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

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

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


enzyme_display_name: beta-lactamase

organism: Pseudomonas aeruginosa

substrate_name: H2O; Cephaloridine

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

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

km_unit: mM

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

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

mutation_type: substitution

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

enzyme: beta-lactamase

substrate: H2O; Cephaloridine


substrate_name: H2O; Penicillin G

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

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

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

substrate: H2O; Penicillin G


organism: Enterobacter cloacae

substrate_name: Nitrocefin; H2O

mutation_signature: Unknown

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

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

proof_lines: pH and temperature not specified in the publication

source_db: brenda

substrate: Nitrocefin; H2O


organism: Escherichia coli

substrate_name: H2O; Nitrocefin

km_display: Not reported

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

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

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

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

substrate: H2O; Nitrocefin


substrate_name: Penicillin G; H2O

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

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

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

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

substrate: Penicillin G; H2O


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


organism: Haemophilus ducreyi

substrate_name: Ampicillin; H2O

substrate: Ampicillin; H2O


organism: Klebsiella pneumoniae

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


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

proof_lines: pH 7.0, temperature not specified in the publication


organism: Mycobacterium tuberculosis

ki_unit: mM

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


organism: Serratia marcescens

substrate_name: H2O; Ampicillin

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

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

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

substrate: H2O; Ampicillin


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

sequence_source: UniProtKB REST accession P52699 canonical sequence

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

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

source_databases_merged: sabio_rk brenda skid


organism: Shewanella livingstonensis

substrate_name: Amoxicillin; H2O

kcat_display: Not reported

sequence_source: UniProtKB REST accession Q53BU1 canonical sequence

substrate: Amoxicillin; H2O


organism: Staphylococcus aureus

sequence_source: UniProtKB REST accession P00807 canonical sequence


organism: Stenotrophomonas maltophilia

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

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


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


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


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


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


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


organism: Proteus vulgaris


substrate_name: Cefdinir; H2O

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

substrate: Cefdinir; H2O


substrate_name: H2O; Cefdinir

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

substrate: H2O; Cefdinir


enzyme_display_name: putrescine N-methyltransferase

organism: Calystegia sepium

substrate_name: Putrescine

source_db: oed

verification_status: unverified

source_license: CC BY 4.0

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

smiles: NCCCCN

data_origin: experimental

enzyme: putrescine N-methyltransferase

substrate: Putrescine

status: unverified

source: oed


organism: Datura stramonium

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


organism: Solanum lycopersicum

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


enzyme_display_name: glycine N-benzoyltransferase

organism: Bos taurus

substrate_name: benzoyl-CoA

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

enzyme: glycine N-benzoyltransferase

substrate: benzoyl-CoA

source: brenda


substrate_name: glycine

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

substrate: glycine


organism: Homo sapiens

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA


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


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


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


substrate_name: Glycine; Benzoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: Glycine; Benzoyl-CoA


organism: Mus musculus

substrate_name: Glycine methyl ester

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: pH 8.0, temperature not specified in the publication

substrate: Glycine methyl ester


enzyme_display_name: glutamate carboxypeptidase

organism: Acinetobacter sp. 263903-1

substrate_name: methotrexate

enzyme: glutamate carboxypeptidase

substrate: methotrexate


organism: Pseudomonas sp.

substrate_name: Folate; H2O

sequence_source: UniProtKB:P06621 direct FASTA lookup

substrate: Folate; H2O


organism: Pseudomonas sp. RS-16

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


enzyme_display_name: Carboxypeptidase G2

sequence_source: UniProtKB P06621 canonical sequence

enzyme: Carboxypeptidase G2


substrate_name: folate; methotrexate

source_db: brenda;skid

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

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

source_databases_merged: brenda skid

substrate: folate; methotrexate

source: brenda;skid


source_db: uniprot

source: uniprot


organism: Stutzerimonas stutzeri

substrate_name: pteroylglutamic acid

substrate: pteroylglutamic acid


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


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

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

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


organism: Ovis aries


organism: Cohnella sp. A01

substrate_name: folate

substrate: folate


organism: Leishmania major

substrate_name: Methotrexate; H2O

substrate: Methotrexate; H2O


proof_lines: pH and temperature not specified in the publication


organism: Pseudomonas sp. RS16

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


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

substrate_name: O-acetyl-L-homoserine

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

substrate: O-acetyl-L-homoserine


organism: [Brevibacterium] flavum


organism: Corynebacterium acetophilum

proof_lines:
O-alkylhomoserine synthesis
O-acetylhomoserine sulfhydrylation


organism: Geobacillus stearothermophilus


organism: Neurospora crassa


substrate_name: O-acetyl-L-serine

substrate: O-acetyl-L-serine


organism: Saccharomyces cerevisiae

substrate_name: Unknown

substrate: Unknown


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


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


organism: Schizosaccharomyces pombe


enzyme_display_name: DNA-directed RNA polymerase

organism: Escherichia phage T7

substrate_name: ATP

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

assay_conditions_summary: pH 7.9; 310.15 K; cofactor ATP

enzyme: DNA-directed RNA polymerase

substrate: ATP


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


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


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


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

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


substrate_name: dGTP

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

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

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

substrate: dGTP


substrate_name: rGTP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

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

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

substrate: rGTP


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

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

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


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

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

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

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


organism: Lathyrus oleraceus

substrate_name: GTP

substrate: GTP


organism: Fusarium oxysporum

substrate_name: CDP-choline

substrate: CDP-choline


organism: Homo sapiens

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

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


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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

verification_status: corrected

assay_conditions_summary: buffer potassium phosphate

status: corrected


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)


organism: Calystegia sepium

substrate_name: Putrescine; S-Adenosyl-L-methionine

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

proof_lines:
isoenzyme PMT1
isoenzyme PMT2

substrate: Putrescine; S-Adenosyl-L-methionine


organism: Unknown

substrate_name: putrescine

substrate: putrescine


organism: Clostridioides difficile

substrate_name: methanethiol

kcat_over_km_origin: calculated

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

smiles: CS

substrate: methanethiol


substrate_name: hydrogen sulfide

smiles: S

substrate: hydrogen sulfide


organism: Thermus thermophilus


proof_lines: at a fixed sulfide concentration of 1 mM


organism: Bacillus subtilis

substrate_name: RNA; ATP

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

assay_conditions_summary: cofactor ATP

substrate: RNA; ATP


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

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

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


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

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


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


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


organism: Nicotiana tabacum

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Solanum dulcamara


organism: Escherichia coli

substrate_name: ATP; RNA

substrate: ATP; RNA


organism: Phytophthora infestans


organism: Rattus norvegicus


organism: Ricinus communis


organism: Secale cereale


enzyme_display_name: legumain

organism: Canavalia ensiformis

assay_conditions_summary: pH 5

enzyme: legumain


organism: Bacillus subtilis (strain 168)

substrate_name: ATP (at 10 degrees Celsius)

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

substrate: ATP (at 10 degrees Celsius)


organism: Homo sapiens


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Xenopus laevis


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


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


organism: Saccharum sp.

substrate_name: Unknown

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

proof_lines: pH and temperature not specified in the publication


organism: Hordeum vulgare

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

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


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

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


organism: Schistosoma mansoni


organism: Sus scrofa


organism: Calystegia sepium

substrate_name: S-Adenosyl-L-methionine; Putrescine

substrate: S-Adenosyl-L-methionine; Putrescine


organism: Datura innoxia


organism: Datura inoxia


organism: Datura stramonium

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

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


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

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


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


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


organism: Hyoscyamus niger


organism: Physalis divaricata


organism: Solanum dulcamara


organism: Solanum lycopersicum


organism: Solanum tuberosum


organism: Bos taurus


organism: Dictyocaulus viviparus


enzyme_display_name: guanidinoacetate N-methyltransferase

organism: Rattus norvegicus

substrate_name: S-Adenosyl-L-methionine

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

enzyme: guanidinoacetate N-methyltransferase

substrate: S-Adenosyl-L-methionine


substrate_name: Guanidinoacetate

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

substrate: Guanidinoacetate


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


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


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


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


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


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


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


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


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


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


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


organism: Oryctolagus cuniculus

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

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

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


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


enzyme_display_name: O-phosphoserine sulfhydrylase

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

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

enzyme: O-phosphoserine sulfhydrylase


organism: Xenopus laevis

substrate_name: pyridylaminated Man3GlcNAc2

substrate: pyridylaminated Man3GlcNAc2


organism: Arabidopsis thaliana

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


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

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

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


organism: Acer pseudoplatanus

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


substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


organism: Cricetulus griseus


organism: Homo sapiens


proof_lines:
recombinant catalytic fragment
transferase A
transferase B


organism: Sus scrofa


organism: Aeropyrum pernix

substrate_name: O-acetyl-L-serine

substrate: O-acetyl-L-serine


organism: Mycobacterium tuberculosis

proof_lines: formation of the aminoacrylate intermediate


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

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


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


organism: Nicotiana tabacum

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

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


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

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


substrate_name: hydrogen sulfide

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

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

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


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


substrate_name: O-phospho-L-serine

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

substrate: O-phospho-L-serine


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

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


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


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

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


enzyme_display_name: cGMP-dependent protein kinase

organism: Caenorhabditis elegans

enzyme: cGMP-dependent protein kinase

substrate: Unknown


organism: Eimeria tenella

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

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

assay_conditions_summary: pH 7; cofactor ATP

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


organism: Toxoplasma gondii

substrate_name: ATP

substrate: ATP


substrate_name: ATP; Kemptide

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8MMZ7 direct FASTA; variant reconstructed from UniProt mutagenesis feature and PMID 11897122 and applied mutation signature M103A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cGMP-dependent protein kinase(Enzyme) mutant M103A C-terminal FLAG-epitope

substrate: ATP; Kemptide


substrate_name: Kemptide; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8MMZ7 direct FASTA; variant reconstructed from UniProt mutagenesis feature and PMID 11897122 and applied mutation signature M1A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cGMP-dependent protein kinase(Enzyme) mutant M1A C-terminal FLAG-epitope

substrate: Kemptide; ATP


sequence_source: UniProtKB:Q8MMZ7 direct FASTA


organism: Bos taurus

substrate_name: septin 3 peptide 86-98

proof_lines:
pH 7.4, 30°C, PKG-I
cGKI beta
cGKI alpha

substrate: septin 3 peptide 86-98


substrate_name: RKRSRAE

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

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines: pH 7.4, 30°C, recombinant PKG Ibeta leucine zipper mutant

substrate: RKRSRAE


mutation_signature: Δ1

mutation_type: deletion

proof_lines: pH 7.4, 30°C, recombinant PKG Ibeta deletion mutant DELTA1-52


proof_lines: pH 7.4, 30°C, recombinant wild-type PKG Ibeta


substrate_name: human serotonin transporter T267D

proof_lines: cGKI cGKII cGKIalpha

substrate: human serotonin transporter T267D


substrate_name: Peptide; ATP

sequence_source: UniProtKB:O76360 REST lookup 2026-06-22

substrate: Peptide; ATP


sequence_source: UniProtKB:Q8MMZ8 REST lookup 2026-06-22


substrate_name: ATP; Sox-AKT-tide peptide

sequence_source: UniProtKB:Q13976 REST lookup 2026-06-22

substrate: ATP; Sox-AKT-tide peptide


enzyme_display_name: 5-oxoprolinase (ATP-hydrolyzing)

organism: Unknown

enzyme: 5-oxoprolinase (ATP-hydrolyzing)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Rattus norvegicus

substrate_name: S-adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 direct FASTA retrieved 2026-06-22; mutation applied with literature-to-P10868 offset +1 and applied mutation signature Y221F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: S-adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 direct FASTA retrieved 2026-06-22; mutation applied with literature-to-P10868 offset +1 and applied mutation signature E45D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P10868 direct FASTA retrieved 2026-06-22

proof_lines:
wild-type
wild type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 direct FASTA retrieved 2026-06-22; mutation applied with literature-to-P10868 offset +1 and applied mutation signature E45Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 direct FASTA retrieved 2026-06-22; mutation applied with literature-to-P10868 offset +1 and applied mutation signature D129N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: guanidinoacetate N-methyltransferase(Enzyme) mutant D129N


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 direct FASTA retrieved 2026-06-22; mutation applied with literature-to-P10868 offset +1 and applied mutation signature T135A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: guanidinoacetate N-methyltransferase(Enzyme) mutant T135A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 direct FASTA retrieved 2026-06-22; mutation applied with literature-to-P10868 offset +1 and applied mutation signature Y133F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: guanidinoacetate N-methyltransferase(Enzyme) mutant Y133F


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 direct FASTA retrieved 2026-06-22; mutation applied with literature-to-P10868 offset +1 and applied mutation signature Y136F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: guanidinoacetate N-methyltransferase(Enzyme) mutant Y136F


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 direct FASTA retrieved 2026-06-22; mutation applied with literature-to-P10868 offset +1 and applied mutation signature D134N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: guanidinoacetate N-methyltransferase(Enzyme) mutant D134N


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

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 direct FASTA retrieved 2026-06-22; mutation applied with literature-to-P10868 offset +1 and applied mutation signature D129A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: guanidinoacetate N-methyltransferase(Enzyme) mutant D129A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10868 direct FASTA retrieved 2026-06-22; mutation applied with literature-to-P10868 offset +1 and applied mutation signature D134E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: guanidinoacetate N-methyltransferase(Enzyme) mutant D134E


organism: Mus musculus

substrate_name: H2O; ATP; 5-Oxo-L-proline

sequence_source: UniProtKB:Q8K010 direct FASTA retrieved 2026-06-22

substrate: H2O; ATP; 5-Oxo-L-proline


organism: Saccharomyces cerevisiae

substrate_name: H2O; 5-Oxoproline; ATP

sequence_source: UniProtKB:P28273 direct FASTA retrieved 2026-06-22

substrate: H2O; 5-Oxoproline; ATP


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

proof_lines:
native enzyme
recombinant enzyme


substrate_name: Guanidinoacetate

substrate: Guanidinoacetate


organism: Plasmodium falciparum

substrate_name: GRTGRRNSI

proof_lines: pH 7.4, 37°C, recombinant FLAG-tagged enzyme

substrate: GRTGRRNSI


organism: Alcaligenes sp.


organism: Paecilomyces variotii


organism: Pseudomonas putida


organism: Pseudomonas sp.


proof_lines:
without 5-oxoproline
initial Km in presence of GTP
initial Km in presence of ITP


organism: Sus scrofa


organism: Triticum aestivum


enzyme_display_name: N-acetylhexosamine 1-kinase

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

substrate_name: GlcNAc

proof_lines: kcat is 1.21 sec(-1) for GlcNAc. kcat is 0.752 sec(-1) for GalNAc.

enzyme: N-acetylhexosamine 1-kinase

substrate: GlcNAc


organism: Bifidobacterium longum

substrate_name: N-acetyl-alpha-D-galactosamine

sequence_source: UniProtKB reviewed accession E8MF12 direct REST/FASTA lookup

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP

proof_lines: cosubstrate: N-acetyl-alpha-D-glucosamine, pH 8.5, 30°C

substrate: N-acetyl-alpha-D-galactosamine


substrate_name: N-acetyl-D-glucosamine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession E8MF12 direct REST/FASTA lookup plus selected-row mutation signature K210A and applied mutation signature K210A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 37°C, recombinant mutant K210A, at 5.0 mM MgCl2

substrate: N-acetyl-D-glucosamine


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession E8MF12 direct REST/FASTA lookup plus selected-row mutation signature N213A and applied mutation signature N213A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 37°C, recombinant mutant N213A at 50 mM MgCl2

proof_lines: pH 8.0, 37°C, recombinant mutant N213A at 5.0 mM MgCl2


proof_lines: pH 8.0, 37°C, recombinant wild-type enzyme, at 5.0 mM MgCl2


substrate_name: myelin basic protein

proof_lines:
epidermal growth factor activated cells
isozyme beta
isozyme alpha

substrate: myelin basic protein


substrate_name: N-acetyl-alpha-D-glucosamine

proof_lines: cosubstrate N-acetyl-alpha-D-glucosamine, pH 8.0, 37°C

proof_lines: cosubstrate N-acetyl-alpha-D-galactosamine, pH 8.0, 37°C

substrate: N-acetyl-alpha-D-glucosamine


organism: Bifidobacterium longum subsp. infantis

substrate_name: ATP

substrate: ATP


organism: Caenorhabditis elegans

substrate_name: ATP; Peptide

sequence_source: UniProtKB canonical sequence Q9TXJ0 (CMK1_CAEEL); REST lookup 2026-06-22

substrate: ATP; Peptide


organism: Homo sapiens

sequence_source: UniProtKB canonical sequence Q9UQM7 (KCC2A_HUMAN); REST lookup 2026-06-22

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

proof_lines:
pH 7.6, 25°C, isoenzyme CaMK IIalpha
Raw SKiD Env: Temp=25°C, pH=7.6


sequence_source: UniProtKB canonical sequence Q13555 (KCC2G_HUMAN); REST lookup 2026-06-22

proof_lines:
pH 7.6, 25°C, isoenzyme CaMK IIgamma
Raw SKiD Env: Temp=25°C, pH=7.6


sequence_source: UniProtKB canonical sequence Q13554 (KCC2B_HUMAN); REST lookup 2026-06-22

proof_lines:
pH 7.6, 25°C, isoenzyme CaMK IIbeta
Raw SKiD Env: Temp=25°C, pH=7.6


sequence_source: UniProtKB canonical sequence Q13557 (KCC2D_HUMAN); REST lookup 2026-06-22

proof_lines:
pH 7.6, 25°C, isoenzyme CaMK IIdelta
Raw SKiD Env: Temp=25°C, pH=7.6


organism: Nicotiana tabacum

substrate_name: histone IIIS

substrate: histone IIIS


substrate_name: syntide-2 (when cmk-1 is not phosphorylated on Thr-179)

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


enzyme_display_name: phosphoinositide 5-phosphatase

organism: Arabidopsis thaliana

enzyme: phosphoinositide 5-phosphatase


substrate_name: PtdIns(4,5)P2 (at pH 7.0 and 22 degrees Celsius)


substrate_name: phosphatidylinositol 4,5-bisphosphate

substrate: phosphatidylinositol 4,5-bisphosphate


organism: Rattus norvegicus


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

substrate_name: Ins(1,4,5)P3 (at pH 7.4 and 30 degrees Celsius)


organism: Schizosaccharomyces pombe


substrate_name: Inositol 2,4,5-trisphosphate

substrate: Inositol 2,4,5-trisphosphate


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_rest_accession_O43001 and applied mutation signature E597Q to reconstruct the assayed variant sequence.


substrate_name: 4-Nitrophenyl phosphate

substrate: 4-Nitrophenyl phosphate


substrate_name: 3-O-Methylfluorescein phosphate

substrate: 3-O-Methylfluorescein phosphate


substrate_name: D-myo-Inositol 1,4,5-trisphosphate

substrate: D-myo-Inositol 1,4,5-trisphosphate


substrate_name: Inositol 4,5-bisphosphate

substrate: Inositol 4,5-bisphosphate


enzyme_display_name: bromide peroxidase

organism: Corallina officinalis

sequence_variant_note: Resolved canonical sequence from UniProt Q8LLW7 canonical sequence plus UniProt PubMed 12121762 H480A mutagenesis feature and applied mutation signature H480A to reconstruct the assayed variant sequence.

proof_lines:
pH 6.5, mutant enzyme H480A
mutant enzyme H480A

enzyme: bromide peroxidase


sequence_source: UniProt Q8LLW7 reviewed canonical sequence

proof_lines:
pH 6.5, native enzyme
pH 6.5, recombinant enzyme
recombinant enzyme


organism: Gracilaria firma

substrate_name: Br-

sequence_variant_note: Resolved canonical sequence from UniProt L7YCT6 canonical sequence with source mutation signature R379F and applied mutation signature R379F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7

proof_lines: mutant R379F, pH 7.0, temperature not specified in the publication

substrate: Br-


substrate_name: I-

sequence_source: UniProt L7YCT6 canonical sequence

proof_lines: wild-type, pH 7.0, temperature not specified in the publication

substrate: I-


sequence_variant_note: Resolved canonical sequence from UniProt L7YCT6 canonical sequence with source mutation signature R379H and applied mutation signature R379H to reconstruct the assayed variant sequence.

proof_lines: mutant R379H, pH 7.0, temperature not specified in the publication


organism: Leptoxyphium fumago

substrate_name: estrone

sequence_source: UniProt P04963 reviewed canonical sequence

assay_conditions_summary: pH 3

proof_lines: with Cl-, pH 3.0, temperature not specified in the publication

proof_lines: with Br-, pH 3.0, temperature not specified in the publication

substrate: estrone


organism: Pseudomonas fluorescens

substrate_name: H2O2; Br-; Monochlorodimedone

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

proof_lines: SABIO-RK modifier species: bromide peroxidase(Enzyme) mutant L29P C-terminal His6-tagged

substrate: H2O2; Br-; Monochlorodimedone


substrate_name: Br-; Monochlorodimedone; H2O2

proof_lines: SABIO-RK modifier species: bromide peroxidase(Enzyme) mutant F227I C-terminal His6-tagged

substrate: Br-; Monochlorodimedone; H2O2


substrate_name: Br-; H2O2; Monochlorodimedone

proof_lines: SABIO-RK modifier species: bromide peroxidase(Enzyme) mutant M95T C-terminal His6-tagged

substrate: Br-; H2O2; Monochlorodimedone


substrate_name: Monochlorodimedone; Br-; H2O2

proof_lines: SABIO-RK modifier species: bromide peroxidase(Enzyme) mutant D99E C-terminal His6-tagged

substrate: Monochlorodimedone; Br-; H2O2


proof_lines: SABIO-RK modifier species: bromide peroxidase(Enzyme) mutant Y69M C-terminal His6-tagged


proof_lines: SABIO-RK modifier species: bromide peroxidase(Enzyme) mutant T122P C-terminal His6-tagged


organism: Ascophyllum nodosum

substrate_name: Unknown

sequence_source: UniProtKB:P81701 reviewed direct EC+organism lookup

substrate: Unknown


sequence_source: UniProtKB:Q8LLW7 reviewed direct EC+organism lookup


organism: Ecklonia cava subsp. stolonifera


organism: Kappaphycus alvarezii


organism: Kitasatospora aureofaciens


organism: Laurencia nipponica

proof_lines:
isoform VBPO2, at pH 6.0 and 25°C
isoform VBPO1, at pH 6.0 and 25°C


organism: Streptomyces griseus

proof_lines:
nonhaem-type bromoperoxidase BPO 3
nonhaem-type bromoperoxidase BPO 1a


organism: Candida albicans

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP


organism: Gallus gallus

substrate_name: ATP

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

substrate: ATP


organism: Homo sapiens

proof_lines: wild type enzyme, with GST-tagged GluN2A as cosubstrate at pH 8.0 and 30°C

proof_lines: wild type enzyme, with GST-tagged GluN2B as cosubstrate, at pH 8.0 and 30°C


proof_lines: mutant enzyme E60G, with GST-tagged GluN2B as cosubstrate, at pH 8.0 and 30°C

proof_lines: mutant enzyme E60G, with GST-tagged GluN2A as cosubstrate at pH 8.0 and 30°C


enzyme_display_name: receptor protein-tyrosine kinase

organism: Arabidopsis thaliana

enzyme: receptor protein-tyrosine kinase


proof_lines: kcat is 0.026 sec(-1) with 1D-myo-inositol 1,4,5-trisphosphate.


proof_lines: kcat is 4.8 sec(-1) with 1D-myo-inositol 1,4,5-trisphosphate.


proof_lines: kcat is 30.6 sec(-1) with 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) as substrate. kcat is 85.3 sec(-1) with 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) as substrate with Mg(2+). kca


substrate_name: 1D-myo-inositol 1,4,5-trisphosphate

proof_lines: kcat is 6.5 sec(-1) with D-myo-inositol 1,4,5-trisphosphate.

substrate: 1D-myo-inositol 1,4,5-trisphosphate


proof_lines: kcat is 26 sec(-1) with 1D-myo-inositol 1,4,5-trisphosphate.


sequence_source: UniProtKB reviewed accession P04626 via UniProt REST TSV


substrate_name: Ac-DYFGW-NHMe

sequence_source: UniProtKB reviewed accession P08069 via UniProt REST TSV

substrate: Ac-DYFGW-NHMe


sequence_source: UniProtKB reviewed accession P00533 via UniProt REST TSV

proof_lines: pH and temperature not specified in the publication


organism: Adeno-associated virus

substrate_name: Protein tyrosine; ATP

substrate: Protein tyrosine; ATP


organism: Avian encephalomyelitis virus


organism: Avian erythroblastosis virus

substrate_name: ATP; Protein tyrosine

substrate: ATP; Protein tyrosine


organism: Caenorhabditis elegans

substrate_name: ATP (in the presence of Mg(2+) at 20 degrees Celsius)

proof_lines: Autophosphorylation gives similar KM values for ATP.


enzyme_display_name: salicylate decarboxylase

organism: Cutaneotrichosporon moniliiforme

substrate_name: salicylate (at 40 degrees Celsius and pH 5.5)

enzyme: salicylate decarboxylase


substrate_name: ginkgolic acid C15:1

sequence_source: UniProtKB:P0CT50 direct REST FASTA

proof_lines: pH not specified in the publication, 40°C

substrate: ginkgolic acid C15:1


substrate_name: salicylate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CT50 canonical sequence with selected-batch mutation_signature P191G applied and applied mutation signature P191G to reconstruct the assayed variant sequence.

substrate: salicylate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CT50 canonical sequence with selected-batch mutation_signature Y64T/P191G/F195V/E302D applied and applied mutation signature Y64T/P191G/F195V/E302D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CT50 canonical sequence with selected-batch mutation_signature P191G/F195V applied and applied mutation signature P191G/F195V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CT50 canonical sequence with selected-batch mutation_signature Y64T/F195V/E302D applied and applied mutation signature Y64T/F195V/E302D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CT50 canonical sequence with selected-batch mutation_signature Y64T/P191G/E302D applied and applied mutation signature Y64T/P191G/E302D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CT50 canonical sequence with selected-batch mutation_signature Y64T applied and applied mutation signature Y64T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CT50 canonical sequence with selected-batch mutation_signature E302D applied and applied mutation signature E302D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CT50 canonical sequence with selected-batch mutation_signature F195V applied and applied mutation signature F195V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CT50 canonical sequence with selected-batch mutation_signature Y64T/P191G/F195V applied and applied mutation signature Y64T/P191G/F195V to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CT50 canonical sequence with selected-batch mutation_signature P191G/E302D applied and applied mutation signature P191G/E302D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CT50 canonical sequence with selected-batch mutation_signature P191A applied and applied mutation signature P191A to reconstruct the assayed variant sequence.


substrate_name: phenol

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

substrate: phenol


enzyme_display_name: alkylglycerol monooxygenase

organism: Unknown

enzyme: alkylglycerol monooxygenase


enzyme_display_name: D-threonine aldolase

organism: Arthrobacter sp.

substrate_name: D-allo-threonine

sequence_source: UniProtKB reviewed accession O82872 (DTA_ARTSP), Arthrobacter sp DK-38; sequence version 1; references PMID 9346293 and PMID 9642221.

enzyme: D-threonine aldolase

substrate: D-allo-threonine


organism: Delftia acidovorans

substrate_name: 4-methylsulfonyl benzaldehyde

proof_lines:
pH 7.5, 25°C, solvent: water
pH 7.5, 25°C, ionic solvent

substrate: 4-methylsulfonyl benzaldehyde


organism: Pseudomonas sp.

substrate_name: D-threonine

proof_lines: pH 8.0, temperature not specified in the publication

substrate: D-threonine


organism: Xanthomonas oryzae


organism: Achromobacter xylosoxidans


sequence_source: UniProtKB reviewed accession O82872 direct lookup

proof_lines:
pH 8.0, 30°C, with Mn2+
pH 8.0, 30°C, without Mn2+


organism: Chlamydomonas reinhardtii

substrate_name: D-threo-phenylserine

sequence_source: UniProtKB unreviewed accession A0A1C9ZZ39 direct lookup

substrate: D-threo-phenylserine


substrate_name: D-Threonine

substrate: D-Threonine


organism: Delftia sp.


organism: Arthrobacter sp

substrate_name: D-threonine (at pH 7.5, in the presence of 0.5 mM MnCl(2))

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


proof_lines: measured in CHO cells after transfection, pH not specified in the publication, 37°C


substrate_name: tetrahydrobiopterin

substrate: tetrahydrobiopterin


organism: Rattus norvegicus

substrate_name: RS-3-(1-hexadecyloxy)propan-1-ol; RS-3-hexadecyloxypropane-1,2-diol; RS-batyl alcohol; tetrahydropterin cofactors

proof_lines: with 6-methyl-5,6,7,8-tetrahydropterin as cofactor

proof_lines: with 6,7-dimethyl-5,6,7,8-tetrahydropterin as cofactor


organism: Cavia porcellus


organism: Crithidia fasciculata


organism: Homo sapiens

substrate_name: 1-Phosphatidyl-D-myo-inositol 4,5-bisphosphate; H2O; inositol phosphate products

source_db: sabio_rk; brenda

source: sabio_rk; brenda


organism: Oryctolagus cuniculus


organism: Rhodnius prolixus

substrate_name: 1D-myo-inositol 1,4,5-trisphosphate


organism: Schizosaccharomyces pombe


organism: Trypanosoma brucei

proof_lines: mutant D360A/N362A, pH not specified in the publication, temperature not specified in the publication


substrate_name: 1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate; 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate

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


sequence_source: UniProtKB reviewed accession Q6ZNB7 (ALKMO_HUMAN)


organism: Arabidopsis thaliana

sequence_source: UniProtKB reviewed accession Q9SKB7 (IP5PE_ARATH)


sequence_source: UniProtKB reviewed accession P32019 (I5P2_HUMAN)


substrate_name: D-myo-Inositol 1,4,5-trisphosphate; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O43001 canonical sequence with E597Q reconstructed from UniProt mutagenesis evidence for PMID 15316017 and applied mutation signature E597Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphoinositide 5-phosphatase(Enzyme) mutant E597Q

substrate: D-myo-Inositol 1,4,5-trisphosphate; H2O


sequence_source: UniProtKB reviewed accession O43001 (SYJ1_SCHPO)


substrate_name: 1-O pyrenedecyl glycerol (in presence of ALDH3A2)


enzyme_display_name: glycerophosphocholine phosphodiesterase

organism: Rattus sp.

substrate_name: sn-glycero 3-phosphocholine

enzyme: glycerophosphocholine phosphodiesterase

substrate: sn-glycero 3-phosphocholine


organism: Serratia plymuthica

substrate_name: glycerophosphoethanolamine

substrate: glycerophosphoethanolamine


enzyme_display_name: 17alpha-hydroxyprogesterone deacetylase

sequence_source: UniProtKB:P05093 direct accession lookup; reviewed Swiss-Prot human CYP17A1

enzyme: 17alpha-hydroxyprogesterone deacetylase


substrate_name: progesterone

substrate: progesterone


substrate_name: pregnenolone

substrate: pregnenolone


organism: Escherichia coli

substrate_name: sn-Glycero-3-phosphocholine; H2O

sequence_source: UniProtKB:P09394 direct accession lookup; reviewed Swiss-Prot E. coli K-12 GlpQ

substrate: sn-Glycero-3-phosphocholine; H2O


organism: Thermocrispum sp. RD004668

substrate_name: choline lysoplasmalogen

sequence_source: UniProtKB:A0A0U4VTN7 checked; sequence not accepted for EC 3.1.4.2 because PMID 27833852 assigns the enzyme to EC 3.1.4.4

substrate: choline lysoplasmalogen


organism: Bos taurus

substrate_name: H2O; sn-Glycero-3-phosphocholine

substrate: H2O; sn-Glycero-3-phosphocholine


organism: Daucus carota

substrate_name: Unknown

substrate: Unknown


organism: Doryteuthis pealeii


substrate_name: sn-glycero 3-phosphorylcholine

proof_lines: addition of Ca2+ decreases Km and increases Vmax.

substrate: sn-glycero 3-phosphorylcholine


organism: Klebsiella aerogenes

substrate_name: 4-nitrophenyl ethylphosphonate

substrate: 4-nitrophenyl ethylphosphonate


organism: Oryza sativa


organism: Rattus norvegicus


substrate_name: progesterone (17-alpha hydroxylation)

sequence_source: source_record; direct UniProt REST P05093 FASTA cross-check

proof_lines: kcat is 1.01 min(-1) with progesterone as substrate. kcat is 0.39 min(-1) with pregnenolone as substrate. kcat is 0.24 min(-1) with 17alpha-hydroxypregnenolone as substrate.

substrate: progesterone (17-alpha hydroxylation)


enzyme_display_name: flavonol synthase

substrate_name: dihydroquercetin

enzyme: flavonol synthase

substrate: dihydroquercetin


organism: Malus domestica

substrate_name: dihydrokaempferol

proof_lines: in 0.1 M K2HPO4/KH2PO4 (0.6 M sorbitol, 0.4% Na-ascorbate, pH 7.25), 50 nmol 2-oxoglutarate and 10 nmol FeSO4 hydrate at 30°C

proof_lines: in 0.1 M K2HPO4/KH2PO4 (0.6 M sorbitol, 0.4% Na-ascorbate, pH 7.25) with 0.095 nmol dihydrokaempferol, 50 nmol 2-oxoglutarate and 10 nmol FeSO4 hydrate at 30°C

substrate: dihydrokaempferol


organism: Populus deltoides

assay_conditions_summary: pH 8; 310.15 K; buffer 10 mM Tris/HCl

proof_lines: in 10 mM Tris/HCl buffer (pH 8.0), at 37°C


organism: Pyrus communis


organism: Zea mays

proof_lines: recombinant FLS1, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: benzoin aldolase

organism: Pseudomonas fluorescens

substrate_name: Benzoin

proof_lines: mutant enzyme F484I, in the presence of 15% (v/v) PEG-400, in 50 mM Tris at 30°C and pH 7.5

enzyme: benzoin aldolase

substrate: Benzoin


proof_lines: mutant enzyme H286A, in the presence of 15% (v/v) PEG-400, in 50 mM Tris at 30°C and pH 7.5


proof_lines: mutant enzyme A480I, in the presence of 15% (v/v) PEG-400, in 50 mM Tris at 30°C and pH 7.5


proof_lines: mutant enzyme A28S, in the presence of 15% (v/v) PEG-400, in 50 mM Tris at 30°C and pH 7.5


proof_lines: wild type enzyme, in the presence of 15% (v/v) PEG-400, in 50 mM Tris at 30°C and pH 7.5


assay_conditions_summary: pH 8; 293.15 K; buffer 50 mM potassium phosphate

proof_lines: Michaelis constant for first binding substrate, mechanistic model


organism: Rhodococcus erythropolis

substrate_name: benzaldehyde

substrate: benzaldehyde


sequence_source: Direct UniProtKB JSON/FASTA lookup for P51853


substrate_name: Benzaldehyde

substrate: Benzaldehyde


organism: Albuca bracteata

sequence_source: UniProtKB:A0A482LTA5 direct exact-accession lookup

proof_lines:
pH 6.0, 20°C
isoform FLS1, at pH 6.0 and 20°C


sequence_source: UniProtKB:A0A482LVU5 direct exact-accession lookup

proof_lines:
pH 6.0, 20°C
isoform FLS2, at pH 6.0 and 20°C


organism: Arabidopsis thaliana

substrate_name: O2; Taxifolin; 2-Oxoglutarate

sequence_source: UniProtKB:Q96330 direct exact-accession lookup

substrate: O2; Taxifolin; 2-Oxoglutarate


substrate_name: 2-Oxoglutarate; O2; Taxifolin

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q96330 canonical sequence plus validated H132Y substitution from selected source mutation_signature and applied mutation signature H132Y to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: flavonol synthase(Enzyme) mutant H132Y GST-tag

substrate: 2-Oxoglutarate; O2; Taxifolin


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q96330 canonical sequence plus validated F134L substitution from selected source mutation_signature and applied mutation signature F134L to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q96330 canonical sequence checked only; variant sequence unresolved

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

proof_lines: SABIO-RK modifier species: flavonol synthase(Enzyme) mutant HF134L GST-tag


substrate_name: 2-Oxoglutarate; Taxifolin; O2

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q96330 canonical sequence plus validated E295Q substitution from selected source mutation_signature and applied mutation signature E295Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: flavonol synthase(Enzyme) mutant E295Q GST-tag

substrate: 2-Oxoglutarate; Taxifolin; O2


substrate_name: Taxifolin; O2; 2-Oxoglutarate

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q96330 canonical sequence plus validated S289T substitution from selected source mutation_signature and applied mutation signature S289T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: flavonol synthase(Enzyme) mutant S289T GST-tag

substrate: Taxifolin; O2; 2-Oxoglutarate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q96330 canonical sequence plus validated H132F substitution from selected source mutation_signature and applied mutation signature H132F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: flavonol synthase(Enzyme) mutant H132F GST-tag


organism: Camellia sinensis

sequence_source: UniProtKB:A2TJG2 direct exact-accession lookup


sequence_source: UniProtKB:A0A286QXZ1 direct exact-accession lookup


sequence_source: UniProtKB:A0A286QXZ3 direct exact-accession lookup


substrate_name: dihydrokampferol

sequence_source: UniProtKB:A0A286QXZ2 direct exact-accession lookup

substrate: dihydrokampferol


organism: Citrus unshiu

sequence_source: UniProtKB:Q9ZWQ9 direct exact-accession lookup


enzyme_display_name: tRNA dimethylallyltransferase

organism: Escherichia coli (strain K12)

substrate_name: tRNA(Phe)

enzyme: tRNA dimethylallyltransferase

substrate: tRNA(Phe)


organism: Saccharomyces cerevisiae

substrate_name: Reduced glutathione; RX

substrate: Reduced glutathione; RX


organism: Escherichia coli

substrate_name: GCGGACUCAAAAUCCGC

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

substrate: GCGGACUCAAAAUCCGC


substrate_name: seventeen-base RNA oligonucleotide

assay_conditions_summary: pH 8

substrate: seventeen-base RNA oligonucleotide


proof_lines:
mutnat Q282A, pH 8.0
mutant Q282A, pH 8.0


substrate_name: dimethylallyl diphosphate

substrate: dimethylallyl diphosphate


organism: Lactobacillus acidophilus

substrate_name: DELTA2-isopentenyl diphosphate

substrate: DELTA2-isopentenyl diphosphate


organism: Homo sapiens


organism: Mus musculus


substrate_name: progesterone

proof_lines: 17alpha-hydroxylation, pH 7.4, 37°C, presence of cytochrome b5

proof_lines: 16alpha-hydroxylation, pH 7.4, 37°C, presence of cytochrome b5

substrate: progesterone


organism: Rattus norvegicus

proof_lines: intermediate substrate, female duodenum enzyme

proof_lines: intermediate substrate, male duodenum enzyme


enzyme_display_name: NAD(+) diphosphatase

substrate_name: ADP-ribose

assay_conditions_summary: cofactor ADP

proof_lines: kcat is 0.06 sec(-1) with ADP-ribose as substrate.

enzyme: NAD(+) diphosphatase

substrate: ADP-ribose


substrate_name: ADP-ribose (at pH 8 and 37 degrees Celsius)

assay_conditions_summary: pH 8; cofactor NADH

proof_lines: kcat is 0.12 sec(-1) with ADP-ribose as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15878881). kcat is 0.01 sec(-1) with NADH as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15878881).


substrate_name: FMN using enzyme purified from E.coli

assay_conditions_summary: pH 7.5; cofactor FAD

proof_lines: kcat is 0.69 sec(-1) for FAD synthase activity using enzyme purified from E.coli (at 37 degrees Celsius and at pH 7.5) (PubMed:21951714). kcat is 0.69 sec(-1) for FAD synthase activity using enzyme purified from E.coli (at 37 degrees Celsiu

proof_lines: kcat is 0.042 sec(-1) for FAD synthase activity using C-terminal region (329-587) purified from E.coli (at 37 degrees Celsius and at pH 7.5) (PubMed:23443125). kcat is 0.0037 sec(-1) for the reverse pyrophosphorolytic reaction using C-termi

substrate: FMN using enzyme purified from E.coli


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 1.5 sec(-1) for NADH. kcat is 0.6 sec(-1) for NAD(+). kcat is 0.6 sec(-1) for ADP-ribose.


organism: Apis cerana indica

substrate_name: maltotriose

substrate: maltotriose


substrate_name: sucrose

substrate: sucrose


organism: Bombyx mori

substrate_name: 4-nitrophenyl alpha-D-glucopyranoside

sequence_source: UniProtKB REST exact accession lookup

substrate: 4-nitrophenyl alpha-D-glucopyranoside


organism: Candida albicans


substrate_name: p-nitrophenyl-alpha-D-glucopyranoside

substrate: p-nitrophenyl-alpha-D-glucopyranoside


organism: Schizosaccharomyces pombe

substrate_name: maltose

substrate: maltose


substrate_name: nigerose

substrate: nigerose


substrate_name: maltohexaose

substrate: maltohexaose


organism: Spodoptera frugiperda


substrate_name: NAD+

assay_conditions_summary: pH 7; 310.15 K; cofactor NAD+

substrate: NAD+


assay_conditions_summary: pH 7; 310.15 K; cofactor NADH


substrate_name: NADH; H2O

assay_conditions_summary: cofactor NAD+

substrate: NADH; H2O


substrate_name: Coenzyme A; H2O

substrate: Coenzyme A; H2O


substrate_name: H2O; NADH

substrate: H2O; NADH


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

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


organism: Triticum aestivum

substrate_name: NAD(+)

substrate: NAD(+)


organism: Bos taurus


proof_lines:
pH 7.5, 37°C, alpha2-beta complex
pH 7.5, 37°C


organism: Sporothrix schenckii

assay_conditions_summary: pH 7.2; 310.15 K; buffer 25 mM HEPES


organism: Sus scrofa


organism: Caenorhabditis elegans

assay_conditions_summary: pH 8.5; cofactor NAD+


proof_lines: in presence of 20 mM MgCl2, 50 mM Tris-HCl, pH 8.5

proof_lines: competitive inhibitor, no inhibiton with NMN+


organism: Nicotiana tabacum

assay_conditions_summary: pH 7.4; cofactor NAD+

proof_lines: 100 mM MOPS-NaOH, pH 7.4, 5 mM MgCl2, 10 mM dithioerythritol, 0.1 mM EDTA


organism: Proteus vulgaris

substrate_name: NADP+

assay_conditions_summary: pH 7; cofactor NADP+

substrate: NADP+


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 7.5; cofactor NAD+


organism: Arabidopsis thaliana

sequence_source: UniProtKB reviewed accession Q94B74; required accession reuse cache

assay_conditions_summary: pH 8; 310.15 K; cofactor NADH


sequence_source: UniProtKB reviewed accession Q9SJC4; required accession reuse cache

normalized_value_unit_evidence: kcat: printed cell 0.18 s^-1 -> 0.18 s^(-1) (the printed column is already in export units); the exported value is 0.18 s^(-1). Km: printed cell 13.7 uM -> 0.0137 mM (divide by 1000); the exported value is 0.014 mM, the same measurement flattened to three decimals (issue category source_km_precision_flattened_to_three_decimals). kcat/Km: the paper PRINTS the kcat/Km cell 1.4 x 10^4 s^-1 M^-1 for this row -> 14.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 12.857142857142856 s^(-1)*mM^(-1), which is the bare quotient of the exported kcat and the flattened Km, not a printed cell.

row_label: Table II, row evidence block `Table II row: NADH / AtNUDT6`, substrate row `NADH`, protein `AtNUDT6`

table_label: Table II (JBC 280:25277-25283) 'The kinetic parameters of ADP-ribose and NADH pyrophosphatases in A. thaliana, human, M. jannaschii, Synechococcus PCC7002, and yeast'


sequence_source: UniProtKB reviewed accession Q9SU14; required accession reuse cache

normalized_value_unit_evidence: kcat: printed cell 0.06 s^-1 -> 0.06 s^(-1) (the printed column is already in export units); the exported value is 0.06 s^(-1). Km: printed cell 37.2 uM -> 0.0372 mM (divide by 1000); the exported value is 0.037 mM, the same measurement flattened to three decimals (issue category source_km_precision_flattened_to_three_decimals). kcat/Km: the paper PRINTS the kcat/Km cell 1.5 x 10^3 s^-1 M^-1 for this row -> 1.5 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 1.6216216216216217 s^(-1)*mM^(-1), which is the bare quotient of the exported kcat and the flattened Km, not a printed cell.

row_label: Table II, row evidence block `Table II row: NADH / AtNUDT7`, substrate row `NADH`, protein `AtNUDT7`


assay_conditions_summary: cofactor NADPH

proof_lines: SABIO-RK modifier species: NAD+ diphosphatase(Enzyme) mutant without transit peptide N-terminal His-tagged


organism: Bacillus methanolicus

substrate_name: NAD+; H2O

substrate: NAD+; H2O


assay_conditions_summary: pH 9.5; 323.15 K; cofactor NAD+


organism: Escherichia coli

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+


substrate_name: NMN

substrate: NMN


substrate_name: NADH


sequence_variant_note: Resolved canonical sequence from P32664 canonical UniProtKB sequence with selected mutation signature reconstructed during review and applied mutation signature H149E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from P32664 canonical UniProtKB sequence with selected mutation signature reconstructed during review and applied mutation signature R148A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P32664; required accession reuse cache


sequence_variant_note: Resolved canonical sequence from P32664 canonical UniProtKB sequence with selected mutation signature reconstructed during review and applied mutation signature R148A/H149E to reconstruct the assayed variant sequence.


organism: Mus musculus

sequence_source: UniProtKB:Q8JZU0 REST/FASTA direct lookup; reviewed NUD13_MOUSE canonical sequence.

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


sequence_source: UniProtKB:P53164 REST/FASTA direct lookup; reviewed NPY1_YEAST canonical sequence.

assay_conditions_summary: pH 7.7; 310.15 K; cofactor NAD+


proof_lines: isozyme PIP5Kbeta, pH 7.5, temperature not specified in the publication

proof_lines: isozyme PIP5Kalpha, pH 7.5, temperature not specified in the publication

proof_lines: isozyme PIP5Kgamma, pH 7.5, temperature not specified in the publication


enzyme_display_name: protein kinase C

organism: Homo sapiens

substrate_name: ATP (for recombinant purified PRKCI)

assay_conditions_summary: cofactor ATP

enzyme: protein kinase C

substrate: ATP (for recombinant purified PRKCI)


organism: Amycolatopsis orientalis

sequence_source: UniProtKB:G4V4T6 direct FASTA

assay_conditions_summary: pH 7.5; 297.15 K; cofactor CoA


substrate_name: phenylacetyl-CoA

substrate: phenylacetyl-CoA


organism: Streptomyces toyocaensis

sequence_source: UniProtKB:Q8KLK7 direct FASTA

assay_conditions_summary: pH 7.4; 297.15 K; cofactor CoA


proof_lines:
pH 7.4, 24°C
Raw SKiD Env: Temp=24°C, pH=7.5
Raw SKiD Env: Temp=24°C, pH=7.4


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8KLK7 canonical FASTA plus row mutation E255Q reconstruction; mutagenesis feature PMID 18004875 and applied mutation signature E255Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8KLK7 canonical FASTA plus row mutation E189Q reconstruction; mutagenesis feature PMID 18004875 and applied mutation signature E189Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8KLK7 canonical FASTA plus row mutation R254K reconstruction; mutagenesis feature PMID 18004875 and applied mutation signature R254K to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q8KLK7 canonical FASTA plus row mutation E255Q reconstruction; mutagenesis feature PMID 18004875


sequence_source: UniProtKB:Q8KLK7 canonical FASTA plus row mutation E189Q reconstruction; mutagenesis feature PMID 18004875


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8KLK7 canonical FASTA plus row mutation Q299N reconstruction; mutagenesis feature PMID 18004875 and applied mutation signature Q299N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q8KLK7 canonical FASTA plus row mutation Q299N reconstruction; mutagenesis feature PMID 18004875


organism: Aspergillus fumigatus

substrate_name: NADPH

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: L-ornithine

proof_lines: pH 7.5, 25°C, cosubstrate: NADH, following the formation of hydroxylated ornithine

proof_lines: pH 7.5, temperature not specified in the publication

substrate: L-ornithine


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

substrate: NADH


substrate_name: L-Ornithine

substrate: L-Ornithine


assay_conditions_summary: pH 7.6; 298.15 K; cofactor NADPH

proof_lines: pH 7.6, 25°C, wild-type enzyme, cofactor: NADPH


proof_lines: pH 7.6, 25°C, mutant enzyme S257A, cofactor: NADPH


enzyme_display_name: tetracycline 11a-monooxygenase

organism: Bacteroides thetaiotaomicron

substrate_name: chlortetracycline

assay_conditions_summary: pH 8.5; cofactor NADPH

proof_lines: pH 8.5, temperature not specified in the publication

enzyme: tetracycline 11a-monooxygenase

substrate: chlortetracycline


organism: Amycolatopsis alba

assay_conditions_summary: pH 7.5; cofactor FAD

proof_lines: recombinant FAD-reconstituted enzyme-enzyme, pH 7.5, temperature not specified in the publication

proof_lines: recombinant holo-enzyme, pH 7.5, temperature not specified in the publication


organism: Bacteroides fragilis

substrate_name: chlorotetracycline

sequence_source: UniProtKB reviewed accession Q01911 (TETX_BACFG), direct EC 1.14.13.231 + organism Bacteroides fragilis lookup

proof_lines: presence of 0.0002% arabinose, pH not specified in the publication, temperature not specified in the publication

proof_lines: presence of 0.02% arabinose, pH not specified in the publication, temperature not specified in the publication

substrate: chlorotetracycline


organism: Bos taurus

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

proof_lines:
pH 7, 25°C, at 5 mM Mg2+
ATP in form of MgATP2-
pH 7.0, 25°C


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: in 1-phosphatidyl-1D-myo-inositol 4-phosphate micelles, type II enzyme

proof_lines: in 1-phosphatidyl-1D-myo-inositol 4-phosphate liposomes, type I enzyme


organism: Ovis aries

substrate_name: ATP

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

substrate: ATP


organism: Rattus norvegicus

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP


organism: Schizosaccharomyces pombe

sequence_source: UniProtKB reviewed accession O13853 (ITS3_SCHPO), direct EC 2.7.1.68 + organism Schizosaccharomyces pombe lookup

assay_conditions_summary: pH 7.5; cofactor ATP


organism: Triticum aestivum


substrate_name: DPA-CoA

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 10 min(-1) for dioxygenase activity.

substrate: DPA-CoA


proof_lines: kcat is 10.32 min(-1) for dioxygenase activity with DPA-CoA as substrate (PubMed:18004875). kcat is 0.172 sec(-1) for dioxygenase activity with DPA-CoA as substrate (PubMed:17507985).


organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)

substrate_name: L-ornithine (in the presence of 1 mM NADH)

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 29 min(-1) with L-ornithine as substrate and 75 min(-1) with NADPH as substrate.


substrate_name: demeclocycline

proof_lines: kcat varies from 1.3 sec(-1) for oxytetracycline to 0.12 sec(-1) for minocycline.

substrate: demeclocycline


organism: Arabidopsis thaliana

sequence_source: UniProtKB exact accession lookup for Q56YP2


sequence_source: UniProtKB exact accession lookup for Q9LMN1


sequence_source: UniProtKB exact accession lookup for O14986


sequence_variant_note: Resolved canonical sequence from UniProtKB exact accession lookup for O14986 and applied mutation signature E362A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 1-phosphatidylinositol-4-phosphate 5-kinase(Enzyme) mutant I beta E362A


sequence_source: UniProtKB exact accession lookup for Q99755


sequence_source: UniProtKB exact accession lookup for P70182


enzyme_display_name: procollagen-lysine 5-dioxygenase

substrate_name: UDP-galactose

enzyme: procollagen-lysine 5-dioxygenase

substrate: UDP-galactose


substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines: pH 7.4, 37°C, recombinant wild-type isozyme PKCalpha


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17252 canonical sequence reconstructed with PMID 17279776 M417A substitution and applied mutation signature M417A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, recombinant isozyme PKCalpha mutant M417A


sequence_source: UniProtKB canonical sequence for accession O00469

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


substrate_name: peptide (IKG)3

substrate: peptide (IKG)3


enzyme_display_name: aspartate--prephenate aminotransferase

substrate_name: L-aspartate

sequence_source: UniProtKB canonical sequence for accession Q9SIE1

enzyme: aspartate--prephenate aminotransferase

substrate: L-aspartate


substrate_name: prephenate

sequence_variant_note: Resolved canonical sequence from UniProtKB canonical sequence for accession Q9SIE1 and applied mutation signature A168G to reconstruct the assayed variant sequence.

substrate: prephenate


sequence_variant_note: Resolved canonical sequence from UniProtKB canonical sequence for accession Q9SIE1 and applied mutation signature T84V to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from UniProtKB canonical sequence for accession Q9SIE1 and applied mutation signature E108K to reconstruct the assayed variant sequence.


organism: Sinorhizobium meliloti

substrate_name: oxaloacetate

sequence_variant_note: Resolved canonical sequence from UniProtKB canonical sequence for accession Q02635 and applied mutation signature K12G to reconstruct the assayed variant sequence.

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

substrate: oxaloacetate


sequence_source: UniProtKB canonical sequence for accession Q02635


substrate_name: aspartate for the asparte aminotransferase activity


organism: Petunia hybrida

substrate_name: prephenate (with 20 mM aspartate as cosubstrate)


substrate_name: ATP; Sox-AKT-tide peptide

sequence_source: UniProtKB:P24723 reviewed Swiss-Prot REST lookup 2026-06-23.

proof_lines: isozyme PKCeta, in 20 mM Tris-HCl, pH 7.5, 10 mM MgCl2, and 0.1 mM CaCl2, at 25°C

substrate: ATP; Sox-AKT-tide peptide


substrate_name: Sox-AKT-tide peptide; ATP

sequence_source: UniProtKB:P05771 reviewed Swiss-Prot REST lookup 2026-06-23.

proof_lines: isozyme PKCbetaI, in 20 mM Tris-HCl, pH 7.5, 10 mM MgCl2, and 0.1 mM CaCl2, at 25°C

proof_lines: isozyme PKCbetaII, in 20 mM Tris-HCl, pH 7.5, 10 mM MgCl2, and 0.1 mM CaCl2, at 25°C

substrate: Sox-AKT-tide peptide; ATP


sequence_source: UniProtKB:Q04759 reviewed Swiss-Prot REST lookup 2026-06-23.

proof_lines: isozyme PKCtheta, in 20 mM Tris-HCl, pH 7.5, 10 mM MgCl2, and 0.1 mM CaCl2, at 25°C


sequence_source: UniProtKB:Q02156 reviewed Swiss-Prot REST lookup 2026-06-23.

proof_lines: isozyme PKCepsilon, in 20 mM Tris-HCl, pH 7.5, 10 mM MgCl2, and 0.1 mM CaCl2, at 25°C


substrate_name: ATP; Peptide

sequence_source: UniProtKB:Q16513 reviewed Swiss-Prot REST lookup 2026-06-23; reconstructed selected PRK2 construct as canonical residues 511-942.

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

proof_lines: SABIO-RK modifier species: protein kinase C(Enzyme) mutant PRK2 (only residues 511-942)

substrate: ATP; Peptide


substrate_name: Peptide; ATP

sequence_source: UniProtKB:Q16512 reviewed Swiss-Prot REST lookup 2026-06-23; reconstructed selected PRK1 construct as canonical residues 511-942.

proof_lines: SABIO-RK modifier species: protein kinase C(Enzyme) mutant PRK1 (only residues 511-942)

substrate: Peptide; ATP


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

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: pH 7.5, 30°C, T176A mutant GST-CK1delta fusion protein


sequence_source: UniProtKB:Q63433 reviewed Swiss-Prot REST lookup 2026-06-23.


organism: Saccharomyces cerevisiae

substrate_name: GGLHRHGSIINRKEEI; ATP

sequence_source: UniProtKB:P24583 reviewed Swiss-Prot REST lookup 2026-06-23.

assay_conditions_summary: cofactor ATP

substrate: GGLHRHGSIINRKEEI; ATP


organism: Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)

sequence_source: UniProt Q8KDS8 source_record; confirmed by UniProt REST lookup

proof_lines: kcat is 17.2 sec(-1) with 2-oxoglutarate as substrate. kcat is 12.3 sec(-1) with prephenate as substrate.


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

substrate_name: L-aspartate (at 45 degrees Celsius)

sequence_source: UniProt Q56232 source_record; confirmed by UniProt REST lookup

proof_lines: kcat is 7.7 sec(-1) toward prephenate. kcat is 32.2 sec(-1) toward oxaloacetate.

substrate: L-aspartate (at 45 degrees Celsius)


organism: Anchusa officinalis


substrate_name: S-(hydroxymethyl)glutathione

assay_conditions_summary: pH 8

proof_lines: kcat is 1351 min(-1) with S-hydroxymethylglutathione as substrate (at pH 8 and 25 degrees Celsius). kcat is 6 min(-1) with farnesol as substrate (at pH 7.5 and 25 degrees Celsius). kcat is 324 min(-1) with cinnamylalcohol as substrate (at p

substrate: S-(hydroxymethyl)glutathione


organism: Pisum sativum

substrate_name: octanol (at pH 10)

assay_conditions_summary: pH 10

proof_lines: kcat is 190 min(-1) with octanol as substrate (at pH 10). kcat is 110 min(-1) with 12-OH-dodecanoic acid as substrate (at pH 10). kcat is 380 min(-1) with S-hydroxymethylglutathione as substrate (at pH 8).

substrate: octanol (at pH 10)


organism: Unknown

substrate_name: S-hydroxymethyl glutathione

substrate: S-hydroxymethyl glutathione


sequence_source: UniProtKB reviewed accession direct lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession direct lookup and applied mutation signature K12G to reconstruct the assayed variant sequence.


organism: Thermus thermophilus


organism: Homo sapiens

substrate_name: Protein; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession direct lookup and applied mutation signature K274R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: protein kinase C(Enzyme) mutant K274R aPKC-iota (RGS-His6 tagged)

substrate: Protein; ATP


substrate_name: ATP; Protein

proof_lines: isozyme PKCalpha, in 20 mM Tris-HCl, pH 7.5, 10 mM MgCl2, and 0.1 mM CaCl2, at 25°C

proof_lines: pH 7.5, 30°C, full-length GST-CK1delta fusion protein

substrate: ATP; Protein


proof_lines: isozyme PKCiota/lambda, in 20 mM Tris-HCl, pH 7.5, 10 mM MgCl2, and 0.1 mM CaCl2, at 25°C


substrate_name: FKKQGSFAKKK

proof_lines: isozyme PKCzeta, in 20 mM Tris-HCl, pH 7.5, 10 mM MgCl2, and 0.1 mM CaCl2, at 25°C

substrate: FKKQGSFAKKK


proof_lines: isozyme PKCdelta, in 20 mM Tris-HCl, pH 7.5, 10 mM MgCl2, and 0.1 mM CaCl2, at 25°C


proof_lines: isozyme PKCgamma, in 20 mM Tris-HCl, pH 7.5, 10 mM MgCl2, and 0.1 mM CaCl2, at 25°C


substrate_name: S-nitrosoglutathione

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

proof_lines: in 0.1 M potassium phosphate (pH 7.5), at 25°C

substrate: S-nitrosoglutathione


organism: Lathyrus oleraceus

assay_conditions_summary: cofactor NAD+

proof_lines: reaction with S-hydroxymethyl glutathione


organism: Pseudomonas putida

substrate_name: NAD+

substrate: NAD+


organism: Rattus norvegicus

substrate_name: NAD+; Reduced glutathione; Formaldehyde

substrate: NAD+; Reduced glutathione; Formaldehyde


substrate_name: S-hydroxymethylglutathione

proof_lines:
wild-type enzyme
wilde-type enzyme

substrate: S-hydroxymethylglutathione


organism: Schwanniomyces vanrijiae


organism: Staphylococcus aureus


organism: Zea mays

substrate_name: formaldehyde

substrate: formaldehyde


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: S-(hydroxymethyl)glutathione (at pH 8)

substrate: S-(hydroxymethyl)glutathione (at pH 8)


organism: Arabidopsis thaliana

substrate_name: NAD+; S-(Hydroxymethyl)glutathione

sequence_source: UniProt REST direct accession lookup for Q96533 on 2026-06-23

substrate: NAD+; S-(Hydroxymethyl)glutathione


substrate_name: S-(Hydroxymethyl)glutathione

substrate: S-(Hydroxymethyl)glutathione


organism: Aspergillus nidulans

sequence_source: UniProt REST direct accession lookup for Q5AVP8 on 2026-06-23


organism: Brassica oleracea var. botrytis

sequence_source: UniProt REST direct accession lookup for J7GP93 on 2026-06-23

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH


organism: Drosophila melanogaster

substrate_name: NAD+; 1-Pentanol

sequence_source: UniProt REST direct accession lookup for P46415 on 2026-06-23

substrate: NAD+; 1-Pentanol


substrate_name: Formaldehyde; Reduced glutathione; NAD+

sequence_source: UniProt REST direct accession lookup for P11766 on 2026-06-23

substrate: Formaldehyde; Reduced glutathione; NAD+


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

proof_lines: mutant K188A, pH and temperature not specified in the publication


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

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


substrate_name: S-(Hydroxymethyl)glutathione; NAD+

proof_lines: SABIO-RK modifier species: S-(hydroxymethyl)glutathione dehydrogenase(Enzyme) mutant T48A

substrate: S-(Hydroxymethyl)glutathione; NAD+


proof_lines: SABIO-RK modifier species: S-(hydroxymethyl)glutathione dehydrogenase(Enzyme) mutant D57L/Y93F


proof_lines: SABIO-RK modifier species: S-(hydroxymethyl)glutathione dehydrogenase(Enzyme) mutant D57L


organism: Bos taurus

proof_lines:
enzyme form F6.0
enzyme form F6.2
enzyme form F6.5


organism: Branchiostoma floridae

assay_conditions_summary: pH 7.5; cofactor NAD+

proof_lines:
in 0.1 M sodium diphosphate at pH 7.5
in 0.1 M sodium diphosphate at pH 8.0


organism: Chlamydomonas reinhardtii

substrate_name: NADH

assay_conditions_summary: pH 7.9; cofactor NADH

proof_lines: pH 7.9, temperature not specified in the publication

substrate: NADH


organism: Escherichia coli


organism: Helicobacter pylori


organism: Homo sapiens

proof_lines:
mutant R368L, pH 7.5, 25°C
mutant R368L, pH 7.5, 30°C
mutant R368L, pH 7.5


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

proof_lines:
mutant E67L, pH 7.5, 30°C
mutant E67L, pH 7.5
mutant E67L, pH 10


proof_lines:
wild type enzyme, pH 7.5
wild type enzyme, pH 7.5, 25°C
wild type enzyme, pH 7.5, 30°C


sequence_variant_note: Resolved canonical sequence from UniProt P11766 canonical FASTA with Y93F applied after direct coordinate check and applied mutation signature Y93F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: S-(hydroxymethyl)glutathione dehydrogenase(Enzyme) mutant Y93F


substrate_name: 1-Octanol; NAD+

sequence_variant_note: Resolved canonical sequence from UniProt P11766 canonical FASTA with R115A applied after direct coordinate check and applied mutation signature R115A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: S-(hydroxymethyl)glutathione dehydrogenase(Enzyme) mutant R115A

substrate: 1-Octanol; NAD+


substrate_name: NAD+; 1-Octanol

sequence_variant_note: Resolved canonical sequence from UniProt P11766 canonical FASTA with R115D applied after direct coordinate check and applied mutation signature R115D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: S-(hydroxymethyl)glutathione dehydrogenase(Enzyme) mutant R115D

substrate: NAD+; 1-Octanol


organism: Lactuca sativa

sequence_source: UniProt J7GHV7 FASTA checked directly on 2026-06-23


organism: Oryctolagus cuniculus

sequence_source: UniProt O19053 FASTA checked directly on 2026-06-23


organism: Rattus norvegicus

substrate_name: Formaldehyde; NAD+; Reduced glutathione

sequence_source: UniProt P12711 FASTA checked directly on 2026-06-23

substrate: Formaldehyde; NAD+; Reduced glutathione


organism: Solanum lycopersicum

sequence_source: UniProt D2Y3F4 FASTA checked directly on 2026-06-23

proof_lines: pH and temperature not specified in the publication


substrate_name: type IV procollagen

proof_lines:
isozyme LH3, at 37°C
isozyme LH2, at 37°C
isozyme LH1, at 37°C

substrate: type IV procollagen


organism: Mus musculus

substrate_name: GDPmannose

substrate: GDPmannose


organism: Pyrococcus horikoshii

substrate_name: C120-dolichyl phosphate

substrate: C120-dolichyl phosphate


substrate_name: dolichyl phosphate

substrate: dolichyl phosphate


organism: Saccharomyces cerevisiae


proof_lines: wild-type enzyme assayed in solution of Nonidet P-40

proof_lines: wild-type enzyme reconstituted with phosphatidylethanolamine


organism: Thermoplasma acidophilum


organism: Zea mays


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: GDP-mannose

proof_lines: For the phosphorylated protein, the Vmax increases to 146.7 nmol/min/mg enzyme, whereas the KM stays at 1.1 uM for GDP-mannose, increasing the catalytic efficiency 6-fold.

substrate: GDP-mannose


enzyme_display_name: type 2 galactoside alpha-(1,2)-fucosyltransferase

substrate_name: Galacto-N-biose

substrate: Galacto-N-biose


substrate_name: galacto-N-biose

enzyme: type 2 galactoside alpha-(1,2)-fucosyltransferase

substrate: galacto-N-biose


substrate_name: phenyl beta-D-galactoside

substrate: phenyl beta-D-galactoside


substrate_name: phenyl-beta-D-galactoside

substrate: phenyl-beta-D-galactoside


substrate_name: phenyl-beta-D-Galactoside

substrate: phenyl-beta-D-Galactoside


substrate_name: phenyl-beta-galactose

substrate: phenyl-beta-galactose


enzyme_display_name: inositol-pentakisphosphate 2-kinase

organism: Arabidopsis thaliana

substrate_name: Ins(1,3,4,5,6)P5 (in the presence of 0.4 mM ATP)

enzyme: inositol-pentakisphosphate 2-kinase


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)


substrate_name: peptide (IKG)3

proof_lines: pH 7.4, 37°C, recombinant wild-type enzyme

substrate: peptide (IKG)3


substrate_name: ascorbate

proof_lines:
lysyl hydroxylase 3
lysyl hydroxylase 1
lysyl hydroxylases 1 and 3

substrate: ascorbate


substrate_name: Procollagen L-lysine

substrate: Procollagen L-lysine


organism: Thermosynechococcus vestitus

substrate_name: GDP-beta-L-fucose

proof_lines: donor hydrolysis reaction, pH not specified in the publication, temperature not specified in the publication

proof_lines: fucosyl transferase reaction, pH not specified in the publication, temperature not specified in the publication

substrate: GDP-beta-L-fucose


substrate_name: GDPmannose; Dolichyl phosphate

proof_lines:
non-phosphorylated enzyme, 37°C, pH 7.0
phosphorylated enzyme, 37°C, pH 7.0

substrate: GDPmannose; Dolichyl phosphate


organism: Gallus gallus

substrate_name: [procollagen]-L-lysine

substrate: [procollagen]-L-lysine


proof_lines:
wild-type enzyme
wild-type enzyme and mutant T604I


organism: Bos taurus


proof_lines: pH 7.2, temperature not specified in the publication


organism: Acanthamoeba castellanii

substrate_name: GDPmannose


organism: Candida albicans


organism: Cricetulus griseus

proof_lines: 37°C, pH 7.0, wild-type enzyme, without dolichyl phosphate, wild-type enzyme

proof_lines: 37°C, pH 7.0, wild-type enzyme, in presence of dolichyl phosphate, wild-type enzyme

proof_lines: 37°C, pH 7.0, wild-type enzyme, with or without dolichyl phosphate, enzyme from cAMP-dependent protein kinase-deficient mutant 10215


organism: Entamoeba histolytica

proof_lines:
unphosphorylated enzyme
phosphorylated enzyme


enzyme_display_name: 7-dimethylallyltryptophan synthase

organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)

substrate_name: dimethylallyl diphosphate

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

enzyme: 7-dimethylallyltryptophan synthase

substrate: dimethylallyl diphosphate


organism: Aspergillus fumigatus

substrate_name: L-o-tyrosine

sequence_source: UniProtKB Q4WYG3 direct REST lookup on 2026-06-23

substrate: L-o-tyrosine


substrate_name: dia,ent-ardeemin fumiquinazoline

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

substrate: dia,ent-ardeemin fumiquinazoline


organism: Aspergillus niger

substrate_name: L-tryptophan

sequence_source: UniProtKB A2R1N3 direct REST lookup on 2026-06-23; sequence not accepted as resolving EC 2.5.1.80 without further arbitration

substrate: L-tryptophan


substrate_name: phloretin

sequence_source: UniProtKB EC+organism lookup: reviewed Aspergillus fumigatus 7-DMATS accessions Q4WYG3 and B0XWK7 share this sequence; selected BRENDA aggregate does not name one accession.

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

proof_lines: pH and temperature not specified in the publication

substrate: phloretin


organism: Neosartorya sp.


enzyme_display_name: phosphoinositide phospholipase C

organism: Homo sapiens

enzyme: phosphoinositide phospholipase C


organism: Rattus norvegicus


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: geranyl diphosphate phosphohydrolase

enzyme: geranyl diphosphate phosphohydrolase


organism: Mus musculus


enzyme_display_name: nicotinamide-nucleotide amidase

organism: Oceanobacillus iheyensis

substrate_name: beta-nicotinamide D-ribonucleotide

sequence_source: UniProtKB direct accession lookup for Q8EQR8 on 2026-06-23

enzyme: nicotinamide-nucleotide amidase

substrate: beta-nicotinamide D-ribonucleotide


organism: Arabidopsis thaliana

substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


substrate_name: farnesyl diphosphate

sequence_source: UniProtKB direct accession lookup for Q6ZVK8 on 2026-06-23

substrate: farnesyl diphosphate


organism: Rosa hybrid cultivar

sequence_source: UniProtKB direct accession lookup for M4I1C6 on 2026-06-23

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


organism: Rosa lucieae


enzyme_display_name: eukaryotic sulfide quinone oxidoreductase

organism: Arenicola marina

substrate_name: hydrogen sulfide

sequence_source: UniProtKB:B0LD08 direct accession lookup

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

substrate: hydrogen sulfide


substrate_name: sulfite

sequence_source: UniProtKB:Q9Y6N5 direct accession lookup

enzyme: eukaryotic sulfide quinone oxidoreductase

substrate: sulfite


substrate_name: Sulfide

proof_lines: with homocysteine as acceptor, at pH 7.4 and 37°C

substrate: Sulfide


substrate_name: glutathione

substrate: glutathione


organism: Urechis unicinctus

sequence_source: UniProtKB:H2KXA2 direct accession lookup

proof_lines: with ubiquinone as cosubstrate, at pH 8.5 and 37°C


organism: Agrobacterium fabrum

substrate_name: nicotinamide mononucleotide

sequence_variant_note: Resolved canonical sequence from UniProtKB:A9CJ26 direct accession lookup; row-specific Y58F reconstruction and applied mutation signature Y58F to reconstruct the assayed variant sequence.

substrate: nicotinamide mononucleotide


sequence_variant_note: Resolved canonical sequence from UniProtKB:A9CJ26 direct accession lookup; row-specific T105A reconstruction and applied mutation signature T105A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A9CJ26 direct accession lookup; row-specific S48A reconstruction and applied mutation signature S48A to reconstruct the assayed variant sequence.


verification_status: verified

sequence_source: UniProtKB:A9CJ26 direct accession lookup

column_label: Table 1 (Kinetic parameters and melting temperature (Tm) of wild-type AtCinA and its mutants), row 'Wild-type'; column 'Km (μM)' = 24; column 'kcat (s-1)' = 8.7; column 'kcat /Km (mM-1s-1)' = 362.5; column 'Tm (°C)' = 85.

normalized_value_unit_evidence: Km: printed Table 1 cell 24 μM; 24 / 1000 = 0.024 mM; the exported value is 0.024 mM. kcat: printed Table 1 cell 8.7 s-1; already in s^-1, no conversion is needed (this paper prints no min^-1 kinetic cell); the exported value is 8.7 s^(-1). kcat/Km: printed Table 1 cell 362.5 mM-1 s-1; mM-1 s-1 is identical to the export unit s^(-1)*mM^(-1), so the printed cell normalizes unchanged to 362.5 s^(-1)*mM^(-1); the exported value is 362.49999999999994 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row 'Wild-type': Km = 24 μM; kcat = 8.7 s-1; printed kcat/Km = 362.5 mM-1 s-1.

row_label: Table 1, row 'Wild-type'

table_label: Table 1: Kinetic parameters and melting temperature (Tm) of wild-type AtCinA and its mutants.

status: verified


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A9CJ26 and applied mutation signature T105A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters and melting temperature (Tm) of wild-type AtCinA and its mutants), row 'T105A'; column 'Km (μM)' = 158; column 'kcat (s-1)' = 3.5; column 'kcat /Km (mM-1s-1)' = 22.1; column 'Tm (°C)' = 81.

normalized_value_unit_evidence: Km: printed Table 1 cell 158 μM; 158 / 1000 = 0.158 mM; the exported value is 0.158 mM. kcat: printed Table 1 cell 3.5 s-1; already in s^-1, no conversion is needed (this paper prints no min^-1 kinetic cell); the exported value is 3.5 s^(-1). kcat/Km: printed Table 1 cell 22.1 mM-1 s-1; mM-1 s-1 is identical to the export unit s^(-1)*mM^(-1), so the printed cell normalizes unchanged to 22.1 s^(-1)*mM^(-1); the exported value is 22.151898734177216 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row 'T105A': Km = 158 μM; kcat = 3.5 s-1; printed kcat/Km = 22.1 mM-1 s-1.

row_label: Table 1, row 'T105A'


sequence_source: UniProtKB:A9CJ26 direct accession lookup; row-specific Y58F reconstruction


normalized_value_unit_evidence: Km: printed Table 1 cell 24 μM; 24 / 1000 = 0.024 mM; the exported value is 0.024 mM. kcat: printed Table 1 cell 8.7 s-1; already in s^-1, no conversion is needed (this paper prints no min^-1 kinetic cell); the exported value is 8.7 s^(-1). kcat/Km: Table 1 also prints a catalytic-efficiency cell of 362.5 mM-1 s-1 for this row, transcribed in kcat_over_km_provenance; this catalog row stores no ratio, so no ratio is written into the record.


sequence_source: UniProtKB:A9CJ26 direct accession lookup; row-specific S48A reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB:A9CJ26 direct accession lookup; row-specific C32A reconstruction and applied mutation signature C32A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A9CJ26 and applied mutation signature C32A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters and melting temperature (Tm) of wild-type AtCinA and its mutants), row 'C32A'; column 'Km (μM)' = 28; column 'kcat (s-1)' = 7.3; column 'kcat /Km (mM-1s-1)' = 260.0; column 'Tm (°C)' = 83.

normalized_value_unit_evidence: Km: printed Table 1 cell 28 μM; 28 / 1000 = 0.028 mM; the exported value is 0.028 mM. kcat: printed Table 1 cell 7.3 s-1; already in s^-1, no conversion is needed (this paper prints no min^-1 kinetic cell); the exported value is 7.3 s^(-1). kcat/Km: printed Table 1 cell 260.0 mM-1 s-1; mM-1 s-1 is identical to the export unit s^(-1)*mM^(-1), so the printed cell normalizes unchanged to 260.0 s^(-1)*mM^(-1); the exported value is 260.7142857142857 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row 'C32A': Km = 28 μM; kcat = 7.3 s-1; printed kcat/Km = 260.0 mM-1 s-1.

row_label: Table 1, row 'C32A'


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T31A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S103A to reconstruct the assayed variant sequence.


proof_lines: recombinant wild-type enzyme, pH 7.5, 37°C


organism: Propionibacterium freudenreichii subsp. shermanii

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


organism: Rosa chinensis

substrate_name: geranyl diphosphate; farnesyl diphosphate


substrate: geranyl diphosphate; farnesyl diphosphate


organism: Escherichia coli (strain K12)

substrate_name: NMN

substrate: NMN


proof_lines: kcat is 0.78 sec(-1) for (2E)-geranyl diphosphate as substrate (at pH 8.0 and 22 degrees Celsius) (PubMed:38944687). kcat is 0.55 sec(-1) with (R)-5-diphosphomevalonate as substrate (at pH 8.0 and 22 degrees Celsius) (PubMed:38944687). kcat


substrate_name: dGTP (at pH 7.5)

proof_lines: Has a 10-fold higher catalytic efficiency toward dGTP compared to 8-oxo-dGTP. kcat is 0.58 sec(-1) with dGTP as substrate (at pH 8.0 and 22 degrees Celsius) (PubMed:38944687). kcat is 0.72 sec(-1) with (2E)-geranyl diphosphate as substrate

substrate: dGTP (at pH 7.5)


proof_lines: kcat is 0.02 sec(-1) with geranyl diphosphate as substrate. kcat is 0.0033 sec(-1) with farnesyl diphosphate as substrate.


enzyme_display_name: 2-keto-3-deoxy-L-rhamnonate aldolase

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

enzyme: 2-keto-3-deoxy-L-rhamnonate aldolase


substrate_name: 2-dehydro-3-deoxy-L-rhamnonate; 2-dehydro-3-deoxy-L-lyxonate; 4-hydroxy-2-oxoheptane-1,7-dioate; 4-hydroxy-2-oxohexanoate; 4-hydroxy-2-oxopentanoate; 2-dehydro-3-deoxy-L-mannonate

source_db: brenda,skid

proof_lines:
pH 8.0, 25°C
pH 8.0, 25°C, Mg2+-activated
pH 8.0, 25°C, Ni2+-activated

source: brenda,skid


organism: Lentzea aerocolonigenes

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine