organism: Propionibacterium freudenreichii

proof_lines:
reverse reaction, pH 8.0, 25°C
as Mg2+ complex, pH 8.0, 25°C
pH 8.0, 25°C


organism: Propionibacterium freudenreichii subsp. shermanii

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

proof_lines:
pH 7.4, 25°C
pH 8.0, 25°C
forward reaction, pH 8.0, 25°C

source: brenda


enzyme_display_name: arylsulfatase (type I)

organism: Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)

substrate_name: para-nitrophenyl sulfate

source_db: uniprot

protein_accession_database: UniProt

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

data_origin: experimental

enzyme: arylsulfatase (type I)

substrate: para-nitrophenyl sulfate

source: uniprot


organism: Homo sapiens

substrate_name: p-nitrocatechol sulfate

substrate: p-nitrocatechol sulfate


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


organism: Azotobacter vinelandii

substrate_name: NAD+; 4-Methylthio-2-oxobutanoate; Coenzyme A

km_display: Not reported

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

assay_conditions_summary: cofactor NAD+


substrate_name: NAD+; 2-Oxoglutarate; Coenzyme A

substrate: NAD+; 2-Oxoglutarate; Coenzyme A


substrate_name: Coenzyme A; NAD+; 2-Oxoglutarate

substrate: Coenzyme A; NAD+; 2-Oxoglutarate


organism: Corynebacterium glutamicum

substrate_name: NAD+; Coenzyme A; 2-Oxoglutarate

verification_status: unverified

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

proof_lines: SABIO-RK modifier species: Enzyme mutant AceF K162Q-K278Q

substrate: NAD+; Coenzyme A; 2-Oxoglutarate

status: unverified


substrate_name: Coenzyme A; 2-Oxoglutarate; NAD+

proof_lines: SABIO-RK modifier species: Enzyme mutant AceF K43Q-K162Q

substrate: Coenzyme A; 2-Oxoglutarate; NAD+


organism: Escherichia coli

substrate_name: 2-Oxoglutarate; NAD+; Coenzyme A

substrate: 2-Oxoglutarate; NAD+; Coenzyme A


organism: Rattus norvegicus


organism: Solanum tuberosum

substrate_name: 2-Oxoglutarate; Coenzyme A; NAD+

substrate: 2-Oxoglutarate; Coenzyme A; NAD+


organism: Sus scrofa

ki_unit: mM


organism: Xenopus laevis


organism: Yarrowia lipolytica

substrate_name: DL-dihydrolipoamide

mutation_type: substitution

substrate: DL-dihydrolipoamide


enzyme_display_name: aliphatic nitrilase

organism: Rhodococcus rhodochrous

substrate_name: m-tolunitrile

sequence_source: UniProtKB:Q03217 direct FASTA lookup

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03217 direct FASTA lookup and applied mutation signature K9A to reconstruct the assayed variant sequence.

enzyme: aliphatic nitrilase

substrate: m-tolunitrile


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03217 direct FASTA lookup and applied mutation signature Y142F to reconstruct the assayed variant sequence.


substrate_name: Benzonitrile

substrate: Benzonitrile


organism: Synechocystis sp.

source_db: oed

sequence_source: UniProtKB:Q55949 direct FASTA lookup

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q55949 direct FASTA lookup and applied mutation signature W146H to reconstruct the assayed variant sequence.

source: oed


kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q55949 direct FASTA lookup and applied mutation signature W146Y to reconstruct the assayed variant sequence.


substrate_name: Fumaronitrile

smiles: N#C/C=C/C#N

substrate: Fumaronitrile


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q55949 direct FASTA lookup and applied mutation signature W146F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6C5L8 and applied mutation signature D423del to reconstruct the assayed variant sequence.

mutation_type: deletion

proof_lines: mutant enzyme D423DEL, at pH 8.0 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6C5L8 and applied mutation signature D423A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6C5L8 and applied mutation signature H419A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6C5L8 and applied mutation signature H419D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6C5L8 and applied mutation signature D423G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6C5L8 and applied mutation signature H419S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q6C5L8 and applied mutation signature H419del to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H419DEL, at pH 8.0 and 30°C


enzyme_display_name: ribonuclease P

organism: Arabidopsis thaliana

substrate_name: H2O; tRNA precursor

enzyme: ribonuclease P

substrate: H2O; tRNA precursor


substrate_name: pre-tRNA-Cys

proof_lines:
25°C, pH 7.8
presence of theophylline, pH 7.6, 37°C
pH 7.6, 37°C

substrate: pre-tRNA-Cys


organism: Bacillus subtilis


organism: Methanococcus maripaludis

substrate_name: pre-tRNATyr

proof_lines:
37°C, pH 7.5, in the absence of L7Ae
37°C, pH 7.5, in the presence of L7Ae

substrate: pre-tRNATyr


organism: Thermotoga maritima

substrate_name: pre-tRNAPhe

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9X1H4 and applied mutation signature K53A to reconstruct the assayed variant sequence.

substrate: pre-tRNAPhe


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9X1H4 and applied mutation signature R59A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9X1H4 and applied mutation signature K62A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9X1H4 and applied mutation signature R89A to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant R89A/U52C, pH 7.5, 37°C


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

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

assay_conditions_summary: cofactor CoA


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate_name: alpha-ketoglutarate

substrate: alpha-ketoglutarate


substrate_name: tRNA(Gln) precursor

substrate: tRNA(Gln) precursor


enzyme_display_name: aqualysin 1

organism: Thermus aquaticus

sequence_source: UniProt:P08594 exact accession lookup; REST checked 2026-06-17 UTC

enzyme: aqualysin 1


sequence_variant_note: Resolved canonical sequence from UniProt:P08594 exact accession lookup; REST checked 2026-06-17 UTC and applied mutation signature G61D with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_accession:P08594 and applied mutation signature D17N with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters of the wild-type and mutant enzymes), enzyme row D17N; column 'k cat (s -1 )' = 110 ± 4.48; column 'K m (mM)' = 0.98 ± 0.05; column 'k cat / K m (mM -1 s -1 )' = 113.

normalized_value_unit_evidence: kcat: printed Table 3 cell 110 ± 4.48 s^-1; the printed unit s^-1 is already canonical, so no factor applies and the cell is 110.0 s^(-1). Km: printed Table 3 cell 0.98 ± 0.05 mM; the printed unit mM is already canonical, so no factor applies and the cell is 0.98 mM. kcat/Km: printed Table 3 cell 113 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 113.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row D17N: k_cat = 110 ± 4.48 s^-1; K_m = 0.98 ± 0.05 mM; printed k_cat/K_m = 113 mM^-1 s^-1.

row_label: Table 3, enzyme row D17N

table_label: Table 3: Kinetic parameters of the wild-type and mutant enzymes (AMB Express 2014, 4:59)

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P08594 and applied mutation signature D183N with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters of the wild-type and mutant enzymes), enzyme row D183N; column 'k cat (s -1 )' = 53.0 ± 3.03; column 'K m (mM)' = 0.74 ± 0.05; column 'k cat / K m (mM -1 s -1 )' = 71.6.

normalized_value_unit_evidence: kcat: printed Table 3 cell 53.0 ± 3.03 s^-1; the printed unit s^-1 is already canonical, so no factor applies and the cell is 53.0 s^(-1). Km: printed Table 3 cell 0.74 ± 0.05 mM; the printed unit mM is already canonical, so no factor applies and the cell is 0.74 mM. kcat/Km: printed Table 3 cell 71.6 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 71.6 s^-1 mM^-1.

row_label: Table 3, enzyme row D183N


sequence_variant_note: Resolved canonical sequence from UniProt:P08594 exact accession lookup; REST checked 2026-06-17 UTC and applied mutation signature E237Q with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P08594 exact accession lookup; REST checked 2026-06-17 UTC and applied mutation signature S277D with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature D138N matches the mutant residue at offset +11 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P08594 and applied mutation signature D58N with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters of the wild-type and mutant enzymes), enzyme row D58N; column 'k cat (s -1 )' = 68.5 ± 1.37; column 'K m (mM)' = 0.99 ± 0.07; column 'k cat / K m (mM -1 s -1 )' = 70.0.

normalized_value_unit_evidence: kcat: printed Table 3 cell 68.5 ± 1.37 s^-1; the printed unit s^-1 is already canonical, so no factor applies and the cell is 68.5 s^(-1). Km: printed Table 3 cell 0.99 ± 0.07 mM; the printed unit mM is already canonical, so no factor applies and the cell is 0.99 mM. kcat/Km: printed Table 3 cell 70.0 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 70.0 s^-1 mM^-1.

row_label: Table 3, enzyme row D58N


sequence_variant_note: Resolved canonical sequence from UniProt:P08594 exact accession lookup; REST checked 2026-06-17 UTC and applied mutation signature D212N with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.


organism: Cereibacter sphaeroides

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


organism: Fusarium proliferatum

sequence_source: UniProt:A0A0E3D8K7 exact accession lookup; REST checked 2026-06-17 UTC

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


organism: Pseudomonas fluorescens

substrate_name: sebaconitrile

sequence_source: UniProt:Q4KCL8 exact accession lookup; REST checked 2026-06-17 UTC

substrate: sebaconitrile


sequence_variant_note: Resolved canonical sequence from UniProt:Q03217 exact accession lookup; REST checked 2026-06-17 UTC and applied mutation signature Y142A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:Q03217 exact accession lookup; REST checked 2026-06-17 UTC and applied mutation signature Y142S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:Q03217 exact accession lookup; REST checked 2026-06-17 UTC and applied mutation signature Y142V to reconstruct the assayed variant sequence.


substrate_name: adiponitrile

sequence_variant_note: Resolved canonical sequence from UniProt:Q03217 exact accession lookup; REST checked 2026-06-17 UTC and applied mutation signature L79A to reconstruct the assayed variant sequence.

substrate: adiponitrile


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q55949 canonical sequence with reconstructed W146F substitution(s); RCSB 3WUY maps the structure entity to Q55949. and applied mutation signature W146F to reconstruct the assayed variant sequence.

smiles: C/C=C/C#N


sequence_source: UniProtKB:Q55949 canonical sequence with reconstructed W146F substitution(s); RCSB 3WUY maps the structure entity to Q55949.


sequence_source: UniProtKB:Q55949 canonical sequence; RCSB 3WUY maps the structure entity to Q55949.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q55949 canonical sequence with reconstructed W146Y substitution(s); RCSB 3WUY maps the structure entity to Q55949. and applied mutation signature W146Y to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q55949 canonical sequence with reconstructed W146Y substitution(s); RCSB 3WUY maps the structure entity to Q55949.


organism: Synechocystis sp. PCC 6803

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q55949 canonical sequence with reconstructed V198L substitution(s); RCSB 3WUY maps the structure entity to Q55949. and applied mutation signature V198L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q55949 canonical sequence with reconstructed W170G substitution(s); RCSB 3WUY maps the structure entity to Q55949. and applied mutation signature W170G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q55949 canonical sequence with reconstructed V198L/W170G substitution(s); RCSB 3WUY maps the structure entity to Q55949. and applied mutation signature V198L/W170G 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.


substrate_name: Succinonitrile

proof_lines: pH 7.5, temperature not specified in the publication

substrate: Succinonitrile


organism: uncultured bacterium

substrate_name: glutaronitrile

assay_conditions_summary: pH 7.5; 303.15 K; buffer 50 mM sodium phosphate

proof_lines: at 30°C in 50 mM sodium phosphate buffer (pH 7.5) and 1 mM dithiothreitol

substrate: glutaronitrile


organism: Aquifex aeolicus (strain VF5)

substrate_name: pre-tRNA(Gly)

substrate: pre-tRNA(Gly)


organism: Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)

substrate_name: pre-tRNA-Tyr in the absence of L7Ae

proof_lines: kcat 10 min(-1) in absence of L7Ae, 63 min(-1) in presence of L7Ae. Kinetic parameters determined at 37 degrees Celsius.

substrate: pre-tRNA-Tyr in the absence of L7Ae


organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

substrate_name: E.coli pre-tRNA(Tyr)

proof_lines: kcat is 9.5 min(-1). For enzyme reconstituted with RNA and 4 known subunits (Rnp1-4).

substrate: E.coli pre-tRNA(Tyr)


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

substrate_name: phenylacetonitrile

proof_lines: kcat is 111 min(-1) with phenylacetonitrile.

substrate: phenylacetonitrile


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9X1H4 FASTA; variant reconstructed by direct residue substitution and applied mutation signature K56A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9X1H4 FASTA; variant reconstructed by direct residue substitution and applied mutation signature F21A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession Q9X1H4 FASTA

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


sequence_source: UniProtKB reviewed accession Q9X1H4 FASTA checked as protein context only

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


sequence_source: UniProtKB reviewed accession Q9X1H4 FASTA checked as canonical protein context

proof_lines: recombinant mutant F17A/U52C, pH 7.5, 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9X1H4 FASTA; variant reconstructed by direct residue substitution and applied mutation signature R15A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession Q9X1H4 FASTA checked; variant not reconstructed


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9X1H4 FASTA; variant reconstructed by direct residue substitution and applied mutation signature R60A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9X1H4 FASTA; variant reconstructed by direct residue substitution and applied mutation signature R14A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9X1H4 FASTA; variant reconstructed by direct residue substitution and applied mutation signature K90A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9X1H4 FASTA; variant reconstructed by direct residue substitution and applied mutation signature K51A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9X1H4 FASTA; variant reconstructed by direct residue substitution and applied mutation signature R65A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P08594 and applied mutation signature G262D with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters of the wild-type and mutant enzymes), enzyme row G262D; column 'k cat (s -1 )' = 61.3 ± 1.86; column 'K m (mM)' = 0.93 ± 0.15; column 'k cat / K m (mM -1 s -1 )' = 66.2.

normalized_value_unit_evidence: kcat: printed Table 3 cell 61.3 ± 1.86 s^-1; the printed unit s^-1 is already canonical, so no factor applies and the cell is 61.3 s^(-1). Km: printed Table 3 cell 0.93 ± 0.15 mM; the printed unit mM is already canonical, so no factor applies and the cell is 0.93 mM. kcat/Km: printed Table 3 cell 66.2 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 66.2 s^-1 mM^-1.

row_label: Table 3, enzyme row G262D


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P08594 and applied mutation signature S277D with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters of the wild-type and mutant enzymes), enzyme row S277D; column 'k cat (s -1 )' = 73.6 ± 5.51; column 'K m (mM)' = 0.80 ± 0.12; column 'k cat / K m (mM -1 s -1 )' = 92.5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 73.6 ± 5.51 s^-1; the printed unit s^-1 is already canonical, so no factor applies and the cell is 73.6 s^(-1). Km: printed Table 3 cell 0.80 ± 0.12 mM; the printed unit mM is already canonical, so no factor applies and the cell is 0.8 mM. kcat/Km: printed Table 3 cell 92.5 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 92.5 s^-1 mM^-1.

row_label: Table 3, enzyme row S277D


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P08594 FASTA; variant reconstructed using UniProt mature-chain offset +127 and applied mutation signature D58N with inferred residue-numbering offset +127 to reconstruct the assayed variant sequence.


organism: Homo sapiens

substrate_name: SupS1 precursor

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

proof_lines: in 50 mM Tris /HCl pH 7.5, 100 mM NH4Cl, 5 mM MgCl2, 2.5 mM EGTA and 0.5 U Rnasin

substrate: SupS1 precursor


organism: Methanocaldococcus jannaschii

substrate_name: tRNA precursor

proof_lines: pH 8.0, 65°C, in presence of 800 mM ammonium acetate and 5 mM MgCl2

substrate: tRNA precursor


organism: Methanothermobacter thermautotrophicus

proof_lines: pH 8.0, 50°C, in presence of 50 mM ammonium acetate and 30 mM MgCl2


organism: Prochlorothrix hollandica


organism: Pyrococcus furiosus

substrate_name: ptRNATyr

proof_lines: enzyme subunit RNase P RNA + RNase P protein 21 + RNase P protein 29

proof_lines: from Escherichia coli, enzyme substrate Rnase P RNA

proof_lines: from Escherichia coli, emzyme subunit RNase P RNA + Pop5 + RNase P protein 30

substrate: ptRNATyr


organism: Pyrococcus horikoshii

proof_lines: wild-type enzyme, pH not specified in the publication, 65°C


organism: Saccharolobus solfataricus

substrate_name: tRNA

substrate: tRNA


organism: Saccharomyces cerevisiae

substrate_name: H2O; tRNA precursor

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

assay_conditions_summary: pH 8; 293.15 K; buffer 10 mM HEPES

proof_lines: pre-tRNA-Tyr with the 3-UUUUU trailer, at 20°C, pH 8.0, in 10 mM HEPES buffer with 10 mM MgCl2 and 100 mM KCl

proof_lines: pre-tRNA-Tyr without the 3-UUUUU trailer, at 20°C, pH 8.0, in 10 mM HEPES buffer with 10 mM MgCl2 and 100 mM KCl

substrate: H2O; tRNA precursor


organism: Schizosaccharomyces pombe

proof_lines: derived from the sup S1 and sup3-e tRNASer genes of Schizosaccharomyces pombe


organism: Spinacia oleracea

substrate_name: tRNAPhe (G+1) precursor

proof_lines: 37°C, substrate substituted with phosphothionate from GMPaS

substrate: tRNAPhe (G+1) precursor


organism: Thermotoga maritima

substrate_name: tRNATyr precursor

substrate: tRNATyr precursor


organism: Bos taurus

substrate_name: Unknown

proof_lines: inhibition of lysoPLD activity, > 60 microM, size of acyl chain is crucial for the maximal inhibitory action, spectrophotometric assay

proof_lines: > 60 microM, inhibition of lysoPLD activity, spectrophotometric assay

substrate: Unknown


enzyme_display_name: chitosanase

organism: Renibacterium sp. QD1

substrate_name: chitosan

enzyme: chitosanase

substrate: chitosan


organism: Streptomyces hygroscopicus


organism: Streptomyces sp.

substrate_name: chitohexaose

substrate: chitohexaose


organism: Sus scrofa

proof_lines:
40°C, pH 4, isoform PSC-II
40°C, pH 4, isoform PSC-I
40°C, pH 4, isoform PSC-III


organism: uncultured bacterium


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


enzyme_display_name: uracil-DNA glycosylase

organism: Aliivibrio salmonicida

substrate_name: dUMP DNA

enzyme: uracil-DNA glycosylase

substrate: dUMP DNA


organism: Archaeoglobus fulgidus

substrate_name: uracil-mismatched double-stranded DNA

substrate: uracil-mismatched double-stranded DNA


substrate_name: uracil-containing single-stranded DNA

substrate: uracil-containing single-stranded DNA


substrate_name: uracil-containing double-stranded DNA

substrate: uracil-containing double-stranded DNA


organism: Escherichia coli


organism: Gadus morhua

substrate_name: uracil-containing calf thymus DNA

proof_lines:
wild type enzyme, at pH 7.5 and 15°C
wild type enzyme, at pH 7.5 and 22°C
wild type enzyme, at pH 7.5 and 37°C

substrate: uracil-containing calf thymus DNA


organism: Solanum lycopersicum


organism: Solanum tuberosum

substrate_name: diphosphate

substrate: diphosphate


substrate_name: D-Fructose 6-phosphate; Diphosphate

substrate: D-Fructose 6-phosphate; Diphosphate


substrate_name: Diphosphate; D-Fructose 6-phosphate

substrate: Diphosphate; D-Fructose 6-phosphate


organism: Toxoplasma gondii

substrate_name: D-fructose 6-phosphate

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

substrate: D-fructose 6-phosphate


organism: Treponema pallidum


organism: Triticum aestivum

proof_lines: versus diphosphate, pH 7.5, 25°C, in presence of fructose 2,6-bisphosphate at saturating concentration

proof_lines: versus fructose 6-phosphate, pH 7.5, 25°C, in presence of fructose 2,6-bisphosphate at saturating concentration


organism: Vigna radiata

substrate_name: sedoheptulose 7-phosphate

proof_lines:
pH 8.0, 25°C
forward reaction, pH 8.0, 25°C

substrate: sedoheptulose 7-phosphate


organism: Aspergillus nidulans

substrate_name: pre-tRNAAsp

substrate: pre-tRNAAsp


organism: Bacillus subtilis

substrate_name: tRNA precursor; H2O

proof_lines:
enzyme RNA moiety, pH 7.0
catalyzed by RNase P RNA
catalyzed by circular RNnase P RNA

substrate: tRNA precursor; H2O


organism: Dictyostelium discoideum

substrate_name: pre-tRNA supS1 tRNASer

proof_lines: at 37°C, in 50 mM Tris/HCl pH 7.6, 10 mM NH4Cl, 5 mM MgCl2, and 5 mM dithiothreitol

substrate: pre-tRNA supS1 tRNASer


substrate_name: H2O; tRNA precursor

proof_lines:
pH 7.6, 37°C
37°C, pH 8.0
absence of spiramycin

substrate: H2O; tRNA precursor


organism: Carpodesmia tamariscifolia

substrate_name: 4-nitrocatechol sulfate

substrate: 4-nitrocatechol sulfate


organism: Chlamydomonas reinhardtii

substrate_name: 4-nitrophenyl sulfate

proof_lines:
without imidazole
with imidazole

substrate: 4-nitrophenyl sulfate


organism: Citrobacter braakii


organism: Eimeria tenella


organism: Gallus gallus

proof_lines: enzyme from fraction II and fraction III


organism: Haliotis iris

substrate_name: 2-hydroxy-5-nitrophenyl sulfate

proof_lines: in presence of 100 mM acetate and 100 mM sulfate

substrate: 2-hydroxy-5-nitrophenyl sulfate


organism: Helix pomatia

substrate_name: ferulic acid 4-sulfate

proof_lines: pH 7.0, temperature not specified in the publication

substrate: ferulic acid 4-sulfate


organism: Hemicentrotus pulcherrimus


organism: Homo sapiens

proof_lines: pH 5.0, 37°C, patient with cerebral palsy


organism: Littorina kurila

substrate_name: p-Nitrophenyl sulfate

substrate: p-Nitrophenyl sulfate


organism: Mus musculus

substrate_name: Unknown

substrate: Unknown


organism: Acinetobacter lwoffii

substrate_name: succinyl-CoA

substrate: succinyl-CoA


organism: Acrididae

substrate_name: Coenzyme A; 2-Oxoglutarate; NAD+

substrate: Coenzyme A; 2-Oxoglutarate; NAD+


organism: Columba sp.

substrate_name: NAD+; Coenzyme A; 2-Oxoglutarate

substrate: NAD+; Coenzyme A; 2-Oxoglutarate


organism: Fasciola hepatica

substrate_name: Coenzyme A; NAD+; 2-Oxoglutarate

substrate: Coenzyme A; NAD+; 2-Oxoglutarate


organism: Lucilia sericata

substrate_name: NAD+; 2-Oxoglutarate; Coenzyme A

substrate: NAD+; 2-Oxoglutarate; Coenzyme A


organism: Oncorhynchus mykiss

substrate_name: 2-Oxoglutarate; NAD+; Coenzyme A

substrate: 2-Oxoglutarate; NAD+; Coenzyme A


organism: Sus scrofa


organism: Rhodospirillum rubrum

substrate_name: phosphate

substrate: phosphate


organism: Ricinus communis

substrate_name: D-fructose 6-phosphate

proof_lines:
forward reaction, pH 7.5, 25°C
reverse reaction, pH 7.8, 25°C
pH 7.8, 25°C

substrate: D-fructose 6-phosphate


organism: Saccharum hybrid cultivar


organism: Sansevieria trifasciata

substrate_name: D-Fructose 6-phosphate; Diphosphate

proof_lines: pH 7.3, reverse reaction, in presence of 2 mM Mg2+

substrate: D-Fructose 6-phosphate; Diphosphate


organism: Hemiscorpius lepturus


substrate_name: lysophosphatidylcholine

proof_lines: kinetic analysis of recombinant autotaxin/lysoPLD using [14C] lysophosphatidylcholine substrate

proof_lines: in presence of 0.25 mM Zn2+ plus 10 mM L-histidine

substrate: lysophosphatidylcholine


proof_lines: substrate p-nitrophenyl thymidine 5-monophosphate, pH 8.0, 30 min of incubation at 37°C, measuring absorbance at 405 nm, twofold higher KI compared to inhibitor S1P


substrate_name: lysophosphatidylcholine 18:0

proof_lines: wild type enzyme, in 50 mM Tris pH 7.4, 5 mM CaCl2, 1 mg/ml bovine serum albumin, at 37°C

substrate: lysophosphatidylcholine 18:0


substrate_name: lysophosphatidylcholine 16:0

proof_lines: mutant enzyme H420Q, in 50 mM Tris pH 7.4, 5 mM CaCl2, 1 mg/ml bovine serum albumin, at 37°C

substrate: lysophosphatidylcholine 16:0


proof_lines: mutant enzyme H226Q, in 50 mM Tris pH 7.4, 5 mM CaCl2, 1 mg/ml bovine serum albumin, at 37°C


proof_lines: mutant enzyme H434Q, in 50 mM Tris pH 7.4, 5 mM CaCl2, 1 mg/ml bovine serum albumin, at 37°C


organism: Mammalia

substrate_name: coumarin-phosphate-fluorescein

proof_lines: coumarin-phosphate-fluorescein is a fluorescence resonance energy transfer (FRET)-based sensor of phosphodiesterase activity. Very useful substrate for enzymatic analysis of purified autotaxin/lysoPLD and can also be used to detect autotaxi

substrate: coumarin-phosphate-fluorescein


proof_lines: achieved under optimal assay conditions, almost same results in blood plasma

proof_lines: CPF4 FRET assay (change of fluorescence intensity), inihibition involves both a reduction in vmax and an increase in km, binding affinity is 1000fold stronger than to 1-alkyl-sn-glycero-3-phosphoethanolamine and analogue substrates


organism: Rattus norvegicus

proof_lines:
Vmax is 0.019 micromol/min/mg
Vmax is 0.035 micromol/min/mg
Vmax is 0.059 micromol/min/mg


organism: Streptomyces chromofuscus


organism: Aspergillus oryzae


enzyme_display_name: thioredoxin-dependent peroxiredoxin

organism: Treponema pallidum

substrate_name: thioredoxin; cumene hydroperoxide; H2O2; t-butyl hydroperoxide

proof_lines: pH 7.0, 25°C, TpAhpC with cumene hydroperoxide

enzyme: thioredoxin-dependent peroxiredoxin


smiles: OO


substrate_name: t-butyl hydroperoxide

smiles: CC(C)(C)OO

substrate: t-butyl hydroperoxide


organism: Trichoderma reesei

proof_lines:
pH 8, 25°C
at pH 7.2 and 30°C


organism: Vibrio vulnificus

substrate_name: reduced thioredoxin A; H2O2

substrate: reduced thioredoxin A; H2O2


organism: Xylella fastidiosa


substrate_name: cumene hydroperoxide; H2O2; t-butyl hydroperoxide


substrate_name: cumene hydroperoxide

substrate: cumene hydroperoxide


organism: Saccharomyces cerevisiae

substrate_name: DELTA1-Pyrroline-5-carboxylate; L-azetidine-2-carboxylic acid; cis-4-hydroxy-L-proline; L-azetidine-2-carboxylate

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

proof_lines:
at pH 7.5 and 30°C
at pH 8.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y168A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 303.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y75A to reconstruct the assayed variant sequence.


substrate_name: L-azetidine-2-carboxylic acid

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y166F to reconstruct the assayed variant sequence.

substrate: L-azetidine-2-carboxylic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature R145A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature R145W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature Y75A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature R145D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature R145G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature Y89A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature Y166F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature Y121A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature R145E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature Y157A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:E9P8D2 direct lookup plus single-substitution reconstruction and applied mutation signature Y168A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature Y89A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature R145E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature Y157A to reconstruct the assayed variant sequence.


substrate_name: acetyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature F65G to reconstruct the assayed variant sequence.

substrate: acetyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature K63R/L117V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature K63P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature K63R/F65L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature F65L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature F65L/L117V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature L117V to reconstruct the assayed variant sequence.


sequence_source: UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature


proof_lines: mutant enzyme LK63R/L117V, at pH 8.5 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB E9P8D2 direct REST check; variant sequence reconstructed from row mutation signature and applied mutation signature K63R/F65L/L117V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K63R/F65L/L117V, at pH 8.5 and 30°C


sequence_source: UniProtKB E9P8D2 direct REST check

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


organism: Pseudoalteromonas carrageenovora

substrate_name: p-Nitrophenyl sulfate

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

proof_lines: 6.5 nM purified arylsulfatase, at 45°C and pH 7.0

proof_lines: 6.5 nM purified arylsulfatase incubated at 45°C and at pH 7.0 in the presence of 10 mM sulfate

substrate: p-Nitrophenyl sulfate


organism: Pseudomonas aeruginosa

substrate_name: 4-nitrophenyl sulfate

proof_lines: mutant enzyme C51A, in 100 mM Tris, pH 8.0, 25°C

substrate: 4-nitrophenyl sulfate


substrate_name: 4-nitrophenyl phosphate

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

proof_lines: wild type enzyme, in 100 mM Tris, pH 8.0, 25°C

substrate: 4-nitrophenyl phosphate


proof_lines: mutant enzyme C51S, in 100 mM Tris, pH 8.0, 25°C


substrate_name: 4-nitrocatechol sulfate

proof_lines:
beta enzyme
pH 8.9, 30°C
alpha enzyme

substrate: 4-nitrocatechol sulfate


organism: Serratia sp. SM1


organism: Sphingomonas sp.


organism: Streptomyces griseorubiginosus

proof_lines:
in absence CaCl2
in presence of 1 mM CaCl2


organism: Strongylocentrotus intermedius

substrate_name: Ascorbate 2-sulfate

substrate: Ascorbate 2-sulfate


organism: Sus scrofa

substrate_name: epinephrine 4-sulfate

proof_lines:
pH 6.9
pH 7.4
arylsulfatase B

substrate: epinephrine 4-sulfate


organism: Renibacterium sp. QD1

substrate_name: chitosan

proof_lines: fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module PfCBM32-2 from Paenibacillus fukuinensis (CsnA-CBM32-2), pH 5.6, 55°C

proof_lines: fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module BgCBM5 from Burkholderia gladioli (CsnA-CBM5), pH 5.6, 55°C

proof_lines: fusion protein of Renibacterium sp. QD1 chitosanase CsnA and the carbohydrate binding module AoCBM35 from Amycolatopsis orientalis (CsnA-CBM35), pH 5.6, 55°C

substrate: chitosan


organism: Aeropyrum pernix

sequence_source: UniProtKB:Q9Y9L0 REST lookup, release 2026_02


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9Y9L0 canonical sequence with C207S reconstructed during review and applied mutation signature C207S to reconstruct the assayed variant sequence.


organism: Fasciola hepatica

sequence_source: UniProtKB:P91883 REST lookup, release 2026_02


organism: Lathyrus oleraceus

assay_conditions_summary: pH 8

proof_lines: wild type enzyme, in 25 mM Tris-HCl (pH 8)


organism: Salmonella enterica subsp. enterica serovar Typhimurium

proof_lines: in 50 mM potassium phosphate pH 7.0, at 25°C


organism: Seriola lalandi

sequence_source: UniProtKB:B9USM4 REST lookup, release 2026_02

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication, Prx197

proof_lines: pH 7.0, temperature not specified in the publication, Prx231


organism: Synechocystis sp. PCC 6803

substrate_name: thioredoxin Q

sequence_source: UniProtKB:P72719 REST lookup, release 2026_02

proof_lines: pH 7.0, temperature not specified in the publication

substrate: thioredoxin Q


substrate_name: thioredoxin A

sequence_source: UniProtKB:Q55624 REST lookup, release 2026_02

substrate: thioredoxin A


sequence_source: UniProtKB:P72697 REST lookup, release 2026_02


organism: Thunnus maccoyii

substrate_name: thioredoxin

sequence_source: UniProtKB:A9QKS0 REST lookup, release 2026_02

substrate: thioredoxin


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for E9P8D2 canonical MPR1 sequence plus selected mutation_signature reconstruction and applied mutation signature L117V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for E9P8D2 canonical MPR1 sequence plus selected mutation_signature reconstruction and applied mutation signature F65L/L117V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F65L/L117V, at pH 8.5 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for E9P8D2 canonical MPR1 sequence plus selected mutation_signature reconstruction and applied mutation signature K63R/F65L/L117V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for E9P8D2 canonical MPR1 sequence plus selected mutation_signature reconstruction and applied mutation signature K63R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for E9P8D2 canonical MPR1 sequence plus selected mutation_signature reconstruction and applied mutation signature K63R/F65L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for E9P8D2 canonical MPR1 sequence plus selected mutation_signature reconstruction and applied mutation signature F65G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for E9P8D2 canonical MPR1 sequence plus selected mutation_signature reconstruction and applied mutation signature K63R/L117V to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST direct lookup for E9P8D2 canonical MPR1 sequence plus selected mutation_signature reconstruction


sequence_source: UniProtKB REST direct lookup for E9P8D2 canonical MPR1 sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for E9P8D2 canonical MPR1 sequence plus selected mutation_signature reconstruction and applied mutation signature F65L to reconstruct the assayed variant sequence.


proof_lines: mutant enzyme K63R/F65L, at pH 8.5 and 30°C


organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)


organism: Gadus morhua

substrate_name: uracil-containing calf thymus DNA

proof_lines:
mutant enzyme G183D, at pH 7.5 and 15°C
mutant enzyme G183D, at pH 7.5 and 22°C
mutant enzyme G183D, at pH 7.5 and 37°C

substrate: uracil-containing calf thymus DNA


organism: Homo sapiens

substrate_name: uracil-mismatched double-stranded DNA with U-G mismatch

proof_lines:
pH 7.5, 30°C, recombinant hUNG2
pH 7.5


organism: Orthopoxvirus vaccinia

substrate_name: uracil-mismatched single-stranded DNA

substrate: uracil-mismatched single-stranded DNA


organism: Xenopus laevis


enzyme_display_name: acylaminoacyl-peptidase

organism: Cucumis sativus

substrate_name: N-acetyl-Ala-p-nitroanilide

enzyme: acylaminoacyl-peptidase

substrate: N-acetyl-Ala-p-nitroanilide


substrate_name: 4-nitrophenyl hexanoate

substrate: 4-nitrophenyl hexanoate


organism: Oryctolagus cuniculus

substrate_name: N-acetyl-Ala-Ala-Arg-Gly

substrate: N-acetyl-Ala-Ala-Arg-Gly


organism: Pyrococcus horikoshii

proof_lines:
pH 5.4, 85°C
pH 5.4, 85°C, heat-activated enzyme


organism: Rattus norvegicus

substrate_name: formylmethionine-Leu

substrate: formylmethionine-Leu


organism: Saccharolobus solfataricus

substrate_name: Unknown

substrate: Unknown


organism: Streptomyces morookaense

substrate_name: Phe-beta-naphthylamide

substrate: Phe-beta-naphthylamide


organism: Sus scrofa


organism: Cereibacter sphaeroides

proof_lines: PrxQ, in 50 mM HEPES/NaOH, pH 7.3, at 25°C

proof_lines: PrxT, in 50 mM HEPES/NaOH, pH 7.3, at 25°C


proof_lines:
pH 7.0, 37°C
Escherichia coli thioredoxin, at 25°C
Km below 0.0007 mM, at 25°C and pH 7.4


organism: Lathyrus oleraceus


organism: Leishmania infantum

substrate_name: tryparedoxin 2

substrate: tryparedoxin 2


organism: Mycobacterium tuberculosis variant bovis


organism: Plasmodium falciparum


organism: Toxoplasma gondii


organism: Saccharomyces cerevisiae

substrate_name: L-azetidine-2-carboxylic acid

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

substrate: L-azetidine-2-carboxylic acid


organism: Gadus morhua

proof_lines: mutant enzyme G183D/R302K, at pH 7.5 and 15°C

proof_lines: mutant enzyme G183D/R302K, at pH 7.5 and 22°C

proof_lines: mutant enzyme G183D/R302K, at pH 7.5 and 37°C


substrate_name: N-acetyl-Met-Ala

proof_lines:
wild-type enzyme
recombinant wild-type enzyme

substrate: N-acetyl-Met-Ala


organism: synthetic construct


organism: Trematomus bernacchii

proof_lines:
50°C, pH 8
15°C, pH 8


organism: Thermus aquaticus


proof_lines:
pH 7.5, 40°C, wild-type
40°C pH 7.5, wild-type
wild type enzyme, 40°C, pH 7.5


proof_lines:
pH 7.4, 40°C
pH 7.5, 40°C
pH 7.5, 40°C, presence of DMSO


enzyme_display_name: histone deacetylase

organism: Homo sapiens

substrate_name: Fluor de Lys HDAC8 substrate

proof_lines: presence of activator N-(phenylcarbamothioyl)benzamide, pH not specified in the publication, temperature not specified in the publication

enzyme: histone deacetylase

substrate: Fluor de Lys HDAC8 substrate


organism: Mus musculus

substrate_name: H2O; Acetylhistone

proof_lines: SABIO-RK modifier species: histone deacetylase(Enzyme) mutant

substrate: H2O; Acetylhistone


enzyme_display_name: cytidine deaminase

organism: Arabidopsis thaliana

substrate_name: deoxycytidine

proof_lines:
recombinant At-CDA1
recombinant AT-CDA
recombinant

enzyme: cytidine deaminase

substrate: deoxycytidine


organism: Brassica oleracea

substrate_name: cytosine beta-D-arabinofuranoside

substrate: cytosine beta-D-arabinofuranoside


organism: Canis lupus familiaris


organism: Crithidia fasciculata


organism: Escherichia coli

proof_lines: at pH 7.5 with H2O and pH 8.4 with H2O or D2O


substrate_name: cytidine

substrate: cytidine


sequence_source: UniProtKB reviewed accession E9P8D2 / MPR1_YEASX direct REST and FASTA lookup


proof_lines: tetramer of recombinant subunit CDA2, 37°C


substrate_name: cytosine arabinoside

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

substrate: cytosine arabinoside


proof_lines:
normal and leukemic spleen enzyme
leukemic spleen enzyme


organism: Nocardioides sp.

substrate_name: CMP

substrate: CMP


organism: Trypanosoma cruzi


organism: Cupriavidus necator


organism: Pannonibacter carbonis


organism: Pseudomonas sp.

substrate_name: potassium cyanide

substrate: potassium cyanide


organism: Pyrococcus abyssi

substrate_name: Malononitrile

proof_lines: in 20 mM potassium phosphate, pH 7.4, with 1 mM dithiothreitol, at 80°C

substrate: Malononitrile


organism: Rhodococcus rhodochrous

substrate_name: adiponitrile

substrate: adiponitrile


substrate_name: glutaronitrile

substrate: glutaronitrile


substrate_name: Crotonitrile

substrate: Crotonitrile


enzyme_display_name: low-specificity L-threonine aldolase

organism: Aeromonas veronii

substrate_name: D-threonine

proof_lines: pH 8.0, temperature not specified in the publication

enzyme: low-specificity L-threonine aldolase

substrate: D-threonine


substrate_name: L-threonine

substrate: L-threonine


substrate_name: L-allo-threonine

sequence_variant_note: Resolved canonical sequence from UniProt P75823 plus direct residue substitution reconstruction from selected mutation_signature and applied mutation signature H83N to reconstruct the assayed variant sequence.

substrate: L-allo-threonine


sequence_variant_note: Resolved canonical sequence from UniProt P75823 plus direct residue substitution reconstruction from selected mutation_signature and applied mutation signature H83F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P75823 plus direct residue substitution reconstruction from selected mutation_signature and applied mutation signature H83F/H126F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P75823 plus direct residue substitution reconstruction from selected mutation_signature and applied mutation signature K222A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P75823 plus direct residue substitution reconstruction from selected mutation_signature and applied mutation signature F87A to reconstruct the assayed variant sequence.


organism: Streptomyces coelicolor

substrate_name: L-Thr

assay_conditions_summary: pH 8; buffer 50 mM Tris-HCl

proof_lines: mutant enzyme H177Y, in 50 mM Tris-HCl buffer (pH 8.0)

substrate: L-Thr


proof_lines: recombinant wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0)


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

proof_lines: kcat is 4.5 sec(-1) for H(2)O(2). kcat is 2.75 sec(-1) for thioredoxin.


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

proof_lines: kcat is 12.53 sec(-1) with H(2)O(2) as substrate and 12.96 sec(-1) with tert-butyl hydroperoxide as substrate.


organism: Chlamydomonas reinhardtii

proof_lines: kcat is 7.4 sec(-1) for the reduction of hydrogen peroxide (with cytosolic thioredoxin) (at 30 degrees Celsius and pH 7.9) (PubMed:19690965). kcat is 7.4 sec(-1) for the reduction of tert-butyl hydroperoxide (with cytosolic thioredoxin) (at


organism: Escherichia coli (strain K12)

proof_lines: kcat is 76.0 sec(-1) with H(2)O(2) as substrate and 70.1 sec(-1) with cumene hydroperoxide as substrate.


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: tert-butyl hydroperoxide (using thioredoxin TrxB as electron donor)

proof_lines: kcat is 0.70 sec(-1) with tert-butyl hydroperoxide as substrate and TrxB as reductant and 11.1 sec(-1) with tert-butyl hydroperoxide as substrate and TrxC as reductant.


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: H(2)O(2) (in the presence of 5 mM DTT)

proof_lines: kcat is 67 min(-1) with H(2)O(2) as substrate (PubMed:11231293). kcat is 56 min(-1) with t-butylhydroperoxide as substrate (PubMed:11231293). kcat is 41 min(-1) with cumene hydroperoxide as substrate (PubMed:11231293).

substrate: H(2)O(2) (in the presence of 5 mM DTT)


substrate_name: H(2)O(2) (in the presence of TRX1)

proof_lines: kcat is 7.5 sec(-1) with H(2)O(2) as substrate (in the presence of TRX1) (PubMed:16879648). kcat is 15.0 sec(-1) with H(2)O(2) as substrate (in the presence of TRX2) (PubMed:16879648). kcat is 8.3 sec(-1) with ert-butylhydroperoxide as subs

substrate: H(2)O(2) (in the presence of TRX1)


organism: Saccharomyces cerevisiae

proof_lines: kcat is 17.9 sec(-1) with azetidine-2-carboxylate as substrate and 121 sec(-1) with (S)-1-pyrroline-5-carboxylate as substrate.


enzyme_display_name: ornithine decarboxylase

organism: Aquifex aeolicus

substrate_name: L-Ornithine

sequence_source: UniProt O66940 canonical sequence from direct accession lookup

enzyme: ornithine decarboxylase

substrate: L-Ornithine


organism: Atropa belladonna

substrate_name: L-ornithine

sequence_source: UniProt A0A060IEJ3 canonical sequence from direct accession lookup

substrate: L-ornithine


organism: Bartonella henselae

sequence_source: UniProt A0A0R4J8C9 canonical sequence from direct accession lookup


organism: Caldisericum exile

substrate_name: L-arginine

substrate: L-arginine


organism: Clostridium botulinum


organism: Erythroxylum coca

sequence_source: UniProt G4XUJ8 canonical sequence from direct accession lookup


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from UniProt P21169 canonical sequence with selected mutation signature I163A reconstructed and applied mutation signature I163A to reconstruct the assayed variant sequence.

proof_lines: mutant I163A, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt P21169 canonical sequence with selected mutation signature I163V reconstructed and applied mutation signature I163V to reconstruct the assayed variant sequence.

proof_lines: mutant I163V, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt P21169 canonical sequence with selected mutation signature E165V reconstructed and applied mutation signature E165V to reconstruct the assayed variant sequence.

proof_lines: mutant E165V, pH 7.0, temperature not specified in the publication


sequence_source: UniProt P21169 canonical sequence from direct accession lookup

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


sequence_variant_note: Resolved canonical sequence from UniProt P21169 canonical sequence with selected mutation signature I163T/E165T reconstructed and applied mutation signature I163T/E165T to reconstruct the assayed variant sequence.

proof_lines: mutant I163T/E165T, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt P21169 canonical sequence with selected mutation signature E165S reconstructed and applied mutation signature E165S to reconstruct the assayed variant sequence.

proof_lines: mutant E165S, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt P21169 canonical sequence with selected mutation signature E165G reconstructed and applied mutation signature E165G to reconstruct the assayed variant sequence.

proof_lines: mutant E165G, pH 7.0, temperature not specified in the publication


organism: Nicotiana glutinosa

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup for Q9FPK5 and applied mutation signature K95A to reconstruct the assayed variant sequence.


substrate_name: L-Lysine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9FPK5 and applied mutation signature C338A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.8; 310.15 K; buffer 40 mM potassium phosphate

column_label: Table 2(B) of Table 2: Kinetic analysis of N. glutinosa ODC mutants by using L-ornithine or L-lysine as the substrate (Biochem. J. 2001, 360, 657-665), enzyme row 'C338A'; column 'Km (uM)' = 1114; column 'Vmax (nmol/min per mg)' = 0.150; column 'kcat (s^-1)' = 0.204; column 'kcat/Km (M^-1 s^-1)' = 183.21; column 'Optimal pH' = 7.6.

normalized_value_unit_evidence: Km: printed Table 2(B) cell 1114 uM; 1114 / 1000 = 1.114 mM. kcat: printed Table 2(B) cell 0.204 s^-1; the cell is already in s^-1 and no unit conversion applies. kcat/Km: printed Table 2(B) cell 183.21 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 183.21 / 1000 = 0.18321 s^-1 mM^-1.

raw_value_unit_evidence: Table 2(B), enzyme row 'C338A', L-Lysine as the varied substrate: Km = 1114 uM; kcat = 0.204 s^-1; printed kcat/Km = 183.21 M^-1 s^-1.

substrate: L-Lysine


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup for Q9FPK5 and applied mutation signature C377A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB direct accession lookup for Q9FPK5

assay_conditions_summary: pH 8; 310.15 K; buffer 40 mM Tris/HCl

column_label: Table 2(A) of Table 2: Kinetic analysis of N. glutinosa ODC mutants by using L-ornithine or L-lysine as the substrate (Biochem. J. 2001, 360, 657-665), enzyme row 'WT'; column 'Km (uM)' = 562; column 'Vmax (nmol/min per mg)' = 12.54; column 'kcat (s^-1)' = 77.78; column 'kcat/Km (M^-1 s^-1)' = 1.5 x 10^5; column 'Optimal pH' = 8.0.

normalized_value_unit_evidence: Km: printed Table 2(A) cell 562 uM; 562 / 1000 = 0.562 mM. kcat: printed Table 2(A) cell 77.78 s^-1; the cell is already in s^-1 and no unit conversion applies. kcat/Km: printed Table 2(A) cell 1.5 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 150000 / 1000 = 150.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2(A), enzyme row 'WT', L-Ornithine as the varied substrate: Km = 562 uM; kcat = 77.78 s^-1; printed kcat/Km = 1.5 x 10^5 M^-1 s^-1.

row_label: Table 2(A), enzyme row 'WT' (wild type), L-Ornithine as the varied substrate


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup for Q9FPK5 and applied mutation signature C338A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant C338A


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant C377A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9FPK5 and applied mutation signature C96A to reconstruct the assayed variant sequence.

column_label: Table 2(A) of Table 2: Kinetic analysis of N. glutinosa ODC mutants by using L-ornithine or L-lysine as the substrate (Biochem. J. 2001, 360, 657-665), enzyme row 'C96A'; column 'Km (uM)' = 812; column 'Vmax (nmol/min per mg)' = 11.22; column 'kcat (s^-1)' = 32.73; column 'kcat/Km (M^-1 s^-1)' = 4.1 x 10^4; column 'Optimal pH' = 8.6.

normalized_value_unit_evidence: Km: printed Table 2(A) cell 812 uM; 812 / 1000 = 0.812 mM. kcat: printed Table 2(A) cell 32.73 s^-1; the cell is already in s^-1 and no unit conversion applies. kcat/Km: printed Table 2(A) cell 4.1 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 41000 / 1000 = 41.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2(A), enzyme row 'C96A', L-Ornithine as the varied substrate: Km = 812 uM; kcat = 32.73 s^-1; printed kcat/Km = 4.1 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup for Q9FPK5 and applied mutation signature C115A to reconstruct the assayed variant sequence.


organism: Nitrosomonas europaea

sequence_source: UniProtKB direct accession lookup for Q82VZ0


organism: Oenococcus oeni

sequence_source: UniProtKB direct accession lookup for Q5ZH57

column_label: Table 1: Steady-state kinetic parameters and substrate specificities of the four decarboxylases (Applied and Environmental Microbiology 2012, 78(6):1953-1961); leading columns 'Microorganism' = 'O. oeni' and 'Reaction pH' = '5.5'; within the 'Ornithine' substrate block the column 'kcat (min^-1)' = 416, the column 'Km (mM)' = 0.7 and the column 'kcat/Km (M^-1 min^-1)' = 5.5 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 1 cell 416 min^-1; one min^-1 is 1/60 s^-1, so 416 / 60 = 6.933333333333334 s^(-1). Km: printed Table 1 cell 0.7 mM; no unit conversion applies, so the canonical value is 0.7 mM. kcat/Km: printed Table 1 cell 5.5 x 10^5 M^-1 min^-1; one M^-1 is 0.001 mM^-1 and one min^-1 is 1/60 s^-1, so 550000 / 60000 = 9.166666666666668 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Microorganism row 'O. oeni' at Reaction pH 5.5, 'Ornithine' substrate block: printed kcat cell 416 min^-1; printed Km cell 0.7 mM; printed kcat/Km cell 5.5 x 10^5 M^-1 min^-1.

row_label: Table 1, Microorganism row 'O. oeni' at Reaction pH 5.5, Ornithine substrate block


column_label: Table 1: Steady-state kinetic parameters and substrate specificities of the four decarboxylases (Applied and Environmental Microbiology 2012, 78(6):1953-1961); leading columns 'Microorganism' = 'O. oeni' and 'Reaction pH' = '5.5'; within the 'DABA' substrate block the column 'kcat (min^-1)' = 2.7, the column 'Km (mM)' = 4.9 and the column 'kcat/Km (M^-1 min^-1)' = 0.5 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.7 min^-1; one min^-1 is 1/60 s^-1, so 2.7 / 60 = 0.045000000000000005 s^(-1). Km: printed Table 1 cell 4.9 mM; no unit conversion applies, so the canonical value is 4.9 mM. kcat/Km: printed Table 1 cell 0.5 x 10^3 M^-1 min^-1; one M^-1 is 0.001 mM^-1 and one min^-1 is 1/60 s^-1, so 500 / 60000 = 0.008333333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Microorganism row 'O. oeni' at Reaction pH 5.5, 'DABA' substrate block: printed kcat cell 2.7 min^-1; printed Km cell 4.9 mM; printed kcat/Km cell 0.5 x 10^3 M^-1 min^-1.

row_label: Table 1, Microorganism row 'O. oeni' at Reaction pH 5.5, DABA substrate block


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21169 REST lookup plus selected row mutation signature E165A and applied mutation signature E165A to reconstruct the assayed variant sequence.

proof_lines: mutant E165A, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21169 REST lookup plus selected row mutation signature I163S and applied mutation signature I163S to reconstruct the assayed variant sequence.

proof_lines: mutant I163S, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21169 REST lookup plus selected row mutation signature I163T and applied mutation signature I163T to reconstruct the assayed variant sequence.

proof_lines: mutant I163T, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21169 REST lookup plus selected row mutation signature I163V/E165V and applied mutation signature I163V/E165V to reconstruct the assayed variant sequence.

proof_lines: mutant I163V/E165V, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21169 REST lookup plus selected row mutation signature E165T and applied mutation signature E165T to reconstruct the assayed variant sequence.

proof_lines: mutant E165T, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21169 REST lookup plus selected row mutation signature I163G and applied mutation signature I163G to reconstruct the assayed variant sequence.

proof_lines: mutant I163G, pH 7.0, temperature not specified in the publication


organism: Giardia lamblia

sequence_source: UniProtKB:A8BFD3 REST lookup

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


organism: Homo sapiens

sequence_source: UniProtKB:P11926 REST lookup


organism: Hyoscyamus niger

sequence_source: UniProtKB:A0A4D6ZW66 REST lookup

proof_lines: pH 8.0, temperature not specified in the publication


organism: Lacticaseibacillus casei

sequence_source: UniProtKB:Q038E5 REST lookup


column_label: Table 1: Steady-state kinetic parameters and substrate specificities of the four decarboxylases (Applied and Environmental Microbiology 2012, 78(6):1953-1961); leading columns 'Microorganism' = 'L. casei' and 'Reaction pH' = '7.5'; within the 'DABA' substrate block the column 'kcat (min^-1)' = 3, the column 'Km (mM)' = 3.9 and the column 'kcat/Km (M^-1 min^-1)' = 0.7 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3 min^-1; one min^-1 is 1/60 s^-1, so 3 / 60 = 0.05 s^(-1). Km: printed Table 1 cell 3.9 mM; no unit conversion applies, so the canonical value is 3.9 mM. kcat/Km: printed Table 1 cell 0.7 x 10^3 M^-1 min^-1; one M^-1 is 0.001 mM^-1 and one min^-1 is 1/60 s^-1, so 700 / 60000 = 0.011666666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Microorganism row 'L. casei' at Reaction pH 7.5, 'DABA' substrate block: printed kcat cell 3 min^-1; printed Km cell 3.9 mM; printed kcat/Km cell 0.7 x 10^3 M^-1 min^-1.

row_label: Table 1, Microorganism row 'L. casei' at Reaction pH 7.5, DABA substrate block


organism: Lactobacillus gasseri

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


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


organism: Lactobacillus sp.

sequence_source: UniProtKB:P43099 REST lookup


organism: Lactobacillus sp. 30a

substrate_name: L-lysine

sequence_variant_note: Resolved canonical sequence from uniprot_accession:P43099|reviewed_swiss_prot|direct_rest_lookup_run_20260616-233539 and applied mutation signature E698D/A713L to reconstruct the assayed variant sequence.

substrate: L-lysine


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P43099|reviewed_swiss_prot|direct_rest_lookup_run_20260616-233539 and applied mutation signature E698D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P43099|reviewed_swiss_prot|direct_rest_lookup_run_20260616-233539 and applied mutation signature A713L to reconstruct the assayed variant sequence.


organism: Leishmania donovani


substrate_name: L-Arginine

substrate: L-Arginine


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P27116|reviewed_swiss_prot|direct_rest_lookup_run_20260616-233539 and applied mutation signature K69A/C360A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant K69A:C360A heterodimer N-terminal His6-tagged


organism: Levilactobacillus brevis

column_label: Table 1: Steady-state kinetic parameters and substrate specificities of the four decarboxylases (Applied and Environmental Microbiology 2012, 78(6):1953-1961); leading columns 'Microorganism' = 'L. brevis' and 'Reaction pH' = '5.5'; within the 'Ornithine' substrate block the column 'kcat (min^-1)' = 290, the column 'Km (mM)' = 1.0 and the column 'kcat/Km (M^-1 min^-1)' = 2.8 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 1 cell 290 min^-1; one min^-1 is 1/60 s^-1, so 290 / 60 = 4.833333333333333 s^(-1). Km: printed Table 1 cell 1.0 mM; no unit conversion applies, so the canonical value is 1.0 mM. kcat/Km: printed Table 1 cell 2.8 x 10^5 M^-1 min^-1; one M^-1 is 0.001 mM^-1 and one min^-1 is 1/60 s^-1, so 280000 / 60000 = 4.666666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Microorganism row 'L. brevis' at Reaction pH 5.5, 'Ornithine' substrate block: printed kcat cell 290 min^-1; printed Km cell 1.0 mM; printed kcat/Km cell 2.8 x 10^5 M^-1 min^-1.

row_label: Table 1, Microorganism row 'L. brevis' at Reaction pH 5.5, Ornithine substrate block


column_label: Table 1: Steady-state kinetic parameters and substrate specificities of the four decarboxylases (Applied and Environmental Microbiology 2012, 78(6):1953-1961); leading columns 'Microorganism' = 'L. brevis' and 'Reaction pH' = '5.5'; within the 'L-Lysine' substrate block the column 'kcat (min^-1)' = 34, the column 'Km (mM)' = 7.2 and the column 'kcat/Km (M^-1 min^-1)' = 4.6 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 34 min^-1; one min^-1 is 1/60 s^-1, so 34 / 60 = 0.5666666666666667 s^(-1). Km: printed Table 1 cell 7.2 mM; no unit conversion applies, so the canonical value is 7.2 mM. kcat/Km: printed Table 1 cell 4.6 x 10^3 M^-1 min^-1; one M^-1 is 0.001 mM^-1 and one min^-1 is 1/60 s^-1, so 4600 / 60000 = 0.07666666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Microorganism row 'L. brevis' at Reaction pH 5.5, 'L-Lysine' substrate block: printed kcat cell 34 min^-1; printed Km cell 7.2 mM; printed kcat/Km cell 4.6 x 10^3 M^-1 min^-1.

row_label: Table 1, Microorganism row 'L. brevis' at Reaction pH 5.5, L-Lysine substrate block


organism: Ligilactobacillus saerimneri 30a


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

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

proof_lines:
pH 5.5, 37°C
Raw SKiD Env: Temp=37°C, pH=5.5

source_databases_merged: brenda skid


organism: Methanosarcina mazei


organism: Mus musculus


sequence_source: Reconstructed from UniProtKB:P00860

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P00860 and applied mutation signature K69A/C360A to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant mouse-K69A:trypanosoma-C360A heterodimer N-terminal His6-tagged


organism: Neurospora crassa


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9FPK5 and applied mutation signature C96A to reconstruct the assayed variant sequence.

column_label: Table 2(B) of Table 2: Kinetic analysis of N. glutinosa ODC mutants by using L-ornithine or L-lysine as the substrate (Biochem. J. 2001, 360, 657-665), enzyme row 'C96A'; column 'Km (uM)' = 1094; column 'Vmax (nmol/min per mg)' = 0.133; column 'kcat (s^-1)' = 0.207; column 'kcat/Km (M^-1 s^-1)' = 188.83; column 'Optimal pH' = 6.8.

normalized_value_unit_evidence: Km: printed Table 2(B) cell 1094 uM; 1094 / 1000 = 1.094 mM. kcat: printed Table 2(B) cell 0.207 s^-1; the cell is already in s^-1 and no unit conversion applies. kcat/Km: printed Table 2(B) cell 188.83 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 188.83 / 1000 = 0.18883 s^-1 mM^-1.

raw_value_unit_evidence: Table 2(B), enzyme row 'C96A', L-Lysine as the varied substrate: Km = 1094 uM; kcat = 0.207 s^-1; printed kcat/Km = 188.83 M^-1 s^-1.


sequence_source: Reconstructed from UniProtKB:Q9FPK5

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q9FPK5 and applied mutation signature C96A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant C96A


column_label: Table 2(B) of Table 2: Kinetic analysis of N. glutinosa ODC mutants by using L-ornithine or L-lysine as the substrate (Biochem. J. 2001, 360, 657-665), enzyme row 'WT'; column 'Km (uM)' = 1592; column 'Vmax (nmol/min per mg)' = 0.152; column 'kcat (s^-1)' = 0.236; column 'kcat/Km (M^-1 s^-1)' = 148.00; column 'Optimal pH' = 6.8.

normalized_value_unit_evidence: Km: printed Table 2(B) cell 1592 uM; 1592 / 1000 = 1.592 mM. kcat: printed Table 2(B) cell 0.236 s^-1; the cell is already in s^-1 and no unit conversion applies. kcat/Km: printed Table 2(B) cell 148.00 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 148 / 1000 = 0.148 s^-1 mM^-1.

raw_value_unit_evidence: Table 2(B), enzyme row 'WT', L-Lysine as the varied substrate: Km = 1592 uM; kcat = 0.236 s^-1; printed kcat/Km = 148.00 M^-1 s^-1.

row_label: Table 2(B), enzyme row 'WT' (wild type), L-Lysine as the varied substrate


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q9FPK5 and applied mutation signature K95A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant K95A


enzyme_display_name: 4-hydroxybenzoate 3-monooxygenase

organism: Cupriavidus pinatubonensis

substrate_name: NADPH

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

enzyme: 4-hydroxybenzoate 3-monooxygenase

substrate: NADPH


proof_lines: pH 7.5, 30°C, recombinant enzyme PHBHCn2, via UV/VIS-NAD(P)H consumption determination, with NADPH

proof_lines: pH 7.5, 30°C, recombinant enzyme PHBHCn2, via product determination per HPLC, with NADPH


organism: Pseudomonas aeruginosa

sequence_variant_note: Resolved canonical sequence from UniProtKB:P20586 canonical FASTA with L199V and Y385F substitutions applied after residue check and applied mutation signature L199V/Y385F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P20586 canonical FASTA direct lookup


proof_lines: pH 8.0, 30°C, wild-type enzyme, with NADPH


sequence_source: UniProtKB:P20586 canonical FASTA with L199V and Y385F substitutions applied after residue check


sequence_source: UniProtKB:P20586 canonical FASTA used only as context; row-specific DA015/DA016 variant was not reconstructable from the selected batch

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

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

proof_lines:
pH 8.0, 30°C, mutant DA015, with NADPH
pH 8.0, 30°C, mutant DA016, with NADPH


source_db: skid

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=30°C, pH=7.5

source: skid


enzyme_display_name: dextransucrase

organism: Lactobacillus hilgardii

substrate_name: Sucrose; Dextran

sequence_source: UniProtKB:E1UYR9 FASTA direct lookup

enzyme: dextransucrase

substrate: Sucrose; Dextran


organism: Leuconostoc citreum

sequence_source: UniProtKB:D5FS20 FASTA direct lookup

proof_lines: recombinant enzyme, pH 5.0, 30°C, in presence of Ca2+


organism: Leuconostoc lactis

substrate_name: sucrose

substrate: sucrose


organism: Leuconostoc mesenteroides


organism: Oenococcus oeni

sequence_source: UniProtKB direct accession lookup: Q5ZH57

column_label: Table 1: Steady-state kinetic parameters and substrate specificities of the four decarboxylases (Applied and Environmental Microbiology 2012, 78(6):1953-1961); leading columns 'Microorganism' = 'O. oeni' and 'Reaction pH' = '5.5'; within the 'L-Lysine' substrate block the column 'kcat (min^-1)' = 5.6, the column 'Km (mM)' = 5.0 and the column 'kcat/Km (M^-1 min^-1)' = 1.1 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.6 min^-1; one min^-1 is 1/60 s^-1, so 5.6 / 60 = 0.09333333333333332 s^(-1). Km: printed Table 1 cell 5.0 mM; no unit conversion applies, so the canonical value is 5.0 mM. kcat/Km: printed Table 1 cell 1.1 x 10^3 M^-1 min^-1; one M^-1 is 0.001 mM^-1 and one min^-1 is 1/60 s^-1, so 1100 / 60000 = 0.018333333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Microorganism row 'O. oeni' at Reaction pH 5.5, 'L-Lysine' substrate block: printed kcat cell 5.6 min^-1; printed Km cell 5.0 mM; printed kcat/Km cell 1.1 x 10^3 M^-1 min^-1.

row_label: Table 1, Microorganism row 'O. oeni' at Reaction pH 5.5, L-Lysine substrate block


organism: Panagrellus redivivus

sequence_source: UniProtKB direct accession lookup: P49725


organism: Paramecium bursaria chlorella virus 1

sequence_source: UniProtKB direct accession lookup: Q84527


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup: Q84527 and applied mutation signature E296D to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant His-tagged E296D


sequence_source: UniProtKB direct accession lookup: Q9HVQ3


organism: Rattus norvegicus

sequence_source: UniProtKB direct accession lookup: P09057


organism: Selenomonas ruminantium

sequence_source: UniProtKB direct accession lookup: O50657


organism: Thermotoga maritima

sequence_source: UniProtKB direct accession lookup: Q9X2I6


organism: Trypanosoma brucei

sequence_source: UniProtKB direct accession lookup: P07805


proof_lines: pH 5.2, 25°C, recombinant mutant H463R/T464V/S512T


proof_lines: pH 5.2, 25°C, recombinant mutant H463R/T464D/S512T


proof_lines: pH 5.2, 25°C, recombinant mutant D460A/H463S/T464L


proof_lines: pH 5.2, 25°C, recombinant mutant D460M/H463Y/T464M/S512C


sequence_source: UniProtKB Q2I2N5 direct lookup

proof_lines: recombinant wild-type enzyme dexYG, pH 5.4, 25°C


proof_lines: recombinant enzyme variant D-F, pH 5.4, 25°C


proof_lines: recombinant enzyme mutant DELTAN190LmDexA, pH 5.6, 30°C


substrate_name: Dextran

sequence: DSTNY

wild_type_sequence: DSTNY

sequence_source: UniProtKB direct accession lookup P85089 (https://rest.uniprot.org/uniprotkb/P85089.json)

proof_lines: pH 5.5, 45°C, isozyme DS-II, low dextran substrate concentration

proof_lines: pH 5.5, 45°C, isozyme DS-II, high dextran substrate concentration

substrate: Dextran


sequence: DSTNTV

wild_type_sequence: DSTNTV

sequence_source: UniProtKB direct accession lookup P85080 (https://rest.uniprot.org/uniprotkb/P85080.json)

proof_lines: pH 5.5, 45°C, isozyme DS-III, low dextran substrate concentration

proof_lines: pH 5.5, 45°C, isozyme DS-III, high dextran substrate concentration


sequence_source: UniProtKB direct accession lookup B2MUU6 (https://rest.uniprot.org/uniprotkb/B2MUU6.json)

proof_lines: pH 5.5, 45°C, isozyme DS-I, low dextran substrate concentration

proof_lines: pH 5.5, 45°C, isozyme DS-I, high dextran substrate concentration


organism: Streptococcus mutans


substrate_name: Dextran; Sucrose

substrate: Dextran; Sucrose


organism: Weissella cibaria

sequence_source: UniProtKB direct accession lookup B9UNL6 (https://rest.uniprot.org/uniprotkb/B9UNL6.json)


organism: Weissella confusa


sequence_source: UniProtKB direct accession lookup X4QKX0 (https://rest.uniprot.org/uniprotkb/X4QKX0.json)

proof_lines:
pH 5.4, 35°C, recombinant enzyme
pH 5.0, 35°C


enzyme_display_name: phospholipase A2

organism: Clonorchis sinensis

substrate_name: phosphatidylcholine

sequence_source: UniProtKB direct accession lookup C6YBD6 (https://rest.uniprot.org/uniprotkb/C6YBD6.json)

assay_conditions_summary: pH 8.5; 313.15 K; buffer 100 mM Tris-HCl

proof_lines: recombinant group III sPLA2, in 100 mM Tris-HCl buffer, pH 8.5, at 40°C, 50 mM sodium bis(2-ethylhexyl) sulfosuccinate and 0.05mM phenolsulfonphthalein in isooctane

enzyme: phospholipase A2

substrate: phosphatidylcholine


organism: Crotalus durissus terrificus

substrate_name: 1-Palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid; H2O


substrate: 1-Palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid; H2O


sequence_source: UniProtKB direct accession lookup P0CG56 (https://rest.uniprot.org/uniprotkb/P0CG56.json)


substrate_name: H2O; 1-Palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid

sequence_source: UniProtKB direct accession lookup P24027 (https://rest.uniprot.org/uniprotkb/P24027.json)


sequence_source: UniProtKB:P07805 reconstructed variant

sequence_variant_note: Mutation signature D361A matches the mutant residue at offset -2 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07805 reconstructed variant and applied mutation signature D88A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07805 reconstructed variant and applied mutation signature D361E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant D88A N-terminal His6-tagged


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

proof_lines:
Ki above 0.1 mM, at pH 7.5 and 37°C
at pH 7.5 and 37°C
Raw SKiD Env: Temp=37°C, pH=7.5

source_databases_merged: sabio_rk brenda skid


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant K69A:C360A heterodimer N-terminal His6-tagged


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant trypanosoma-K69A:mouse-C360A heterodimer N-terminal His6-tagged


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


organism: Trypanosoma brucei brucei

sequence_variant_note: Resolved canonical sequence from UniProtKB:P07805 reconstructed variant and applied mutation signature F397A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant F397A


organism: Vibrio vulnificus


organism: Xenopus laevis

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


organism: Acanthophis antarcticus

substrate_name: Unknown

sequence: NLLQFGFMIRCANKRRRPVWPYEESGC

wild_type_sequence: NLLQFGFMIRCANKRRRPVWPYEESGC

substrate: Unknown


organism: Agkistrodon piscivorus leucostoma

substrate_name: 4-nitro-3-(octanoyloxy) benzoic acid (NOBA)


organism: Anuroctonus phaiodactylus


organism: Arabidopsis thaliana


organism: Beauveria bassiana (strain ARSEF 2860)

substrate_name: phosphatidyl-choline

substrate: phosphatidyl-choline


organism: Bitis arietans

sequence: SLIEFGKMITEETNRPVFPYEATIVVCDCGNGNGS

wild_type_sequence: SLIEFGKMITEETNRPVFPYEATIVVCDCGNGNGS


organism: Bos taurus

assay_conditions_summary: pH 4


organism: Bothrocophias hyoprora

substrate: 4-nitro-3-(octanoyloxy) benzoic acid (NOBA)


organism: Bothrops bilineatus smaragdinus


sequence_source: UniProtKB direct accession lookup: P62022


sequence_source: UniProtKB direct accession lookup: P08878 and P62022

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

substrate: H2O; 1-Palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid


organism: Crotalus lutosus

substrate_name: 4-nitro-3-octanoyloxy benzoic acid

sequence_source: UniProtKB direct accession lookup: C0HK05

substrate: 4-nitro-3-octanoyloxy benzoic acid


organism: Crotalus viridis lutosus


organism: Daboia russelii russelii

substrate_name: soya lecithin

sequence_source: UniProtKB direct accession lookup: P59071

proof_lines: at pH 8.9, temperature not specified in the publication

substrate: soya lecithin


organism: Echis carinatus

substrate_name: Phosphatidylcholine; H2O

sequence_source: UniProtKB direct accession lookup: Q7T3S7

substrate: Phosphatidylcholine; H2O


organism: Homo sapiens

sequence_source: UniProtKB direct accession lookup: Q13093

proof_lines: pH 7.4, 37°C, recombinant His-tagged Lp-PLA2


sequence_source: UniProtKB direct accession lookup: P14555


organism: Mus musculus

sequence_source: UniProtKB direct accession lookup: P47713


organism: Oryctolagus cuniculus

sequence_source: UniProtKB direct accession lookup: P14422

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


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB direct accession lookup: Q12405


organism: Sus scrofa

sequence_source: UniProtKB direct accession lookup: P00592

proof_lines: mutant A12T/H15D/M20L/E71N, pH 8.0, 24°C


proof_lines:
pH 8.5, 37°C
Raw SKiD Env: Temp=24°C, pH=8


enzyme_display_name: myeloblastin

sequence_source: UniProtKB direct accession lookup: P24158

proof_lines: 52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0

proof_lines: pH and temperature not specified in the publication

enzyme: myeloblastin


sequence_source: UniProtKB direct accession lookup: Q61096


enzyme_display_name: acetylspermidine deacetylase

organism: Danio rerio

sequence_source: UniProtKB reviewed F1QCV2 canonical protein sequence, checked directly on 2026-06-17.

enzyme: acetylspermidine deacetylase


sequence_variant_note: Resolved canonical sequence from F1QCV2 canonical sequence with row-specific N93A substitution reconstructed after direct residue check on 2026-06-17. and applied mutation signature N93A to reconstruct the assayed variant sequence.

smiles: CC(=O)NCCCCNCCCN


sequence_variant_note: Resolved canonical sequence from F1QCV2 canonical sequence with row-specific E274L substitution reconstructed after direct residue check on 2026-06-17. and applied mutation signature E274L to reconstruct the assayed variant sequence.


substrate_name: Acetylcadaverine

smiles: CC(=O)NCCCCCN

substrate: Acetylcadaverine


substrate_name: N-butylacetamide

smiles: CCCCN=C(C)O

substrate: N-butylacetamide


sequence_source: F1QCV2 canonical sequence with row-specific N93A substitution reconstructed after direct residue check on 2026-06-17.


sequence_variant_note: Resolved canonical sequence from F1QCV2 canonical sequence with row-specific D94A substitution reconstructed after direct residue check on 2026-06-17. and applied mutation signature D94A to reconstruct the assayed variant sequence.


sequence_source: F1QCV2 canonical sequence with row-specific E274L substitution reconstructed after direct residue check on 2026-06-17.


mutation_signature: recombinant deletion mutant DELTAnuA2

proof_lines: pH 8.0, 22°C, recombinant deletion mutant DELTAnuA2


substrate_name: acetylputrescine

smiles: CC(O)=NCCCCN

substrate: acetylputrescine


sequence_source: F1QCV2 canonical sequence with row-specific D94A substitution reconstructed after direct residue check on 2026-06-17.


enzyme_display_name: amidophosphoribosyltransferase

substrate_name: 5-Phospho-alpha-D-ribose 1-diphosphate; H2O; L-Glutamine

sequence_source: UniProtKB:Q9T0J5 direct lookup

enzyme: amidophosphoribosyltransferase


substrate_name: 5-Phospho-alpha-D-ribose 1-diphosphate; L-Glutamine; H2O

sequence_source: UniProtKB:Q9STG9 direct lookup

proof_lines: at pH 7.8, temperature not specified in the publication

proof_lines: cell extracts of recombinant AtGPRAT2 expressing Escherichia coli


organism: Escherichia coli

substrate_name: L-Glutamine; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AG16 canonical sequence with selected-batch mutation signature applied and applied mutation signature L415A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant L415A

substrate: L-Glutamine; H2O


sequence_source: UniProtKB:P0AG16 canonical sequence only

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant Y74L

substrate: 5-Phospho-alpha-D-ribose 1-diphosphate; H2O; L-Glutamine


substrate_name: L-Glutamine; H2O; 5-Phospho-alpha-D-ribose 1-diphosphate

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant R73L


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AG16 canonical sequence with selected-batch mutation signature applied and applied mutation signature R73H with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant R73H


substrate_name: H2O; 5-Phospho-alpha-D-ribose 1-diphosphate; L-Glutamine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AG16 canonical sequence with selected-batch mutation signature applied and applied mutation signature G102A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant G102A


substrate_name: H2O; L-Glutamine; 5-Phospho-alpha-D-ribose 1-diphosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AG16 canonical sequence with selected-batch mutation signature applied and applied mutation signature N101G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant N101G


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AG16 canonical sequence with selected-batch mutation signature applied and applied mutation signature Y74S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant Y74S

substrate: H2O; 5-Phospho-alpha-D-ribose 1-diphosphate; L-Glutamine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AG16 canonical sequence with selected-batch mutation signature applied and applied mutation signature N101D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant N101D

substrate: 5-Phospho-alpha-D-ribose 1-diphosphate; L-Glutamine; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AG16 canonical sequence with selected-batch mutation signature applied and applied mutation signature R73L/Y74L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant R73L/Y74L

substrate: H2O; L-Glutamine; 5-Phospho-alpha-D-ribose 1-diphosphate


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: amidophosphoribosyltransferase(Enzyme) mutant Y74F


substrate_name: L-Glutamine; 5-Phospho-alpha-D-ribose 1-diphosphate; H2O

sequence_source: UniProtKB:P0AG16 direct lookup


proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant D127A

substrate: L-Glutamine; 5-Phospho-alpha-D-ribose 1-diphosphate; H2O


proof_lines: SABIO-RK modifier species: amidophosphoribosyltransferase(Enzyme) mutant Ala insert


organism: Glycine max

sequence_source: UniProtKB:P52418 direct lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:F1QCV2 and applied mutation signature N93A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:F1QCV2 and applied mutation signature D94A 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.

proof_lines: pH 8.0, 22°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:F1QCV2 and applied mutation signature E274L to reconstruct the assayed variant sequence.


smiles: CC(O)=NCCCCCCCCN


enzyme_display_name: uridine phosphorylase

organism: Phytophthora capsici

substrate_name: uridine

sequence_source: UniProtKB:A0A6G6VYG7 direct REST sequence

proof_lines: pH and temperature not specified in the publication

enzyme: uridine phosphorylase

substrate: uridine


organism: Plasmodium falciparum

substrate_name: Inosine

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

substrate: Inosine


organism: Schistosoma mansoni

substrate_name: thymidine

substrate: thymidine


organism: Shewanella oneidensis

assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer, pH 7.5, 25°C


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


substrate_name: phosphate

sequence_source: UniProtKB:Q8E9X9 direct REST sequence

substrate: phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8E9X9 direct REST sequence with row-specific mutation reconstruction and applied mutation signature R176K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8E9X9 direct REST sequence with row-specific mutation reconstruction and applied mutation signature R176A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8E9X9 direct REST sequence with row-specific mutation reconstruction and applied mutation signature R89K to reconstruct the assayed variant sequence.


enzyme_display_name: acetylglutamate kinase

organism: Arabidopsis thaliana

substrate_name: ATP; N-Acetyl-L-glutamate

sequence_source: UniProtKB:Q9SCL7 direct REST sequence

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: in the presence of 1 mM L-arginine, in 50 mM imidazole, pH 7.5

proof_lines: in the absence of protein PII, in 50 mM imidazole, pH 7.5

proof_lines: in the presence of protein PII, in 50 mM imidazole, pH 7.5

enzyme: acetylglutamate kinase

substrate: ATP; N-Acetyl-L-glutamate


substrate_name: N-Acetyl-L-glutamate; ATP

assay_conditions_summary: cofactor ATP

substrate: N-Acetyl-L-glutamate; ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6C8 direct REST sequence with row-specific mutation reconstruction and applied mutation signature R66K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

proof_lines: SABIO-RK modifier species: acetylglutamate kinase(Enzyme) mutant R66K


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

sequence_source: UniProtKB:P0A6C8 direct REST sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6C8 direct REST sequence with row-specific mutation reconstruction and applied mutation signature K8R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetylglutamate kinase(Enzyme) mutant K8R


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6C8 direct REST sequence with row-specific mutation reconstruction and applied mutation signature N158Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetylglutamate kinase(Enzyme) mutant N158Q


organism: Unknown

substrate_name: N-acetyl-L-glutamate

substrate: N-acetyl-L-glutamate


enzyme_display_name: glucan 1,6-alpha-glucosidase

organism: Lactobacillus acidophilus

substrate_name: isomaltotetraose

sequence_source: UniProtKB Q5FMB7 direct REST lookup on 2026-06-17

enzyme: glucan 1,6-alpha-glucosidase

substrate: isomaltotetraose


substrate_name: Dextran

substrate: Dextran


substrate_name: isomaltotriose

substrate: isomaltotriose


substrate_name: isomaltose

substrate: isomaltose


proof_lines: purified recombinant enzyme, pH 6.0, 37°C


substrate_name: panose

substrate: panose


organism: Streptococcus mutans


substrate_name: isomaltohexaose

sequence_variant_note: Resolved canonical sequence from UniProtKB Q99040 direct REST lookup on 2026-06-17 with reconstructed W238A substitution and applied mutation signature W238A to reconstruct the assayed variant sequence.

substrate: isomaltohexaose


substrate_name: isomaltoheptaose

sequence_source: UniProtKB Q99040 direct REST lookup on 2026-06-17

substrate: isomaltoheptaose


substrate_name: Panose

substrate: Panose


sequence_variant_note: Resolved canonical sequence from UniProtKB Q99040 direct REST lookup on 2026-06-17 with reconstructed W238P substitution and applied mutation signature W238P to reconstruct the assayed variant sequence.


substrate_name: p-Nitrophenyl-alpha-D-glucoside

sequence_variant_note: Resolved canonical sequence from UniProtKB Q99040 direct REST lookup on 2026-06-17 with reconstructed W238N substitution and applied mutation signature W238N to reconstruct the assayed variant sequence.

substrate: p-Nitrophenyl-alpha-D-glucoside


sequence_source: UniProtKB Q99040 direct REST lookup on 2026-06-17 with reconstructed W238A substitution


sequence_source: UniProtKB Q99040 direct REST lookup on 2026-06-17 with reconstructed W238N substitution


substrate_name: Isomaltose; H2O

proof_lines: SABIO-RK modifier species: glucan 1,6-alpha-glucosidase(Enzyme) mutant W238N

unit: lgwedgeoneswedgeone

substrate: Isomaltose; H2O


substrate_name: acetylputrescine

sequence_source: UniProtKB reviewed accession Q969S8 fetched by direct REST lookup during review

substrate: acetylputrescine


substrate_name: Nalpha,Nepsilon-diacetyl-L-lysinamide

substrate: Nalpha,Nepsilon-diacetyl-L-lysinamide


smiles: CC(O)=NCCCNCCCCNCCCN


substrate_name: Acetylcadaverine

substrate: Acetylcadaverine


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


organism: Trypanosoma brucei

substrate_name: L-Ornithine

proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant His-tagged D332E

substrate: L-Ornithine


substrate_name: L-ornithine

substrate: L-ornithine


sequence_source: UniProtKB reviewed accession P07805 fetched by direct REST lookup during review

proof_lines:
wild type enzyme, at pH 7.5 and 37°C
wild-type, pH 8.0, 37°C


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant E94A N-terminal His6-tagged


enzyme_display_name: Amidophosphoribosyltransferase

organism: Homo sapiens

substrate_name: Unknown

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) Q06203 direct REST lookup on 2026-06-17

enzyme: Amidophosphoribosyltransferase

substrate: Unknown


organism: Rattus norvegicus

substrate_name: L-Glutamine; H2O; 5-Phospho-alpha-D-ribose 1-diphosphate

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) P35433 direct REST lookup on 2026-06-17


enzyme_display_name: Uridine phosphorylase

organism: Aeropyrum pernix

substrate_name: uridine

sequence_source: UniProtKB UniProtKB unreviewed (TrEMBL) Q9YA34 direct REST lookup on 2026-06-17

enzyme: Uridine phosphorylase

substrate: uridine


sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) P12758 direct REST lookup on 2026-06-17


enzyme_display_name: Uridine phosphorylase 1

substrate_name: Phosphate; Uridine

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) Q16831 direct REST lookup on 2026-06-17

proof_lines:
in 100 mMn Tris buffer pH 7.4, at 37°C
pH 7.4, 37°C, versus uridine
pH 7.4, 37°C, versus phosphate

enzyme: Uridine phosphorylase 1

substrate: Phosphate; Uridine


enzyme_display_name: Uridine phosphorylase 2

substrate_name: Uridine; Phosphate

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) O95045 direct REST lookup on 2026-06-17

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

enzyme: Uridine phosphorylase 2

substrate: Uridine; Phosphate


organism: Mus musculus

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) Q8CGR7 direct REST lookup on 2026-06-17


sequence_source: UniProtKB UniProtKB unreviewed (TrEMBL) A0A410UCT3 direct REST lookup on 2026-06-17


enzyme_display_name: Acetylglutamate kinase

substrate_name: N-acetyl-L-glutamate

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) P0A6C8 direct REST lookup on 2026-06-17

enzyme: Acetylglutamate kinase

substrate: N-acetyl-L-glutamate


substrate_name: ATP; N-Acetyl-L-glutamate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P0A6C8 canonical sequence fetched by direct REST lookup on 2026-06-17; row-specific variant reconstructed from selected mutation_signature D162E. and applied mutation signature D162E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetylglutamate kinase(Enzyme) mutant D162E

substrate: ATP; N-Acetyl-L-glutamate


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines:
pH 7.5, 37°C, mutant G11A, Vmax: 9.7
pH 7.5, 37°C, mutant G11A, Vmax: 11.1


substrate_name: ATP

proof_lines:
pH 7.5, 37°C, wild-type, Vmax: 72.6
pH 7.5, 37°C, wild-type, Vmax: 80

substrate: ATP