (S)-ureidoglycolate (PubMed:19935661).

enzyme: ureidoglycolate amidohydrolase

substrate: (S)-ureidoglycolate


organism: Glycine max

substrate_name: H2O; (-)-Ureidoglycolate

substrate: H2O; (-)-Ureidoglycolate


organism: Oryza sativa


substrate_name: ureidoglycolate

proof_lines:
in presence of Mn2+
in absence of Mn2+

substrate: ureidoglycolate


organism: Oryza sativa subsp. japonica

sequence_source: source_record; UniProt REST accession Q2QMN7 cross-check


sequence_source: UniProt Q8VXY9 canonical sequence; direct UniProt REST check on 2026-06-02 plus RCSB 4PXB/4PXC/4PXE accession anchors from PMID 25020232.


sequence_source: Reconstructed from UniProt Q8VXY9 canonical sequence by applying Y423F; residue check performed on 2026-06-02; RCSB 4PXB/4PXC/4PXE support Q8VXY9 identity from PMID 25020232.


proof_lines:
wild-type enzyme, pH 8.5, 30°C
pH 7.4, 30°C, wild-type enzyme


sequence_source: Reconstructed from UniProt Q8VXY9 canonical sequence by applying H424N; residue check performed on 2026-06-02; RCSB 4PXB/4PXC/4PXE support Q8VXY9 identity from PMID 25020232.

sequence_variant_note: Mutation signature H424N matches the mutant residue at offset +0 and the reference residue at offset -9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: Reconstructed from UniProt Q8VXY9 canonical sequence by applying Q257N; residue check performed on 2026-06-02; RCSB 4PXB/4PXC/4PXE support Q8VXY9 identity from PMID 25020232.


sequence_source: UniProtKB Q8VXY9 direct REST lookup on 2026-06-02; variant reconstructed from the checked Q8VXY9 canonical sequence


sequence_source: UniProtKB Q8VXY9 direct REST lookup on 2026-06-02; canonical sequence matches local accession cache

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8.5
Raw SKiD Env: Temp=30°C, pH=7.4


substrate_name: (-)-Ureidoglycolate; H2O

sequence_source: UniProtKB Q2QMN7 direct REST lookup on 2026-06-02; canonical sequence matches local accession cache

column_label: Table I: Kinetic constants (Plant Physiol. 163:672-681, 2013), row 'OsUAH': column 'Km' = 188; column 'kcat (s^-1)' = 55; column 'Catalytic Efficiency (s^-1 M^-1)' = 2.95 x 10^5; column 'Specific Activity (units mg^-1)' is printed but is not one of the export schema's kinetic metrics.

normalized_value_unit_evidence: Km: printed cell 188 uM; 188 uM / 1000 = 0.188 mM, equal to the catalog value. kcat: printed cell 55 s^-1; no unit conversion needed, equal to the catalog value. This catalog row does not carry a catalytic-efficiency value, so no ratio is exported or proposed here.

raw_value_unit_evidence: Table I, row 'OsUAH' (Plant Physiol. 163:672-681, 2013): Km = 188 uM; kcat = 55 s^-1.

substrate: (-)-Ureidoglycolate; H2O


substrate_name: (-)-Ureidoglycolate

normalized_value_unit_evidence: Km: printed cell 188 uM; 188 uM / 1000 = 0.188 mM. kcat: printed cell 55 s^-1; no unit conversion needed. Catalytic Efficiency: printed cell 2.95 x 10^5 s^-1 M^-1; 2.95 x 10^5 s^-1 M^-1 / 1000 = 295.0 s^-1 mM^-1. This paper prints its own Catalytic Efficiency cell for this row; it is an independently reported primary value and it does not equal the quotient computed from the row's own kcat and Km (55.0 / 0.188 = 292.5531914893617). The catalog carries the quotient; this record proposes the paper's own printed value (295.0) as the catalytic-efficiency correction, per the ratio policy for an independently reported primary catalytic-efficiency cell.

raw_value_unit_evidence: Table I, row 'OsUAH' (Plant Physiol. 163:672-681, 2013): Km = 188 uM; kcat = 55 s^-1; printed Catalytic Efficiency = 2.95 x 10^5 s^-1 M^-1.

table_label: Table I: Kinetic constants (Plant Physiol. 163:672-681, 2013)

substrate: (-)-Ureidoglycolate


enzyme_display_name: palmitoyl-CoA hydrolase

organism: Homo sapiens

substrate_name: myristoyl-CoA

sequence_source: UniProtKB reviewed accession Q8N1Q8 direct lookup

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

column_label: Figure 2F (PDF page 5 of 13, journal page 2689), decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C14:0`: Km (uM) = 8.6; kcat (s^-1) = 19.7; kcat/Km (M^-1 s^-1) = 2.3x10^6.

normalized_value_unit_evidence: kcat: printed cell 19.7 s^-1 -> 19.7 s^(-1) (already per second, carried unchanged); the exported value is 19.7 s^(-1). Km: printed cell 8.6 uM -> 0.0086 mM (divide by 1000); the exported value is 0.009 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.3x10^6 M^-1 s^-1 for this substrate line -> 2300.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 2188.888888888889 s^(-1)*mM^(-1).

row_label: Figure 2F, decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C14:0`

table_label: Figure 2F (PDF page 5 of 13, journal page 2689) 'Steady-state kinetic constants for hThem5 catalyzed hydrolysis of selected Acyl-CoA esters'

enzyme: palmitoyl-CoA hydrolase

substrate: myristoyl-CoA


substrate_name: Arachidonyl-CoA

substrate: Arachidonyl-CoA


substrate_name: H2O; Myristoyl-CoA

sequence_source: UniProtKB reviewed accession Q5T1C6 direct lookup plus selected-source N183A mutation reconstruction

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant N183A His6-tagged

substrate: H2O; Myristoyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5T1C6 and applied mutation signature K207A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

column_label: Table 1: Steady-state kinetic constants of wild-type and mutant hHTEM4-catalyzed hydrolysis of myristoyl-CoA at pH 7.5 and 25 C (Biochemistry 2012, 51(33):6490-6492, NIH Public Access author manuscript page 9), printed column heads hTHEM4 | kcat (s-1) | Km (uM) | kcat/Km (M-1 s-1). hTHEM4 row 'K207A': column 'kcat (s-1)' = 1.5 ± 0.1; column 'Km (uM)' = 2.8 ± 0.1; column 'kcat/Km (M-1 s-1)' = 6.7 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.5 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 1.5 s^(-1); the exported value is 1.5 s^(-1). Km: printed Table 1 cell 2.8 uM; 1 uM is 0.001 mM, so 2.8 / 1000 = 0.0028 mM; the paper value is 0.0028 mM; the exported value is 0.003 mM. kcat/Km: printed Table 1 cell 6.7 x 10^5 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 6.7 x 10^5 / 1000 = 670 s^-1 mM^-1; the paper value is 670 s^(-1)*mM^(-1); the exported value is 500 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, hTHEM4 row 'K207A', myristoyl-CoA hydrolysis: kcat = 1.5 s-1; Km = 2.8 uM; printed kcat/Km = 6.7 x 10^5 M-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5T1C6 and applied mutation signature R206A to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-state kinetic constants of wild-type and mutant hHTEM4-catalyzed hydrolysis of myristoyl-CoA at pH 7.5 and 25 C (Biochemistry 2012, 51(33):6490-6492, NIH Public Access author manuscript page 9), printed column heads hTHEM4 | kcat (s-1) | Km (uM) | kcat/Km (M-1 s-1). hTHEM4 row 'R206A': column 'kcat (s-1)' = 1.5 ± 0.1; column 'Km (uM)' = 4.4 ± 0.6; column 'kcat/Km (M-1 s-1)' = 3.6 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.5 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 1.5 s^(-1); the exported value is 1.5 s^(-1). Km: printed Table 1 cell 4.4 uM; 1 uM is 0.001 mM, so 4.4 / 1000 = 0.0044 mM; the paper value is 0.0044 mM; the exported value is 0.004 mM. kcat/Km: printed Table 1 cell 3.6 x 10^5 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 3.6 x 10^5 / 1000 = 360 s^-1 mM^-1; the paper value is 360 s^(-1)*mM^(-1); the exported value is 375 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, hTHEM4 row 'R206A', myristoyl-CoA hydrolysis: kcat = 1.5 s-1; Km = 4.4 uM; printed kcat/Km = 3.6 x 10^5 M-1 s-1.


substrate_name: Myristoyl-CoA; H2O

sequence_source: UniProtKB reviewed accession Q5T1C6 direct lookup plus selected-source D161E mutation reconstruction

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant D161E His6-tagged

substrate: Myristoyl-CoA; H2O


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5T1C6 and applied mutation signature H152A to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-state kinetic constants of wild-type and mutant hHTEM4-catalyzed hydrolysis of myristoyl-CoA at pH 7.5 and 25 C (Biochemistry 2012, 51(33):6490-6492, NIH Public Access author manuscript page 9), printed column heads hTHEM4 | kcat (s-1) | Km (uM) | kcat/Km (M-1 s-1). hTHEM4 row 'H152A': column 'kcat (s-1)' = 0.04 ± 0.01; column 'Km (uM)' = 62 ± 4; column 'kcat/Km (M-1 s-1)' = 6.7 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.04 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.04 s^(-1); the exported value is 0.04 s^(-1). Km: printed Table 1 cell 62 uM; 1 uM is 0.001 mM, so 62 / 1000 = 0.062 mM; the paper value is 0.062 mM; the exported value is 0.062 mM. kcat/Km: printed Table 1 cell 6.7 x 10^2 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 6.7 x 10^2 / 1000 = 0.67 s^-1 mM^-1; the paper value is 0.67 s^(-1)*mM^(-1); the exported value is 0.645161290323 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, hTHEM4 row 'H152A', myristoyl-CoA hydrolysis: kcat = 0.04 s-1; Km = 62 uM; printed kcat/Km = 6.7 x 10^2 M-1 s-1.


organism: Escherichia coli

substrate_name: lauroyl-CoA

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

substrate: lauroyl-CoA


substrate_name: Octanoyl-CoA; H2O

sequence_source: UniProtKB reviewed direct lookup: O00154, Homo sapiens, cytosolic acyl coenzyme A thioester hydrolase, EC 3.1.2.2.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA

substrate: Octanoyl-CoA; H2O


substrate_name: H2O; Choloyl-CoA

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

substrate: H2O; Choloyl-CoA


substrate_name: Decanoyl-CoA; H2O

sequence_source: UniProtKB reviewed direct lookup: Q86TX2, Homo sapiens, acyl-coenzyme A thioesterase 1, EC 3.1.2.-.

substrate: Decanoyl-CoA; H2O


sequence_source: UniProtKB reviewed direct lookup: P49753, Homo sapiens, acyl-coenzyme A thioesterase 2 mitochondrial, EC 3.1.2.2.


substrate_name: H2O; Succinyl-CoA

substrate: H2O; Succinyl-CoA


mutation_type: deletion

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant delta99 N-terminal His6-MBP-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB P0ADA1 reviewed sequence plus PMID 16515533 mutagenesis mapping mature G44A to precursor G70A. and applied mutation signature G44A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.


substrate_name: p-Nitrophenyl butyrate

sequence_variant_note: Resolved canonical sequence from UniProtKB P0ADA1 reviewed sequence plus PMID 16515533 mutagenesis mapping mature N73A to precursor N99A. and applied mutation signature N73A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.

substrate: p-Nitrophenyl butyrate


substrate_name: H2O; p-Nitrophenyl butyrate

sequence_source: UniProtKB P0ADA1 reviewed sequence plus PMID 16515533 mutagenesis mapping mature G44A to precursor G70A.

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant G44A

substrate: H2O; p-Nitrophenyl butyrate


sequence_variant_note: Resolved canonical sequence from UniProtKB P0ADA1 reviewed sequence plus PMID 16515533 mutagenesis mapping mature D154A to precursor D180A. and applied mutation signature D154A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant D154A


substrate_name: Lauroyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB P0ADA1 reviewed sequence plus PMID 16515533 mutagenesis mapping mature S10A to precursor S36A. and applied mutation signature S10A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.

substrate: Lauroyl-CoA


sequence_source: UniProtKB P0ADA1 reviewed sequence plus PMID 16515533 mutagenesis mapping mature D154A to precursor D180A.


sequence_source: UniProtKB P0ADA1 reviewed sequence plus PMID 16515533 mutagenesis mapping mature N73A to precursor N99A.


substrate_name: p-Nitrophenyl butyrate; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB P0ADA1 reviewed sequence plus PMID 16515533 mutagenesis mapping mature H157A to precursor H183A. and applied mutation signature H157A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant H157A

substrate: p-Nitrophenyl butyrate; H2O


substrate_name: Lauroyl-CoA; H2O

sequence_source: UniProtKB:F4HU51 reviewed canonical sequence; selected Q8GYW7 resolves as a secondary accession on that live entry.

substrate: Lauroyl-CoA; H2O


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0ADA1 and applied mutation signature S10A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; buffer 0.1 M sodium phosphate

column_label: Table 2 (Kinetic analysis of wild-type and mutants of TAP), substrate stub 'L-NBTNPE', parameter stub rows 'k cat (s-1)', 'K m (mM)' and 'k cat /K m', enzyme-form column head 'S10A': k cat 0.02, K m 0.061, k cat /K m 0.32.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.02 s-1; the value is already in s^-1, so no unit conversion applies, giving 0.02 s^(-1). Km: printed Table 2 cell 0.061 mM; the value is already in mM, so no unit conversion applies, giving 0.061 mM. kcat/Km: the Table 2 k cat /K m stub prints 0.32 in this column; the table's own kcat column unit s^-1 and Km column unit mM make that printed cell 0.32 s^(-1)*mM^(-1), so no unit conversion applies.

raw_value_unit_evidence: Table 2, substrate stub 'L-NBTNPE', enzyme-form column head 'S10A': k cat = 0.02 s-1; K m = 0.061 mM; printed k cat /K m = 0.32.

table_label: Table 2: Kinetic analysis of wild-type and mutants of TAP (Biochem. J. 2006, 397, 69-76)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0ADA1 and applied mutation signature G44A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic analysis of wild-type and mutants of TAP), substrate stub 'NPB', parameter stub rows 'k cat (s-1)', 'K m (mM)' and 'k cat /K m', enzyme-form column head 'G44A': k cat 3.16, K m 1.10, k cat /K m 2.87.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.16 s-1; the value is already in s^-1, so no unit conversion applies, giving 3.16 s^(-1). Km: printed Table 2 cell 1.10 mM; the value is already in mM, so no unit conversion applies, giving 1.1 mM. kcat/Km: the Table 2 k cat /K m stub prints 2.87 in this column; the table's own kcat column unit s^-1 and Km column unit mM make that printed cell 2.87 s^(-1)*mM^(-1), so no unit conversion applies.

raw_value_unit_evidence: Table 2, substrate stub 'NPB', enzyme-form column head 'G44A': k cat = 3.16 s-1; K m = 1.10 mM; printed k cat /K m = 2.87.


sequence_source: UniProtKB:P0ADA1 reviewed canonical precursor sequence.

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

column_label: Table 2 (Kinetic analysis of wild-type and mutants of TAP), substrate stub 'L-NBTNPE', parameter stub rows 'k cat (s-1)', 'K m (mM)' and 'k cat /K m', enzyme-form column head 'Wild-type': k cat 88.99, K m 0.174, k cat /K m 512.40.

normalized_value_unit_evidence: kcat: printed Table 2 cell 88.99 s-1; the value is already in s^-1, so no unit conversion applies, giving 88.99 s^(-1). Km: printed Table 2 cell 0.174 mM; the value is already in mM, so no unit conversion applies, giving 0.174 mM. kcat/Km: the Table 2 k cat /K m stub prints 512.40 in this column; the table's own kcat column unit s^-1 and Km column unit mM make that printed cell 512.4 s^(-1)*mM^(-1), so no unit conversion applies.

raw_value_unit_evidence: Table 2, substrate stub 'L-NBTNPE', enzyme-form column head 'Wild-type': k cat = 88.99 s-1; K m = 0.174 mM; printed k cat /K m = 512.40.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ADA1 reviewed canonical precursor sequence with N73A applied at full precursor residue 99 after UniProt signal peptide residues 1-26. and applied mutation signature N73A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant N73A


sequence_source: UniProtKB:P0ADA1 reviewed canonical precursor sequence with S10A applied at full precursor residue 36 after UniProt signal peptide residues 1-26.

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +26, so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant S10A


column_label: Table 2 (Kinetic analysis of wild-type and mutants of TAP), substrate stub 'NPB', parameter stub rows 'k cat (s-1)', 'K m (mM)' and 'k cat /K m', enzyme-form column head 'Wild-type': k cat 15.29, K m 0.87, k cat /K m 17.75.

normalized_value_unit_evidence: kcat: printed Table 2 cell 15.29 s-1; the value is already in s^-1, so no unit conversion applies, giving 15.29 s^(-1). Km: printed Table 2 cell 0.87 mM; the value is already in mM, so no unit conversion applies, giving 0.87 mM. kcat/Km: the Table 2 k cat /K m stub prints 17.75 in this column; the table's own kcat column unit s^-1 and Km column unit mM make that printed cell 17.75 s^(-1)*mM^(-1), so no unit conversion applies.

raw_value_unit_evidence: Table 2, substrate stub 'NPB', enzyme-form column head 'Wild-type': k cat = 15.29 s-1; K m = 0.87 mM; printed k cat /K m = 17.75.


proof_lines:
native enzyme
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=37°C, pH=7


enzyme_display_name: Thioesterase 1/protease 1/lysophospholipase L1

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ADA1 direct accession lookup and applied mutation signature G44A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ADA1 direct accession lookup and applied mutation signature S10A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.

enzyme: Thioesterase 1/protease 1/lysophospholipase L1


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ADA1 direct accession lookup and applied mutation signature N73A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ADA1 direct accession lookup and applied mutation signature D154A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0ADA1 direct accession lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ADA1 direct accession lookup and applied mutation signature P110A/L109P with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.


organism: Rattus norvegicus

substrate_name: H2O; Palmitoyl-CoA

sequence_source: UniProtKB Q64559 canonical FASTA

proof_lines:
the induced E. coli enzyme
brain ACT
recombinant enzyme

substrate: H2O; Palmitoyl-CoA


sequence_source: UniProt Q5T1C6 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProt Q5T1C6 canonical sequence; H152F reconstructed after direct residue check and applied mutation signature H152F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q5T1C6 canonical sequence; T177A reconstructed after direct residue check and applied mutation signature T177A to reconstruct the assayed variant sequence.


sequence_source: UniProt Q5T1C6 canonical sequence; T177A reconstructed after direct residue check

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant T177A His6-tagged


sequence_variant_note: Resolved canonical sequence from UniProt Q5T1C6 canonical sequence; D161N reconstructed after direct residue check and applied mutation signature D161N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant D161N His6-tagged


sequence_source: UniProt Q5T1C6 canonical sequence; H152F reconstructed after direct residue check

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant H152F His6-tagged


sequence_source: UniProt Q5T1C6 canonical sequence; D161N reconstructed after direct residue check


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q5T1C6 (THEM4_HUMAN); canonical residue K207 matched and was substituted to A. and applied mutation signature K207A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant K207A His6-tagged


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5T1C6 and applied mutation signature D161E to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-state kinetic constants of wild-type and mutant hHTEM4-catalyzed hydrolysis of myristoyl-CoA at pH 7.5 and 25 C (Biochemistry 2012, 51(33):6490-6492, NIH Public Access author manuscript page 9), printed column heads hTHEM4 | kcat (s-1) | Km (uM) | kcat/Km (M-1 s-1). hTHEM4 row 'D161E': column 'kcat (s-1)' = 0.1 ± 0.01; column 'Km (uM)' = 45 ± 3; column 'kcat/Km (M-1 s-1)' = 2.3 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.1 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.1 s^(-1); the exported value is 0.1 s^(-1). Km: printed Table 1 cell 45 uM; 1 uM is 0.001 mM, so 45 / 1000 = 0.045 mM; the paper value is 0.045 mM; the exported value is 0.045 mM. kcat/Km: printed Table 1 cell 2.3 x 10^3 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 2.3 x 10^3 / 1000 = 2.3 s^-1 mM^-1; the paper value is 2.3 s^(-1)*mM^(-1); the exported value is 2.22222222222 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, hTHEM4 row 'D161E', myristoyl-CoA hydrolysis: kcat = 0.1 s-1; Km = 45 uM; printed kcat/Km = 2.3 x 10^3 M-1 s-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q5T1C6 (THEM4_HUMAN); canonical residue R206 matched and was substituted to A. and applied mutation signature R206A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant R206A His6-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q5T1C6 (THEM4_HUMAN); canonical residue H152 matched and was substituted to A. and applied mutation signature H152A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant H152A His6-tagged


sequence_source: UniProtKB reviewed accession O14734 (ACOT8_HUMAN) canonical sequence.


organism: Mus musculus

substrate_name: palmitoleoyl-CoA

sequence_source: UniProtKB reviewed accession P58137 (ACOT8_MOUSE) canonical sequence.

assay_conditions_summary: pH 7.4; cofactor CoA

substrate: palmitoleoyl-CoA


substrate_name: Palmitoyl-CoA; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O55137 (ACOT1_MOUSE); canonical residue S232 matched and was substituted to A. and applied mutation signature S232A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant S232A His-tagged

substrate: Palmitoyl-CoA; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O55137 (ACOT1_MOUSE); canonical residue D324 matched and was substituted to A. and applied mutation signature D324A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant D324A His-tagged


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


organism: Bos taurus

substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


substrate_name: S-palmitoyl H-Ras

substrate: S-palmitoyl H-Ras


substrate_name: S-palmitoyl-CoA

substrate: S-palmitoyl-CoA


substrate_name: succinyl-CoA

substrate: succinyl-CoA


sequence_source: UniProtKB O55137 live lookup; source SABIO-RK records cite O55137 for Mus musculus PMID 11694534.


sequence_variant_note: Resolved canonical sequence from UniProtKB O55137 live lookup plus selected SABIO-RK H358Q modifier note; residue 358 in canonical O55137 is H and was substituted to Q. and applied mutation signature H358Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant H358Q His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB O55137 live lookup plus selected SABIO-RK S232C modifier note; residue 232 in canonical O55137 is S and was substituted to C. and applied mutation signature S232C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant S232C His-tagged


substrate_name: H2O; Hexanoyl-CoA

sequence_source: UniProtKB Q6Q2Z6 live lookup; source SABIO-RK records cite Q6Q2Z6 for Mus musculus PMID 15007068.

substrate: H2O; Hexanoyl-CoA


substrate_name: Hexanoyl-CoA; H2O

sequence_source: UniProtKB Q9QYR7 live lookup; source SABIO-RK records cite Q9QYR7 for Mus musculus PMID 15007068.

substrate: Hexanoyl-CoA; H2O


sequence_source: UniProtKB Q91V12 live lookup; source SABIO-RK records cite Q91V12 for Mus musculus PMID 15288813.


sequence_source: UniProtKB Q9QYR9 live lookup; selected BRENDA snapshots cite Q9QYR9 for Mus musculus palmitoyl-CoA and myristoyl-CoA rows.

assay_conditions_summary: pH 7.6; 310.15 K; cofactor CoA


organism: Mycobacterium tuberculosis

substrate_name: dodecanoyl-CoA

sequence_source: UniProtKB P9WM67 live lookup; selected BRENDA/SKiD snapshots cite P9WM67 for Mycobacterium tuberculosis substrate rows.

assay_conditions_summary: pH 7.5; cofactor CoA

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

substrate: dodecanoyl-CoA


substrate_name: myristoyl-CoA

substrate: myristoyl-CoA


substrate_name: taurine toward choloyl-CoA

substrate: taurine toward choloyl-CoA


substrate_name: palmitoyl-CoA (C16:0)

substrate: palmitoyl-CoA (C16:0)


substrate_name: decanoyl-CoA

substrate: decanoyl-CoA


substrate_name: Arachidonoyl-CoA

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

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines:
isozyme MTE-I, pH 7.4, 37°C
isozyme CTE-I, pH 7.4, 37°C

substrate: Arachidonoyl-CoA


substrate_name: hexanoyl-coA

substrate: hexanoyl-coA


substrate_name: palmitoyl-CoA (isoform A at 30 degrees Celsius)


substrate_name: propanoyl-CoA

substrate: propanoyl-CoA


organism: Escherichia coli (strain K12)

proof_lines: kcat is 88.99 sec(-1) for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester as substrate (PubMed:16515533). kcat is 62.4 sec(-1) for p-nitrophenyl butyrate as substrate (PubMed:9070299). kcat is 15.29 sec(-1) for p-nitrophenyl butyrate as


substrate_name: n-decanoyl-CoA

proof_lines: kcat is 0.016 sec(-1) for n-decanoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.0047 sec(-1) for n-octanoyl-CoA hydrolase activity (PubMed:19170545). kcat is 0.022 sec(-1) for n-hexanoyl-CoA hydrolase activity (PubMed:19170545). kc

substrate: n-decanoyl-CoA


substrate_name: Unknown

proof_lines: kcat is 5 min(-1) for the hydrolysis of hexadecanoyl-CoA (PubMed:22897136). kcat is 3.5 min(-1) for the hydrolysis of tetradecanoyl-CoA (PubMed:22897136). kcat is 2.3 min(-1) for the hydrolysis of dodecanoyl-CoA (PubMed:22897136). kcat is 0

substrate: Unknown


substrate_name: acetoacetyl-CoA

proof_lines: kcat is 14.8 sec(-1) for the degradation of acetoacetyl-CoA (3-oxoacyl-CoA thiolase) (PubMed:25478839). kcat is 1.4 sec(-1) for the synthesis of acetoacetyl-CoA (PubMed:25478839). kcat is 0.02 sec(-1) for octanoyl-CoA hydrolysis (PubMed:254

substrate: acetoacetyl-CoA


substrate_name: acetyl-CoA

proof_lines: In summary, KM for medium- to long-chain acyl CoAs is in the order 1.4-6.7 uM, and with short-chain acyl CoAs range from 8 to 30 uM. KM for bile acid-CoA esters is in the range 6-15 uM.

substrate: acetyl-CoA


substrate_name: hexanoyl-CoA (at 37 degrees Celsius)

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

proof_lines: kcat is 3 sec(-1) for hexanoyl-CoA hydrolase activity (at 37 degrees Celsius) (PubMed:19405909). kcat is 5 sec(-1) for decanoyl-CoA hydrolase activity (at 37 degrees Celsius) (PubMed:19405909). kcat is 3 sec(-1) for dodecanoyl-CoA hydrolase

substrate: hexanoyl-CoA (at 37 degrees Celsius)


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 0.037 sec(-1) with palmitoyl-CoA as substrate. kcat is 0.019 sec(-1) with stearoyl-CoA as substrate. kcat is 0.015 sec(-1) with lauroyl-CoA as substrate. kcat is 0.012 sec(-1) with hexanoyl-CoA as substrate.


proof_lines: kcat is 0.00342 sec(-1) with palmitoyl-CoA as substrate.


organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

substrate_name: p-nitrophenyl butyrate

proof_lines: The N-terminal esterase domain, when expressed alone, shows activities five to ten times higher than those of the complete enzyme EstP towards all tested substrates, whereas substrate affinity and the activity profiles are still the same.

substrate: p-nitrophenyl butyrate


sequence_source: UniProtKB:F4HU51; PMID 14660652

assay_conditions_summary: pH 8; cofactor CoA


organism: Buckleyzyma aurantiaca

substrate_name: stearoyl-CoA

assay_conditions_summary: pH 7.4; 298.15 K; cofactor CoA

substrate: stearoyl-CoA


organism: Cavia porcellus

substrate_name: hexadecanoyl-CoA

substrate: hexadecanoyl-CoA


organism: Cereibacter sphaeroides

assay_conditions_summary: pH 7.8; 295.15 K; cofactor CoA


organism: Cricetulus griseus

substrate_name: H2O; Palmitoyl-CoA

substrate: H2O; Palmitoyl-CoA


organism: Diutina rugosa

substrate_name: dodecanoyl-CoA

substrate: dodecanoyl-CoA


substrate_name: fatty-acyl-CoA thioester

substrate: fatty-acyl-CoA thioester


organism: Euglena gracilis

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA


organism: Mougeotia scalaris


organism: Mycolicibacterium smegmatis


substrate_name: oleoyl-CoA

proof_lines:
pH 7.5, 37°C
for the microsomal enzyme

substrate: oleoyl-CoA


organism: Homo sapiens

substrate_name: H2O; Myristoyl-CoA

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

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant delta39 C-terminal His6-tag

substrate: H2O; Myristoyl-CoA


substrate_name: myristoyl-CoA

sequence_source: UniProtKB reviewed entry Q5T1C6 / THEM4_HUMAN FASTA, checked directly during review.

substrate: myristoyl-CoA


substrate_name: Linoleoyl-CoA

sequence_source: UniProtKB reviewed entry Q8N1Q8 / THEM5_HUMAN FASTA, checked directly during review.

column_label: Figure 2F (PDF page 5 of 13, journal page 2689), decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C18:2`: Km (uM) = 4.2; kcat (s^-1) = 12.2; kcat/Km (M^-1 s^-1) = 2.9x10^6.

normalized_value_unit_evidence: kcat: printed cell 12.2 s^-1 -> 12.2 s^(-1) (already per second, carried unchanged); the exported value is 12.2 s^(-1). Km: printed cell 4.2 uM -> 0.0042 mM (divide by 1000); the exported value is 0.004 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.9x10^6 M^-1 s^-1 for this substrate line -> 2900.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 3049.9999999999995 s^(-1)*mM^(-1).

row_label: Figure 2F, decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C18:2`

substrate: Linoleoyl-CoA


substrate_name: Palmitoleoyl-CoA

column_label: Figure 2F (PDF page 5 of 13, journal page 2689), decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C16:1`: Km (uM) = 26.7; kcat (s^-1) = 11.5; kcat/Km (M^-1 s^-1) = 4.3x10^5.

normalized_value_unit_evidence: kcat: printed cell 11.5 s^-1 -> 11.5 s^(-1) (already per second, carried unchanged); the exported value is 11.5 s^(-1). Km: printed cell 26.7 uM -> 0.0267 mM (divide by 1000); the exported value is 0.027 mM. kcat/Km: the paper PRINTS the kcat/Km cell 4.3x10^5 M^-1 s^-1 for this substrate line -> 430.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 425.9259259259259 s^(-1)*mM^(-1).

row_label: Figure 2F, decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C16:1`

substrate: Palmitoleoyl-CoA


substrate_name: Oleoyl-CoA

substrate: Oleoyl-CoA


sequence_variant_note: Resolved canonical sequence from PMID 22586271 Materials and Methods sequence for human THEM5 35-247 with C-terminal His6 tag. and applied mutation signature Δ34 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) wildtype delta34Them5


column_label: Figure 2F (PDF page 5 of 13, journal page 2689), decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C18:0`: Km (uM) = 4.2; kcat (s^-1) = 1.2; kcat/Km (M^-1 s^-1) = 2.9 x10^5.

normalized_value_unit_evidence: kcat: printed cell 1.2 s^-1 -> 1.2 s^(-1) (already per second, carried unchanged); the exported value is 1.2 s^(-1). Km: printed cell 4.2 uM -> 0.0042 mM (divide by 1000); the exported value is 0.004 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.9 x10^5 M^-1 s^-1 for this substrate line -> 290.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 300.0 s^(-1)*mM^(-1).

row_label: Figure 2F, decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C18:0`


substrate_name: alpha-Linolenoyl-CoA

column_label: Figure 2F (PDF page 5 of 13, journal page 2689), decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C18:3`: Km (uM) = 15.4; kcat (s^-1) = 13.3; kcat/Km (M^-1 s^-1) = 8.6x10^5.

normalized_value_unit_evidence: kcat: printed cell 13.3 s^-1 -> 13.3 s^(-1) (already per second, carried unchanged); the exported value is 13.3 s^(-1). Km: printed cell 15.4 uM -> 0.0154 mM (divide by 1000); the exported value is 0.015 mM. kcat/Km: the paper PRINTS the kcat/Km cell 8.6x10^5 M^-1 s^-1 for this substrate line -> 860.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 886.6666666666667 s^(-1)*mM^(-1).

row_label: Figure 2F, decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C18:3`

substrate: alpha-Linolenoyl-CoA


organism: Rhodotorula aurantiaca

substrate_name: H2O; Octanoyl-CoA

substrate: H2O; Octanoyl-CoA


organism: Sus scrofa

substrate_name: acetyl-CoA

assay_conditions_summary: pH 8; 301.15 K; cofactor CoA

proof_lines: pH 8.0, 28°C, with palmitoyl-CoA as substrate

substrate: acetyl-CoA


enzyme_display_name: phosphoenolpyruvate carboxykinase (ATP)

organism: Escherichia coli

substrate_name: oxaloacetate

sequence_source: UniProtKB P22259 canonical FASTA; R65Q reconstructed after confirming canonical residue 65 is R

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

enzyme: phosphoenolpyruvate carboxykinase (ATP)

substrate: oxaloacetate


sequence_source: UniProtKB P22259 canonical FASTA; H232Q reconstructed after confirming canonical residue 232 is H


sequence_source: UniProtKB P22259 canonical FASTA; K212S reconstructed after confirming canonical residue 212 is K


sequence_source: UniProtKB P22259 canonical FASTA; K254S reconstructed after confirming canonical residue 254 is K


sequence_source: UniProtKB P22259 canonical FASTA from direct REST lookup


sequence_source: UniProtKB P22259 canonical FASTA; S250A reconstructed after confirming canonical residue 250 is S

sequence_variant_note: Mutation signature S250A matches the mutant residue at offset +0 and the reference residue at offset +8; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB P22259 canonical FASTA; R333Q reconstructed after confirming canonical residue 333 is R


substrate_name: ATP; Oxaloacetate

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines:
at pH 7.0 and 37°C
Raw SKiD Env: Temp=37°C, pH=7

substrate: ATP; Oxaloacetate


organism: Anaerobiospirillum succiniciproducens

substrate_name: ADP; CO2; Phosphoenolpyruvate

sequence_source: UniProtKB accession O09460 direct REST check

assay_conditions_summary: cofactor ATP

substrate: ADP; CO2; Phosphoenolpyruvate


substrate_name: CO2; ADP; Phosphoenolpyruvate

sequence_source: UniProtKB accession O09460 canonical sequence with T249A substitution applied after residue check

proof_lines: SABIO-RK modifier species: phosphoenolpyruvate carboxykinase (ATP)(Enzyme) mutant Thr249Ala

substrate: CO2; ADP; Phosphoenolpyruvate


substrate_name: Phosphoenolpyruvate; CO2; ADP

sequence_source: UniProtKB accession O09460 canonical sequence with D262E substitution applied after residue check

proof_lines: SABIO-RK modifier species: phosphoenolpyruvate carboxykinase (ATP)(Enzyme) mutant Asp262Glu

substrate: Phosphoenolpyruvate; CO2; ADP


organism: Arabidopsis thaliana

sequence_source: UniProtKB accession Q9T074 direct REST check

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP


substrate_name: ADP

sequence_source: UniProtKB accession B5X574 direct REST check

substrate: ADP


substrate_name: phosphoenolpyruvate

sequence_source: UniProtKB accession P22259 direct REST check

substrate: phosphoenolpyruvate


sequence_source: UniProtKB accession P22259 canonical sequence with K213S substitution applied after residue check


sequence_source: UniProtKB accession P22259 canonical sequence with D269N substitution applied after residue check


organism: Leishmania major

sequence_source: UniProtKB REST accession E9ADF9

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession E9ADF9 and applied mutation signature Y180F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession E9ADF9 and applied mutation signature H205Q to reconstruct the assayed variant sequence.


substrate_name: ADP; phosphoenolpyruvate; ATP; oxaloacetate

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession E9ADF9 and applied mutation signature Y180A to reconstruct the assayed variant sequence.


organism: Ruminococcus albus

substrate_name: ADP; phosphoenolpyruvate; oxaloacetate; ATP

sequence_source: UniProtKB REST accession B3Y6D3

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

assay_conditions_summary: pH 7; cofactor ATP


organism: Saccharomyces cerevisiae

substrate_name: Phosphoenolpyruvate; CO2; ADP; ADP; CO2; Phosphoenolpyruvate; Phosphoenolpyruvate; ADP; CO2

sequence_source: UniProtKB REST accession P10963

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P10963 and applied mutation signature R336Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphoenolpyruvate carboxykinase (ATP)(Enzyme) mutant R336Q


substrate_name: ADP; Phosphoenolpyruvate; CO2; ADP; CO2; Phosphoenolpyruvate; CO2; ADP; Phosphoenolpyruvate; Oxaloacetate; ATP

proof_lines:
ADP in form of MnADP-
CO2 in form of HCO3-
ATP in form of MnATP2-


substrate_name: CO2; Phosphoenolpyruvate; ADP; Phosphoenolpyruvate; CO2; ADP; CO2; ADP; Phosphoenolpyruvate

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession P10963 and applied mutation signature R336K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphoenolpyruvate carboxykinase (ATP)(Enzyme) mutant R336K


organism: Trypanosoma cruzi

sequence_source: UniProtKB reviewed accession P51058

assay_conditions_summary: pH 9; cofactor ATP


organism: Unknown


substrate_name: ADP (at 37 degrees Celsius and at pH 6.2)


organism: Escherichia coli (strain K12)

substrate_name: manganese (at 31 degrees Celsius and pH 7.5)


sequence_variant_note: Resolved canonical sequence from UniProt REST uniprotkb/E9ADF9 checked during review; accession is Leishmania major phosphoenolpyruvate carboxykinase (ATP), EC 4.1.1.49. Sequence reconstructed by applying Y180A to the canonical E9ADF9 sequence; canonical residue 180 was Y. and applied mutation signature Y180A to reconstruct the assayed variant sequence.


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from UniProt REST uniprotkb/E9ADF9 checked during review; accession is Leishmania major phosphoenolpyruvate carboxykinase (ATP), EC 4.1.1.49. Sequence reconstructed by applying Y180F to the canonical E9ADF9 sequence; canonical residue 180 was Y. and applied mutation signature Y180F to reconstruct the assayed variant sequence.

substrate: ATP


sequence_variant_note: Resolved canonical sequence from UniProt REST uniprotkb/E9ADF9 checked during review; accession is Leishmania major phosphoenolpyruvate carboxykinase (ATP), EC 4.1.1.49. Sequence reconstructed by applying H205Q to the canonical E9ADF9 sequence; canonical residue 205 was H. and applied mutation signature H205Q to reconstruct the assayed variant sequence.


sequence_source: UniProt REST uniprotkb/E9ADF9 checked during review; accession is Leishmania major phosphoenolpyruvate carboxykinase (ATP), EC 4.1.1.49. Sequence reconstructed by applying Y180F to the canonical E9ADF9 sequence; canonical residue 180 was Y.


sequence_source: UniProt REST uniprotkb/E9ADF9 checked during review; accession is Leishmania major phosphoenolpyruvate carboxykinase (ATP), EC 4.1.1.49. Sequence reconstructed by applying H205Q to the canonical E9ADF9 sequence; canonical residue 205 was H.


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


sequence_source: UniProt REST uniprotkb/E9ADF9 checked during review; accession is Leishmania major phosphoenolpyruvate carboxykinase (ATP), EC 4.1.1.49. Canonical wild-type sequence used unchanged.

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


substrate_name: IDP

sequence_source: UniProtKB P10963 canonical sequence

assay_conditions_summary: pH 6.9; 303.15 K; cofactor ATP

substrate: IDP


substrate_name: ITP

substrate: ITP


substrate_name: UDP

substrate: UDP


substrate_name: CTP

substrate: CTP


sequence_variant_note: Resolved canonical sequence from UniProtKB P10963 canonical sequence with reviewed T463A substitution reconstructed during review and applied mutation signature T463A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphoenolpyruvate carboxykinase (ATP)(Enzyme) mutant T463A


sequence_source: UniProtKB P10963 canonical sequence with reviewed T463A substitution reconstructed during review


substrate_name: GTP

substrate: GTP


organism: Alternanthera ficoidea

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

proof_lines:
pH 7.3, 37°C, 10 mM bicarbonate
pH 7.3, 37°C, 0.05 mM bicarbonate


organism: Alternanthera ficoides

proof_lines:
pH 7.3, 37°C, 0.05 mM bicarbonate
pH 7.3, 37°C, 10 mM bicarbonate


organism: Alternanthera pungens


organism: Alternanthera sessilis


sequence_variant_note: Resolved canonical sequence from UniProtKB:O09460 plus PMID 14987800 H225E mutation evidence and applied mutation signature H225E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 303.15 K; cofactor ATP


substrate_name: oxaloacetate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P10963/PCK1 direct REST lookup; mutation reconstructed after confirming residue 272 is E in the canonical 549 aa sequence. and applied mutation signature E272Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.6; 303.15 K; buffer 100 mM MOPS; cofactor ATP

proof_lines: mutant enzyme E272Q, in 100 mM MOPS buffer (pH 6.6), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P10963/PCK1 direct REST lookup; mutation reconstructed after confirming residue 212 is K in the canonical 549 aa sequence. and applied mutation signature K212R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K212R, in 100 mM MOPS buffer (pH 6.6), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P10963/PCK1 direct REST lookup; mutation reconstructed after confirming residue 213 is K in the canonical 549 aa sequence. and applied mutation signature K213Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K213Q, in 100 mM MOPS buffer (pH 6.6), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P10963/PCK1 direct REST lookup; mutation reconstructed after confirming residue 460 is L in the canonical 549 aa sequence. and applied mutation signature L460A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; buffer 100 mM MOPS; cofactor ATP

proof_lines: mutant enzyme L460A, in 100 mM MOPS buffer (pH 7.0), at 30°C

proof_lines: mutant enzyme L460A, in 100 mM MOPS buffer (pH 6.6), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P10963/PCK1 direct REST lookup; mutation reconstructed after confirming residue 299 is E in the canonical 549 aa sequence. and applied mutation signature E299A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E299A, in 100 mM MOPS buffer (pH 6.6), at 30°C

proof_lines: mutant enzyme E299A, in 100 mM MOPS buffer (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P10963/PCK1 direct REST lookup; mutation reconstructed after confirming residue 207 is Y in the canonical 549 aa sequence. and applied mutation signature Y207L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y207L, in 100 mM MOPS buffer (pH 6.6), at 30°C


organism: Salinivibrio costicola

substrate_name: Unknown

substrate: Unknown


organism: Thermus thermophilus


organism: Trypanosoma brucei


proof_lines:
ATP in form of MnATP2-
ADP in form of MnADP-
CO2 in form of HCO3-


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


proof_lines: condition: 0.1 mM Mn2+, 5 mM Mg2 /Vmax: 37 micromol/min/mg

proof_lines: condition: 4 mM Mn2+ /Vmax: 47 micromol/min/mg


substrate_name: ADP

proof_lines:
in presence of Mg2+
CO2 in form of HCO3-
in presence of Mn2+


organism: Megathyrsus maximus

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP


assay_conditions_summary: pH 6.6; 303.15 K; cofactor ADP


sequence_source: UniProt REST P10963 canonical sequence checked directly during review


sequence_variant_note: Resolved canonical sequence from UniProt REST P10963 canonical sequence with T463A reconstructed during review and applied mutation signature T463A to reconstruct the assayed variant sequence.


substrate_name: GDP

substrate: GDP


sequence_source: UniProt REST P10963 canonical sequence with T463A reconstructed during review


substrate_name: phosphoenolpyruvate

sequence_source: UniProt REST P10963 direct lookup

proof_lines: for the pyruvate kinase-like activity of wild-type

proof_lines: wild-type, apparent kinetic parameters for wild-type in the phosphoenolpyruvate formation direction


sequence_variant_note: Resolved canonical sequence from UniProt REST P10963 direct lookup with R457M reconstruction and applied mutation signature R457M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P10963 direct lookup with S252A reconstruction and applied mutation signature S252A to reconstruct the assayed variant sequence.

proof_lines: S252A mutant, apparent kinetic parameters for S252A mutant in the phosphoenolpyruvate carboxylation direction

proof_lines: for the pyruvate kinase-like activity of S252A mutant

proof_lines: for the oxaloacetate decarboxylase activity of S252A mutant


organism: Selenomonas ruminantium

sequence_source: UniProt REST O83023 direct lookup

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9ADF9 FASTA direct lookup; Y180A reconstructed from the canonical sequence. and applied mutation signature Y180A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:E9ADF9 FASTA direct lookup.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9ADF9 FASTA direct lookup; H205Q reconstructed from the canonical sequence. and applied mutation signature H205Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9ADF9 FASTA direct lookup; Y180F reconstructed from the canonical sequence. and applied mutation signature Y180F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:E9ADF9 FASTA direct lookup; Y180A reconstructed from the canonical sequence.


sequence_source: UniProtKB:E9ADF9 FASTA direct lookup; H205Q reconstructed from the canonical sequence.


enzyme_display_name: adenosine deaminase

organism: Mus musculus

substrate_name: H2O; Adenosine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P03958; reconstructed_variant_sequence:E217Q and applied mutation signature E217Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant E217Q

enzyme: adenosine deaminase

substrate: H2O; Adenosine


substrate_name: Adenosine; H2O

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

substrate: Adenosine; H2O


substrate_name: Adenosine

substrate: Adenosine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P03958; reconstructed_variant_sequence:E217G and applied mutation signature E217G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P03958; reconstructed_variant_sequence:E217D and applied mutation signature E217D to reconstruct the assayed variant sequence.


organism: Plasmodium falciparum

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8IJA9; reconstructed_variant_sequence:D176A and applied mutation signature D176A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant D176A

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme D176A


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8IJA9; reconstructed_variant_sequence:C27Q/L227I and applied mutation signature C27Q/L227I to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant C27Q+L227I

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme C27Q/L227I


organism: Bos taurus

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

proof_lines:
kidney cortex large isozyme
spleen small isozyme
lung small isozyme


organism: Homo sapiens

substrate_name: adenosine

proof_lines: 25°C, 50 mM Tris-HCl buffer, pH 7.4, enzyme concentration 1.5 nM

substrate: adenosine


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8IJA9 canonical sequence; L179H reconstructed after direct residue check confirmed canonical residue 179 is L. and applied mutation signature L179H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant L179H

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme L179H


organism: Schizosaccharomyces pombe

substrate_name: adenine

substrate: adenine


organism: Thermotoga maritima

sequence_source: UniProtKB reviewed accession Q9X034 canonical sequence; retained only as context because the accession EC annotation conflicts with selected EC 3.5.4.4.

assay_conditions_summary: pH 8; 303.15 K; buffer composition Primary measurement evidence: evidence location type: figure

column_label: Figure S3: UV spectra for the conversion of SAH, MTA, and adenosine to SIH, MTI, and inosine as catalyzed by Tm0936 and the associated plots for the measurement of the kinetic constants (Nature 2007 Supplementary Information, PDF page 18); kinetics panel titled 'Kinetic Parameters for Tm0936 with Adenosine at pH 8.0 and 30 oC'; parameter line 'kcat' = 2.3 s-1; parameter line 'Km' = 0.25 mM; parameter line 'kcat/Km' = 9.2 x 10^3 M-1s-1; parameter line 'Ki' = 21 mM (every value printed as a numeral with its standard deviation).

normalized_value_unit_evidence: kcat: printed Figure S3 panel line kcat = 2.3 s^-1; the printed unit s^-1 is already the export unit (this panel prints no min^-1 kinetic value), so no unit conversion applies and the paper value is 2.3 s^(-1); the exported value is 2.3 s^(-1). Km: printed Figure S3 panel line Km = 0.25 mM; the printed unit mM is already the export unit, so no unit conversion applies; the paper value is 0.25 mM; the exported value is 0.25 mM. kcat/Km: printed Figure S3 panel line kcat/Km = 9.2 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9.2 x 10^3 / 1000 = 9.2 s^(-1)*mM^(-1); the exported value is 9.2 s^(-1)*mM^(-1). Ki: printed Figure S3 panel line Ki = 21 mM; the catalog row stores no Ki value and this pass does not add one.

raw_value_unit_evidence: Figure S3, kinetics panel 'Kinetic Parameters for Tm0936 with Adenosine at pH 8.0 and 30 oC': kcat = 2.3 s^-1; Km = 0.25 mM; printed kcat/Km = 9.2 x 10^3 M^-1 s^-1; printed Ki = 21 mM.

row_label: Figure S3, kinetics panel titled 'Kinetic Parameters for Tm0936 with Adenosine at pH 8.0 and 30 oC'


normalized_value_unit_evidence: kcat: printed Figure S3 panel line kcat = 2.3 s^-1; the printed unit s^-1 is already the export unit (this panel prints no min^-1 kinetic value), so no unit conversion applies and the paper value is 2.3 s^(-1); the exported value is 2.3 s^(-1). Km: printed Figure S3 panel line Km = 0.25 mM; the printed unit mM is already the export unit, so no unit conversion applies; the paper value is 0.25 mM; the exported value is 0.25 mM. kcat/Km: printed Figure S3 panel line kcat/Km = 9.2 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9.2 x 10^3 / 1000 = 9.2 s^(-1)*mM^(-1); this catalog row stores no kcat_over_km value, so the printed efficiency line is carried as typed primary_reported provenance only and no ratio metric is compared. Ki: printed Figure S3 panel line Ki = 21 mM; the catalog row stores no Ki value and this pass does not add one.

table_label: Figure S3: UV spectra for the conversion of SAH, MTA, and adenosine to SIH, MTI, and inosine as catalyzed by Tm0936 and the associated plots for the measurement of the kinetic constants (Nature 2007 Supplementary Information, PDF page 18)


organism: Xenopus laevis

sequence_source: UniProtKB reviewed accession Q2VQV9 canonical sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q8IJA9 / ADA_PLAF7 direct REST+FASTA check, accessed 2026-06-03 and applied mutation signature T174A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant T174A

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme T174A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q8IJA9 / ADA_PLAF7 direct REST+FASTA check, accessed 2026-06-03 and applied mutation signature T174I to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant T174I

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme T174I


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q8IJA9 / ADA_PLAF7 direct REST+FASTA check, accessed 2026-06-03 and applied mutation signature D176M to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant D176M

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme D176M


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q8IJA9 / ADA_PLAF7 direct REST+FASTA check, accessed 2026-06-03 and applied mutation signature F136L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant F136L

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme F136L


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q8IJA9 / ADA_PLAF7 direct REST+FASTA check, accessed 2026-06-03 and applied mutation signature D176A/L179H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant D176A+L179H


sequence_source: UniProtKB reviewed entry Q8IJA9 / ADA_PLAF7 direct REST+FASTA check, accessed 2026-06-03

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


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q8IJA9 / ADA_PLAF7 direct REST+FASTA check, accessed 2026-06-03 and applied mutation signature D176A/L179A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme D176A/L179A


substrate_name: L-citrulline

substrate: L-citrulline


organism: Escherichia coli (strain K12)

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


organism: Gallus gallus

sequence: TPLWSLMQDLMM


substrate_name: adenosine (for adenosine phosphorylase activity)


substrate_name: adenosine (at 25 degrees Celsius and pH 5.5)


organism: Lutzomyia longipalpis


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

substrate_name: 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (at pH 4.5 and 40 degrees Celsius)

proof_lines: kcat is 13000 min(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate. kcat is 33300 min(-1) with syringaldazine as substrate (at pH 4.5 and 40 degrees Celsius).


proof_lines: kcat is 1450 min(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate. kcat is 21720 min(-1) with syringaldazine as substrate (at pH 4.5 and 40 degrees Celsius).

substrate: 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (at pH 4.5 and 40 degrees Celsius)


organism: Helicobacter pylori (strain ATCC 700392 / 26695)

proof_lines: kcat is 1101 min(-1) and 0.47 min(-1) with adenosine and adenine as substrate, respectively.


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

substrate_name: 5'-deoxyadenosine (at pH 9 and 60 degrees Celsius)

assay_conditions_summary: pH 9

proof_lines: kcat is 120000 sec(-1) for 5'-deoxyadenosine deamination. kcat is 160 sec(-1) for S-methyl-5'-thioadenosine deamination. kcat is 1300 sec(-1) for S-adenosyl-L-homocysteine deamination. kcat is 110 sec(-1) for adenosine deamination (at pH 9


organism: Plasmodium berghei (strain Anka)

substrate_name: adenosine (at pH 8)

proof_lines: kcat is 4.7 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.35 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:19728741).

substrate: adenosine (at pH 8)


organism: Plasmodium cynomolgi (strain B)

proof_lines: kcat is 5.3 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.31 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:19728741).


organism: Plasmodium falciparum (isolate 3D7)

proof_lines: kcat is 4.1 sec(-1) with adenosine as substrate (PubMed:31002765). kcat is 5.6 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 13.92 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:31002765). kcat is 5.8 sec(-1) with


organism: Plasmodium gallinaceum

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


organism: Plasmodium knowlesi

proof_lines: kcat is 6.8 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.51 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:19728741).


organism: Plasmodium vivax (strain Salvador I)

proof_lines: kcat is 1.8 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.13 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:19728741).


organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)

proof_lines: kcat is 11.5 sec(-1) with adenosine as substrate.


organism: Unknown prokaryotic organism

proof_lines: kcat is 18 sec(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate. kcat is 660 sec(-1) with syringaldazine as substrate. kcat is 1175 sec(-1) with 2,6-dimethoxyphenol as substrate (at pH 4.5 and 40 degrees Celsius).


organism: Homo sapiens

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


sequence_variant_note: Resolved canonical sequence from uniprot_canonical_sequence_plus_residue_substitution and applied mutation signature D8N to reconstruct the assayed variant sequence.


proof_lines: pH 7.4, temperature not specified in the publication


organism: Methanocaldococcus jannaschii

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

proof_lines: pH and temperature not specified in the publication, mutant enzyme Y136R


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


proof_lines: pH and temperature not specified in the publication, mutant enzyme E150R


organism: Mus musculus

sequence_variant_note: Resolved canonical sequence from uniprot_canonical_sequence_plus_residue_substitution and applied mutation signature E217G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant E217G


sequence_variant_note: Resolved canonical sequence from uniprot_canonical_sequence_plus_residue_substitution and applied mutation signature E217D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant E217D


organism: Escherichia coli


organism: Fasciola gigantica


organism: Gallus gallus


organism: Hyalomma dromedarii


organism: Kitasatospora aureofaciens


organism: Klebsiella sp.


organism: Argopecten irradians concentricus

substrate_name: 6-Chloropurine riboside

substrate: 6-Chloropurine riboside


organism: Aspergillus terricola


organism: Bacillus cereus


organism: Biomphalaria glabrata


organism: Camelus dromedarius


organism: Danio rerio

proof_lines:
membrane-bound ADA
soluble fraction


organism: Arabidopsis thaliana

sequence_source: UniProtKB direct lookup Q8LPL7

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


organism: Bos taurus

sequence_source: UniProtKB direct lookup P56658

proof_lines: pH 7.0, temperature not specified in the publication


wild_type_sequence: TPLWSLMQDLMM

sequence_source: UniProtKB direct lookup P84520


organism: Helicobacter pylori

sequence_source: UniProtKB direct lookup O25046


organism: Homo sapiens

sequence_source: UniProtKB direct lookup P00813

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

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme, wild-type enzyme (refolded)


sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup P00813 and applied mutation signature M155A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant M155A refolded

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme M155A (refolded)


sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup P00813 and applied mutation signature M155D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine deaminase(Enzyme) mutant M155D refolded


organism: Rattus norvegicus

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


organism: Streptomyces coelicolor

proof_lines: 37°C, pH not specified in the publication


organism: Streptomyces sp.

substrate_name: AMP

substrate: AMP


organism: Sus scrofa


organism: Trichomonas vaginalis

proof_lines: pH 7.5, 37°C, Vmax is 2.61 nmol NH3/min/mg protein


organism: Xenopus laevis


organism: Mus musculus


organism: Nocardioides sp.


organism: Plasmodium berghei

sequence_source: UniProtKB reviewed A0A509ALD0; adenosine deaminase from Plasmodium berghei strain Anka; EC 3.5.4.4 evidence cites PMID 19728741.

assay_conditions_summary: pH 8; buffer 100 mM Tris-HCl

proof_lines: wild type enzyme, in 100 mM Tris-HCl buffer (pH 8.0), temperature not specified in the publication


organism: Plasmodium cynomolgi

sequence_source: UniProtKB reviewed K6UCV4; adenosine deaminase from Plasmodium cynomolgi strain B; EC 3.5.4.4 evidence cites PMID 19728741.


organism: Plasmodium falciparum

sequence_source: UniProtKB reviewed Q8IJA9; adenosine deaminase from Plasmodium falciparum isolate 3D7; EC 3.5.4.4 evidence cites PMID 19728741.


organism: Plasmodium gallinaceum

sequence_source: UniProtKB A0A0K1SC59 canonical reviewed entry; EC 3.5.4.4 evidence cites PMID 19728741

column_label: Table 2. Kinetic constants for Plasmodium ADAs with adenosine and 5'-methylthioadenosine (MTA) as substrates, printed column heads Species | Adenosine: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1) | MTA: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1); Table 4. Kinetic and inhibition constants for PvADA-mutants, printed column heads Mutant | Adenosine: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1) | Coformycin: Ki (nM), Ki* (nM). Table 2, species row P. gallinaceum; adenosine column group; Km cell = 32 uM; kcat cell = 1.9 s^-1; kcat/Km cell = 5.9 x 10^4 M^-1 s^-1. captured primary segment: Table 2, adenosine column group, species row P. gallinaceum: Km 32 uM; kcat 1.9 s^-1; kcat/Km 5.9 x 10^4 M^-1 s^-1.

normalized_value_unit_evidence: Km: printed Table 2 cell 32 uM; 1 uM = 1/1000 mM, so 32 / 1000 = 0.032 mM; the export stores 32.0 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat: printed Table 2 cell 1.9 s^-1; the printed turnover column is already per second, so the cell is carried across unchanged as 1.9 s^-1; the export stores 1.9 s^-1, the same value. kcat/Km: printed Table 2 cell 5.9 x 10^4 under the printed unit row M^-1 s^-1, which is 59000.0 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 59000.0 / 1000 = 59.0 s^-1 mM^-1; the export stores 59000.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Table 2, species row P. gallinaceum, adenosine column group: Km = 32 uM; kcat = 1.9 s^-1; kcat/Km = 5.9 x 10^4 under the printed unit row M^-1 s^-1.

row_label: Table 2, species row P. gallinaceum


organism: Plasmodium knowlesi


organism: Plasmodium vivax

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5KE01 and applied mutation signature D172E to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic constants for Plasmodium ADAs with adenosine and 5'-methylthioadenosine (MTA) as substrates, printed column heads Species | Adenosine: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1) | MTA: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1); Table 4. Kinetic and inhibition constants for PvADA-mutants, printed column heads Mutant | Adenosine: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1) | Coformycin: Ki (nM), Ki* (nM). Table 4, mutant row PvADA-Glu172; adenosine column group; Km cell = 83 uM; kcat cell = 12.9 s^-1; kcat/Km cell = 1.5 x 10^5 M^-1 s^-1. captured primary segment: Table 4, adenosine column group, mutant row PvADA-Glu172: Km 83 uM; kcat 12.9 s^-1; kcat/Km 1.5 x 10^5 M^-1 s^-1.

normalized_value_unit_evidence: Km: printed Table 4 cell 83 uM; 1 uM = 1/1000 mM, so 83 / 1000 = 0.083 mM; the export stores 83.0 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat: printed Table 4 cell 12.9 s^-1; the printed turnover column is already per second, so the cell is carried across unchanged as 12.9 s^-1; the export stores 12.9 s^-1, the same value. kcat/Km: printed Table 4 cell 1.5 x 10^5 under the printed unit row M^-1 s^-1, which is 150000.0 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 150000.0 / 1000 = 150.0 s^-1 mM^-1; the export stores 150000.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Table 4, mutant row PvADA-Glu172, adenosine column group: Km = 83 uM; kcat = 12.9 s^-1; kcat/Km = 1.5 x 10^5 under the printed unit row M^-1 s^-1.

row_label: Table 4, mutant row PvADA-Glu172


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5KE01 and applied mutation signature D172A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; buffer 100 mM Tris-HCl

column_label: Table 2. Kinetic constants for Plasmodium ADAs with adenosine and 5'-methylthioadenosine (MTA) as substrates, printed column heads Species | Adenosine: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1) | MTA: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1); Table 4. Kinetic and inhibition constants for PvADA-mutants, printed column heads Mutant | Adenosine: Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1) | Coformycin: Ki (nM), Ki* (nM). Table 4, mutant row PvADA-Ala172; adenosine column group; Km cell = 104 uM; kcat cell = 14.0 s^-1; kcat/Km cell = 1.3 x 10^5 M^-1 s^-1. captured primary segment: Table 4, adenosine column group, mutant row PvADA-Ala172: Km 104 uM; kcat 14.0 s^-1; kcat/Km 1.3 x 10^5 M^-1 s^-1.

normalized_value_unit_evidence: Km: printed Table 4 cell 104 uM; 1 uM = 1/1000 mM, so 104 / 1000 = 0.104 mM; the export stores 104.0 mM, which is the printed micromolar cell carrying the millimolar label without conversion. kcat: printed Table 4 cell 14.0 s^-1; the printed turnover column is already per second, so the cell is carried across unchanged as 14.0 s^-1; the export stores 14.0 s^-1, the same value. kcat/Km: printed Table 4 cell 1.3 x 10^5 under the printed unit row M^-1 s^-1, which is 130000.0 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 130000.0 / 1000 = 130.0 s^-1 mM^-1; the export stores 130000.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without conversion.

raw_value_unit_evidence: Table 4, mutant row PvADA-Ala172, adenosine column group: Km = 104 uM; kcat = 14.0 s^-1; kcat/Km = 1.3 x 10^5 under the printed unit row M^-1 s^-1.

row_label: Table 4, mutant row PvADA-Ala172


assay_conditions_summary: pH 8; 310.15 K; buffer 100 mM Tris-HCl


organism: Plasmodium yoelii


organism: Saccharomyces cerevisiae

substrate: phosphoenolpyruvate


assay_conditions_summary: cofactor ATP

proof_lines: pH high (pH range:6-8.4), pH:12, PEP carboxylation direction

proof_lines: kinetic parameter in the PEP carboxylation direction

substrate: ADP


proof_lines: F216Y: kinetic parameter in the PEP carboxylation direction

proof_lines: F216Y: kinetic parameter in the PEP formation direction


proof_lines: wild type enzyme, in 100 mM MOPS buffer (pH 6.6), at 30°C

proof_lines: wild type enzyme, in 100 mM MOPS buffer (pH 7.0), at 30°C


assay_conditions_summary: pH 6.6; 303.15 K; buffer 100 mM MOPS

proof_lines: mutant enzyme K212M, in 100 mM MOPS buffer (pH 6.6), at 30°C


substrate_name: oxaloacetate

proof_lines: Km above 2.0 mM, mutant enzyme E284Q, in 100 mM MOPS buffer (pH 6.6), at 30°C

substrate: oxaloacetate


enzyme_display_name: deoxynucleoside kinase

organism: Drosophila melanogaster

substrate_name: thymidine

enzyme: deoxynucleoside kinase

substrate: thymidine


substrate_name: Thymidine; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9XZT6 canonical sequence plus selected source mutation signature and applied mutation signature F114Y to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: deoxynucleoside kinase(Enzyme) mutant F114Y

substrate: Thymidine; ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9XZT6 canonical sequence plus selected source mutation signature and applied mutation signature Q81E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9XZT6 canonical sequence


sequence_source: UniProtKB Q9XZT6 canonical sequence plus selected source mutation signature


proof_lines: recombinant N-terminally truncated mutant V84A/M88R, pH 7.6, 37°C

proof_lines: recombinant mutant V84A/M88R, pH 7.6, 37°C


proof_lines: uncompetitive versus 2-deoxythymidine, recombinant mutant N64D

proof_lines: competitive versus ATP, recombinant mutant N64D


proof_lines:
recombinant mutants N45D and N64D
mutant enzyme N45D/N64D


proof_lines:
recombinant mutant N45D
recombinant mutants N45D


proof_lines:
37°C, pH 7.5, mutant enzyme Q81N
pH 7.6, 37°C, recombinant mutant Q81N


organism: Anopheles gambiae

sequence_source: UniProtKB:Q86LB8 direct lookup


organism: Bombyx mori

substrate_name: ATP; Thymidine

sequence_source: UniProtKB:Q9BKL3 direct lookup

substrate: ATP; Thymidine


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:Q9XZT6 canonical sequence and applied mutation signature ΔC10 with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: deoxynucleoside kinase(Enzyme) mutant dNKdeltaC10


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:Q9XZT6 canonical sequence and applied mutation signature ΔC20 with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: deoxynucleoside kinase(Enzyme) mutant dNKdeltaC20


sequence_source: reconstructed from UniProtKB:Q9XZT6 canonical sequence

sequence_variant_note: Mutation signature ΔC30 could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: deoxynucleoside kinase(Enzyme) mutant dNKdeltaC30


sequence_source: UniProtKB:Q9XZT6 direct lookup

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines:
pH 8, 37°C
pH 7.8, 22°C, recombinant enzyme
Raw SKiD Env: Temp=22°C, pH=7.8


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:Q9XZT6 canonical sequence and applied mutation signature Q81N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: deoxynucleoside kinase(Enzyme) mutant Q81N


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:Q9XZT6 canonical sequence and applied mutation signature F114A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: deoxynucleoside kinase(Enzyme) mutant F114A


proof_lines: recombinant N-terminally truncated mutant M88R, pH 7.6, 37°C


proof_lines: recombinant mutant V84A/M88R/A110D, pH 7.6, 37°C


substrate_name: Dideoxycytidine

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: pH 7.6, 37°C, recombinant wild-type enzyme

substrate: Dideoxycytidine


sequence_variant_note: Resolved canonical sequence from UniProt Q9XZT6 canonical sequence with V84S reconstructed after direct residue check and applied mutation signature V84S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9XZT6 canonical sequence with V84M reconstructed after direct residue check and applied mutation signature V84M to reconstruct the assayed variant sequence.