sequence_source: UniProtKB P04694 direct REST/FASTA lookup

assay_conditions_summary: pH 7.5; 310.15 K; buffer 1-mL reaction mixtures containing 150 mM triethanolamine

column_label: Table 2 pairs a leftmost column of metric names with a Substrate pair column and then one enzyme column per protein form. The cited cells are read from the Wild type enzyme column. In the Km (mM) block the substrate-pair row p-hydroxyphenylpyr reads 1.2; in the kcat (sec-1) block the same substrate-pair row reads 165; in the kcat/Km (sec-1 . M-1 . 10^3) block the same substrate-pair row reads 138, where the parenthesised number beside it is the relative percentage the table footnote defines and is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.2 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 1.2 mM. kcat: printed Table 2 cell 165 under the column head kcat (sec-1); sec-1 is s^-1, so no unit conversion applies and the paper value is 165 s^(-1). kcat/Km: printed Table 2 cell 138 under the column head kcat/Km (sec-1 . M-1 . 10^3), which is 138 x 10^3 M-1 s-1 = 138000.0 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 138000.0 / 1000 = 138.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Wild type enzyme column, substrate-pair row p-hydroxyphenylpyr: Km = 1.2 mM; kcat = 165 sec-1; printed kcat/Km = 138 x 10^3 M-1 s-1.

row_label: Table 2, Wild type column, substrate-pair row p-hydroxyphenylpyr

table_label: Table 2: Kinetic parameters for the overall reactions of the N-truncated recombinant rat TAT, Arg315Lys, and Asn54Ser variants (Protein Science 2003, 12:1039-1050)


enzyme_display_name: tyrosine transaminase

organism: Rattus norvegicus

substrate_name: 2-Oxoglutarate; L-Tyrosine

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

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

km_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB P04694 canonical sequence plus PMID 12717026 R315K mutation label and applied mutation signature R315K to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: SABIO-RK modifier species: tyrosine transaminase(Enzyme) mutant R315K

enzyme: tyrosine transaminase

substrate: 2-Oxoglutarate; L-Tyrosine


substrate_name: L-Glutamate

source_db: oed

verification_status: corrected

mutation_signature: Unknown

source_license: CC BY 4.0

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

column_label: Table 2 pairs a leftmost column of metric names with a Substrate pair column and then one enzyme column per protein form. The cited cells are read from the Wild type enzyme column. In the Km (mM) block the substrate-pair row L-Glutamate reads 2.2; in the kcat (sec-1) block the same substrate-pair row reads 210; in the kcat/Km (sec-1 . M-1 . 10^3) block the same substrate-pair row reads 96, where the parenthesised number beside it is the relative percentage the table footnote defines and is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table 2 cell 2.2 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 2.2 mM. kcat: printed Table 2 cell 210 under the column head kcat (sec-1); sec-1 is s^-1, so no unit conversion applies and the paper value is 210 s^(-1). kcat/Km: printed Table 2 cell 96 under the column head kcat/Km (sec-1 . M-1 . 10^3), which is 96 x 10^3 M-1 s-1 = 96000.0 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 96000.0 / 1000 = 96.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Wild type enzyme column, substrate-pair row L-Glutamate: Km = 2.2 mM; kcat = 210 sec-1; printed kcat/Km = 96 x 10^3 M-1 s-1.

row_label: Table 2, Wild type column, substrate-pair row L-Glutamate

data_origin: experimental

substrate: L-Glutamate

status: corrected

source: oed


substrate_name: L-Tyrosine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04694 and applied mutation signature R315K to reconstruct the assayed variant sequence.

column_label: Table 2 pairs a leftmost column of metric names with a Substrate pair column and then one enzyme column per protein form. The cited cells are read from the Arg315Lys enzyme column. In the Km (mM) block the substrate-pair row L-Tyrosine reads 2.3; in the kcat (sec-1) block the same substrate-pair row reads 510; in the kcat/Km (sec-1 . M-1 . 10^3) block the same substrate-pair row reads 222, where the parenthesised number beside it is the relative percentage the table footnote defines and is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table 2 cell 2.3 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 2.3 mM. kcat: printed Table 2 cell 510 under the column head kcat (sec-1); sec-1 is s^-1, so no unit conversion applies and the paper value is 510 s^(-1). kcat/Km: printed Table 2 cell 222 under the column head kcat/Km (sec-1 . M-1 . 10^3), which is 222 x 10^3 M-1 s-1 = 222000.0 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 222000.0 / 1000 = 222.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Arg315Lys enzyme column, substrate-pair row L-Tyrosine: Km = 2.3 mM; kcat = 510 sec-1; printed kcat/Km = 222 x 10^3 M-1 s-1.

row_label: Table 2, Arg315Lys column, substrate-pair row L-Tyrosine

substrate: L-Tyrosine


substrate_name: L-Tyrosine; 2-Oxoglutarate

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

substrate: L-Tyrosine; 2-Oxoglutarate


verification_status: verified

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

column_label: Table 2 pairs a leftmost column of metric names with a Substrate pair column and then one enzyme column per protein form. The cited cells are read from the Wild type enzyme column. In the Km (mM) block the substrate-pair row 2-oxoglutarate reads 0.40; in the kcat (sec-1) block the same substrate-pair row reads 566; in the kcat/Km (sec-1 . M-1 . 10^3) block the same substrate-pair row reads 1415, where the parenthesised number beside it is the relative percentage the table footnote defines and is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.40 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 0.40 mM. kcat: printed Table 2 cell 566 under the column head kcat (sec-1); sec-1 is s^-1, so no unit conversion applies and the paper value is 566 s^(-1). kcat/Km: printed Table 2 cell 1415 under the column head kcat/Km (sec-1 . M-1 . 10^3), which is 1415 x 10^3 M-1 s-1 = 1415000.0 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 1415000.0 / 1000 = 1415.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Wild type enzyme column, substrate-pair row 2-oxoglutarate: Km = 0.40 mM; kcat = 566 sec-1; printed kcat/Km = 1415 x 10^3 M-1 s-1.

row_label: Table 2, Wild type column, substrate-pair row 2-oxoglutarate

status: verified


sequence_variant_note: Resolved canonical sequence from UniProtKB P04694 canonical sequence plus PMID 12717026 N54S mutation label and applied mutation signature N54S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine transaminase(Enzyme) mutant N54S


column_label: Table 2 pairs a leftmost column of metric names with a Substrate pair column and then one enzyme column per protein form. The cited cells are read from the Arg315Lys enzyme column. In the Km (mM) block the substrate-pair row L-Glutamate reads 1.9; in the kcat (sec-1) block the same substrate-pair row reads 199; in the kcat/Km (sec-1 . M-1 . 10^3) block the same substrate-pair row reads 105, where the parenthesised number beside it is the relative percentage the table footnote defines and is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.9 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 1.9 mM. kcat: printed Table 2 cell 199 under the column head kcat (sec-1); sec-1 is s^-1, so no unit conversion applies and the paper value is 199 s^(-1). kcat/Km: printed Table 2 cell 105 under the column head kcat/Km (sec-1 . M-1 . 10^3), which is 105 x 10^3 M-1 s-1 = 105000.0 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 105000.0 / 1000 = 105.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Arg315Lys enzyme column, substrate-pair row L-Glutamate: Km = 1.9 mM; kcat = 199 sec-1; printed kcat/Km = 105 x 10^3 M-1 s-1.

row_label: Table 2, Arg315Lys column, substrate-pair row L-Glutamate


organism: Trypanosoma cruzi

substrate_name: L-alanine

source_db: brenda

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P33447 direct REST/FASTA lookup; N17S reconstructed from the canonical sequence and applied mutation signature N17S to reconstruct the assayed variant sequence.

substrate: L-alanine

source: brenda


sequence_source: UniProtKB reviewed P33447 direct REST/FASTA lookup


kcat_display: Not reported


organism: Variovorax paradoxus

substrate_name: (S)-beta-phenylalanine

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

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

proof_lines: enzyme shows substrate inhibition, pH 7.6, 30°C

source_databases_merged: brenda skid

substrate: (S)-beta-phenylalanine


organism: Arabidopsis thaliana

substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


proof_lines: isoform TAT1, with L-glutamate as cosubstrate, at pH 8.5 and 30 C

proof_lines: isoform TAT1, with L-tyrosine as cosubstrate, at pH 8.5 and 30 C

proof_lines: isoform TAT1, with 2-oxoglutarate as cosubstrate, at pH 8.5 and 30 C


substrate_name: L-tyrosine

substrate: L-tyrosine


organism: Klebsiella pneumoniae

substrate_name: 4-Methylthio-2-oxobutanoate; L-Tyrosine

substrate: 4-Methylthio-2-oxobutanoate; L-Tyrosine


organism: Leishmania donovani

proof_lines: N-terminal domain, with pyruvate as cosubstrate, at pH 8.0 and 37 C

proof_lines: C-terminal domain, with pyruvate as cosubstrate, at pH 8.0 and 37 C


organism: Petunia x hybrida

verification_status: unverified

kcat_over_km_origin: calculated

status: unverified


substrate_name: L-phenylalanine

proof_lines: cosubstrate 4-hydroxyphenylpyruvate, pH 10.0, 30 C

proof_lines: cosubstrate phenylalanine, pH 10.0, 30 C

substrate: L-phenylalanine


substrate_name: L-glutamate

substrate: L-glutamate


enzyme_display_name: Phenylpyruvate aminotransferase

enzyme_name_source: UniProtKB direct accession lookup

sequence_source: UniProtKB V5M241 REST/FASTA direct lookup on 2026-06-05

enzyme: Phenylpyruvate aminotransferase


substrate_name: phenylpyruvate

substrate: phenylpyruvate


enzyme_display_name: Tyrosine aminotransferase

sequence_variant_note: Resolved canonical sequence from UniProtKB P04694 REST/FASTA direct lookup on 2026-06-05 and applied mutation signature N54S to reconstruct the assayed variant sequence.

enzyme: Tyrosine aminotransferase


sequence_source: UniProtKB P04694 REST/FASTA direct lookup on 2026-06-05


sequence_variant_note: Resolved canonical sequence from UniProtKB P04694 REST/FASTA direct lookup on 2026-06-05 and applied mutation signature R315K to reconstruct the assayed variant sequence.


source_db: uniprot

source: uniprot


substrate_name: tryptophan (at pH 7.4 and 10 mM KMTB)

substrate: tryptophan (at pH 7.4 and 10 mM KMTB)


organism: Mus musculus

substrate_name: tyrosine

substrate: tyrosine


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


organism: Tapinella panuoides


enzyme_display_name: pantothenate kinase

organism: Homo sapiens

substrate_name: (R)-pantothenate

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: recombinant isozyme mPanK2, pH 7.5, 37°C

proof_lines: recombinant isozyme iPanK2, pH 7.5, 37°C

enzyme: pantothenate kinase

substrate: (R)-pantothenate


organism: Thermotoga maritima

substrate_name: (R)-Pantothenate

sequence_source: UniProtKB reviewed Swiss-Prot accession Q9WZY5

substrate: (R)-Pantothenate


substrate_name: (R)-Pantothenate; ATP

assay_conditions_summary: cofactor ATP

substrate: (R)-Pantothenate; ATP


organism: Staphylococcus aureus

sequence_source: UniProtKB reviewed accession Q2FWC7, fetched 2026-06-05

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


substrate_name: ATP; (R)-Pantothenate

substrate: ATP; (R)-Pantothenate


substrate_name: ATP

substrate: ATP


substrate_name: N-Pentylpantothenamide

substrate: N-Pentylpantothenamide


substrate_name: N-Heptylpantothenamide

substrate: N-Heptylpantothenamide


organism: Thermococcus kodakaraensis

assay_conditions_summary: pH 8; 315.15 K; cofactor ATP


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Swiss-Prot accession P0A6I3 with row-specific F247V reconstruction and applied mutation signature F247V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pantothenate kinase(Enzyme) mutant F247V


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

sequence_source: UniProtKB reviewed Swiss-Prot accession P0A6I3

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines: at pH 7.6, temperature not specified in the publication

proof_lines: pH 7.5, 37°C, recombinant His-tagged enzyme

source_databases_merged: sabio_rk brenda skid


assay_conditions_summary: pH 6; 293.00 K; cofactor ATP


organism: Helicobacter pylori

sequence_source: UniProtKB reviewed Swiss-Prot accession O25533

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP


km_display: Not reported

sequence_source: UniProtKB reviewed Swiss-Prot accession Q9BZ23


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:Q9H999 / PANK3_HUMAN direct accession lookup on 2026-06-05; reviewed Homo sapiens pantothenate kinase 3 annotated with EC 2.7.1.33.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9H999 canonical sequence with row-specific R207W substitution computed on 2026-06-05 from selected mutation_signature R207W. and applied mutation signature R207W to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pantothenate kinase(Enzyme) mutant R207W His-tagged


proof_lines:
isoform PanK3, at pH 7.5 and 37°C
Raw SKiD Env: Temp=37°C, pH=7.5


sequence_source: UniProtKB:Q8R2W9 / PANK3_MOUSE direct accession lookup on 2026-06-05; reviewed Mus musculus pantothenate kinase 3 annotated with EC 2.7.1.33.


sequence_source: UniProtKB:Q8K4K6-2 isoform sequence lookup on 2026-06-05; Q8K4K6 is reviewed Mus musculus pantothenate kinase 1, and isoform 2 is named PanK1-beta.


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB:P9WPA7 / COAA_MYCTU direct accession lookup on 2026-06-05; reviewed Mycobacterium tuberculosis strain H37Rv pantothenate kinase annotated with EC 2.7.1.33.

proof_lines: 25°C, pH 7.8, determined from coupled assay

proof_lines: 25°C, pH 7.8, determined by isothermal titration calorimetry


organism: Picrophilus oshimae

substrate_name: pantothenate

sequence_source: UniProtKB:Q6L2I5 / Q6L2I5_PICTO direct accession lookup on 2026-06-05; unreviewed Picrophilus torridus strain entry under Picrophilus oshimae taxonomy, annotated as pantothenate kinase EC 2.7.1.33.

substrate: pantothenate


organism: Rattus norvegicus

substrate_name: L-Tyrosine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04694 and applied mutation signature N54S to reconstruct the assayed variant sequence.

column_label: Table 2 pairs a leftmost column of metric names with a Substrate pair column and then one enzyme column per protein form. The cited cells are read from the Asn54Ser enzyme column. In the Km (mM) block the substrate-pair row L-Tyrosine reads 5.3; in the kcat (sec-1) block the same substrate-pair row reads 132; in the kcat/Km (sec-1 . M-1 . 10^3) block the same substrate-pair row reads 25, where the parenthesised number beside it is the relative percentage the table footnote defines and is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table 2 cell 5.3 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 5.3 mM. kcat: printed Table 2 cell 132 under the column head kcat (sec-1); sec-1 is s^-1, so no unit conversion applies and the paper value is 132 s^(-1). kcat/Km: printed Table 2 cell 25 under the column head kcat/Km (sec-1 . M-1 . 10^3), which is 25 x 10^3 M-1 s-1 = 25000.0 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 25000.0 / 1000 = 25.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Asn54Ser enzyme column, substrate-pair row L-Tyrosine: Km = 5.3 mM; kcat = 132 sec-1; printed kcat/Km = 25 x 10^3 M-1 s-1.

row_label: Table 2, Asn54Ser column, substrate-pair row L-Tyrosine

substrate: L-Tyrosine


sequence_source: UniProtKB REST direct accession check: P04694


column_label: Table 2 pairs a leftmost column of metric names with a Substrate pair column and then one enzyme column per protein form. The cited cells are read from the Asn54Ser enzyme column. In the Km (mM) block the substrate-pair row p-hydroxyphenylpyr reads 1.3; in the kcat (sec-1) block the same substrate-pair row reads 5.9; in the kcat/Km (sec-1 . M-1 . 10^3) block the same substrate-pair row reads 4.5, where the parenthesised number beside it is the relative percentage the table footnote defines and is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.3 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 1.3 mM. kcat: printed Table 2 cell 5.9 under the column head kcat (sec-1); sec-1 is s^-1, so no unit conversion applies and the paper value is 5.9 s^(-1). kcat/Km: printed Table 2 cell 4.5 under the column head kcat/Km (sec-1 . M-1 . 10^3), which is 4.5 x 10^3 M-1 s-1 = 4500.0 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 4500.0 / 1000 = 4.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Asn54Ser enzyme column, substrate-pair row p-hydroxyphenylpyr: Km = 1.3 mM; kcat = 5.9 sec-1; printed kcat/Km = 4.5 x 10^3 M-1 s-1.

row_label: Table 2, Asn54Ser column, substrate-pair row p-hydroxyphenylpyr


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


organism: Thermococcus litoralis

substrate_name: 2-Oxoglutarate; L-Tyrosine

substrate: 2-Oxoglutarate; L-Tyrosine


organism: Trypanosoma cruzi

substrate_name: pyruvate

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check: P33447; variant reconstructed from selected mutation_signature R20A and applied mutation signature R20A to reconstruct the assayed variant sequence.

substrate: pyruvate


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines: recombinant isozyme PanK1beta, pH 7.0, 37°C


organism: Arabidopsis thaliana

sequence_source: UniProtKB:Q8L5Y9 canonical sequence from direct accession lookup


organism: Aspergillus nidulans

sequence_source: UniProtKB:O93921 canonical sequence from direct accession lookup


organism: Bacillus subtilis

sequence_source: UniProtKB:P37564 canonical sequence from direct accession lookup


organism: Entamoeba histolytica

sequence_source: UniProtKB:B1N2P3 canonical sequence from direct accession lookup

assay_conditions_summary: pH 6; 310.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I3 canonical sequence with row-specific H177Q substitution reconstructed during review and applied mutation signature H177Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pantothenate kinase(Enzyme) mutant H177Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A6I3 canonical sequence with row-specific R106A substitution reconstructed during review and applied mutation signature R106A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pantothenate kinase(Enzyme) mutant R106A


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)


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

substrate_name: pantothenate (at 50 degrees Celsius)

substrate: pantothenate (at 50 degrees Celsius)


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

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


organism: Caenorhabditis elegans

substrate_name: tyrosine (para-tyrosine)

proof_lines: kcat is 2852 sec(-1) with tyrosine (para-tyrosine) as substrate (PubMed:31043480). kcat is 2520 sec(-1) with meta-tyrosine as substrate (PubMed:31043480).

substrate: tyrosine (para-tyrosine)


substrate_name: p-nitrophenylphosphate

proof_lines: kcat is 1.99 sec(-1) with p-nitrophenylphosphate as substrate. kcat is 0.26 sec(-1) with phosphopantetheine as substrate. kcat is 0.94 sec(-1) with 4'-phosphopantotheine-S-sulfonate as substrate. kcat is 0.52 sec(-1) with 4'-phosphopantothe

substrate: p-nitrophenylphosphate


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

substrate_name: pantothenate (in the absence of ammonium)

proof_lines: kcat is 12.5 min(-1) for the phosphorylation of pantothenate in the absence of ammonium. kcat is 25 min(-1) for the phosphorylation of pantothenate in the presence of ammonium.


enzyme_display_name: phosphate acetyltransferase

organism: Rhodopseudomonas palustris

substrate_name: CoA

assay_conditions_summary: cofactor CoA

enzyme: phosphate acetyltransferase

substrate: CoA


organism: Salmonella enterica

substrate_name: acetyl phosphate

assay_conditions_summary: 303.15 K; cofactor CoA

substrate: acetyl phosphate


substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

proof_lines: 37°C, pH 7.5, wild-type enzyme, per trimer of His-tagged enzyme

substrate: acetyl-CoA


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

proof_lines: 37°C, pH 7.5, mutant enzyme M294I, per trimer of His-tagged enzyme


proof_lines: 37°C, pH 7.5, mutant enzyme R252H, per trimer of His-tagged enzyme


proof_lines: 37°C, pH 7.5, mutant enzyme G273D, per trimer of His-tagged enzyme


organism: Fructilactobacillus sanfranciscensis


organism: Lactococcus lactis subsp. cremoris

substrate_name: Acetyl phosphate; Coenzyme A

substrate: Acetyl phosphate; Coenzyme A


organism: Lactococcus lactis subsp. lactis

substrate_name: Coenzyme A; Acetyl phosphate

substrate: Coenzyme A; Acetyl phosphate


organism: Limosilactobacillus fermentum


organism: Methanosarcina thermophila


substrate_name: desulfo-CoA

substrate: desulfo-CoA


enzyme_display_name: Type III pantothenate kinase

organism: Bacillus subtilis (strain 168)

enzyme: Type III pantothenate kinase


organism: Helicobacter pylori (strain ATCC 700392 / 26695)


enzyme_display_name: Pantothenate kinase 2, mitochondrial

organism: Homo sapiens

enzyme: Pantothenate kinase 2, mitochondrial


enzyme_display_name: Pantothenate kinase 3

substrate_name: ATP

enzyme: Pantothenate kinase 3

substrate: ATP


organism: Mus musculus

substrate_name: pantothenate


enzyme_display_name: Pantothenate kinase 1

enzyme: Pantothenate kinase 1


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 and GenBank L23147/AAA72041.1; variant sequence reconstructed from selected BRENDA mutation note and applied mutation signature C277A/C312A/C325A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 and GenBank L23147/AAA72041.1; variant sequence reconstructed from selected BRENDA mutation note and applied mutation signature R133Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 and GenBank L23147/AAA72041.1; variant sequence reconstructed from selected BRENDA mutation note and applied mutation signature C159S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 and GenBank L23147/AAA72041.1; variant sequence reconstructed from selected BRENDA mutation note and applied mutation signature C312A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P38503 and GenBank L23147/AAA72041.1

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

proof_lines:
wild-type after expression in E. coli
wild-type
wild type


sequence_variant_note: Resolved canonical sequence from UniProtKB P38503 and GenBank L23147/AAA72041.1; variant sequence reconstructed from selected BRENDA mutation note and applied mutation signature R310Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 reviewed entry; direct UniProt REST lookup on 2026-06-05 and applied mutation signature C325A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 reviewed entry; direct UniProt REST lookup on 2026-06-05 and applied mutation signature C159A/C277A/C312A/C325A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 reviewed entry; direct UniProt REST lookup on 2026-06-05 and applied mutation signature C159A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 reviewed entry; direct UniProt REST lookup on 2026-06-05 and applied mutation signature R287Q to reconstruct the assayed variant sequence.

proof_lines:
mutant R287Q
R287Q mutant


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 reviewed entry; direct UniProt REST lookup on 2026-06-05 and applied mutation signature R28Q to reconstruct the assayed variant sequence.

proof_lines:
mutant R28Q
R28Q mutant


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38503 reviewed entry; direct UniProt REST lookup on 2026-06-05 and applied mutation signature C277A to reconstruct the assayed variant sequence.


enzyme_display_name: Xaa-Pro aminopeptidase

substrate_name: Arg-Pro-Pro

sequence_source: UniProtKB reviewed FASTA Q9NQW7

enzyme: Xaa-Pro aminopeptidase

substrate: Arg-Pro-Pro


substrate_name: H2O; Met-Pro-Ala

sequence_source: UniProtKB reviewed FASTA Q9NQH7

substrate: H2O; Met-Pro-Ala


substrate_name: Bradykinin

substrate: Bradykinin


substrate_name: H2O; Bradykinin

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA Q9NQW7 and applied mutation signature R535A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: Xaa-Pro aminopeptidase(Enzyme) mutant R535A His-tagged

proof_lines: pH 7.5, 37°C, recombinant mutant R535A, with 0.1 mM guanidine hydrochloride

substrate: H2O; Bradykinin


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA Q9NQW7 and applied mutation signature Y527F to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: Xaa-Pro aminopeptidase(Enzyme) mutant Y527F His-tagged


organism: Streptomyces murinus

sequence_source: UniProtKB:A9E3K0 direct REST lookup on 2026-06-05

proof_lines:
native enzyme, pH 7.4, 30°C
recombinant enzyme, pH 7.4, 30°C


organism: Synechocystis sp. PCC 6803

sequence_source: UniProtKB:P74468 direct REST lookup on 2026-06-05


organism: Thermococcus onnurineus NA1

substrate_name: L-Met-L-Pro

sequence_source: UniProtKB:Q2QC92 direct REST lookup on 2026-06-05

substrate: L-Met-L-Pro


organism: Xanthomonas campestris

sequence_source: UniProtKB:Q8P5S7 direct REST lookup on 2026-06-05


organism: Deinococcus radiodurans

substrate_name: Arg-Pro-Ala

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUY4 and applied mutation signature R55A to reconstruct the assayed variant sequence.

column_label: Table 4: Michaelis Menten kinetics of wild-type Dr-smAPP and its mutants (Proteins 2019, 87(3):212-225), substrate block 'Arg-Pro-Ala', enzyme row 'R55A'; column 'Km (mM)' = 3.5; column 'kcat (s-1)' = 101; column 'kcat/Km (mM-1 s-1)' = 29.

normalized_value_unit_evidence: Km: printed Table 4 cell 3.5 mM; the printed unit is already mM, so the value carries over as 3.5 mM. The exported value is 3.5 mM. kcat: printed Table 4 cell 101 s^-1; the printed unit is already s^-1, so the value carries over as 101 s^(-1). The exported value is 101 s^(-1). kcat/Km: printed Table 4 cell 29 mM^-1 s^-1; the printed unit is the canonical ratio unit, so the printed cell is 29 s^-1 mM^-1, the printed-precision rendering of the exact same-row quotient 101 / 3.5 = 28.857142857142858 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 4, substrate block 'Arg-Pro-Ala', enzyme row 'R55A': Km = 3.5 mM; kcat = 101 s^-1; printed kcat/Km = 29 mM^-1 s^-1.

substrate: Arg-Pro-Ala


substrate_name: Met-Pro-Ala

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUY4 canonical sequence fetched directly; D53A variant reconstructed from residue D53 to A. and applied mutation signature D53A to reconstruct the assayed variant sequence.

substrate: Met-Pro-Ala


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUY4 canonical sequence fetched directly; R55A variant reconstructed from residue R55 to A. and applied mutation signature R55A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9RUY4 canonical sequence fetched directly; Y56A variant reconstructed from residue Y56 to A. and applied mutation signature Y56A to reconstruct the assayed variant sequence.


substrate_name: Met-Pro

sequence_source: UniProtKB:Q9RUY4 canonical sequence fetched directly and used unchanged for wild type.

column_label: Table 2: Michaelis Menten kinetics (Proteins 2019, 87(3):212-225), substrate block 'Met-Pro', enzyme row 'Dr-smAPP'; column 'Km (mM)' = 11.9; column 'kcat (s-1)' = 97; column 'kcat/Km (mM-1 s-1)' = 8.15.

normalized_value_unit_evidence: Km: printed Table 2 cell 11.9 mM; the printed unit is already mM, so the value carries over as 11.9 mM. The exported value is 11.9 mM. kcat: printed Table 2 cell 97 s^-1; the printed unit is already s^-1, so the value carries over as 97 s^(-1). The exported value is 97 s^(-1). kcat/Km: printed Table 2 cell 8.15 mM^-1 s^-1; the printed unit is the canonical ratio unit, so the printed cell is 8.15 s^-1 mM^-1, the printed-precision rendering of the exact same-row quotient 97 / 11.9 = 8.15126050420168 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 2, substrate block 'Met-Pro', enzyme row 'Dr-smAPP': Km = 11.9 mM; kcat = 97 s^-1; printed kcat/Km = 8.15 mM^-1 s^-1.

substrate: Met-Pro


column_label: Table 2: Michaelis Menten kinetics (Proteins 2019, 87(3):212-225), substrate block 'Met-Pro-Ala', enzyme row 'Dr-smAPP'; column 'Km (mM)' = 1.9; column 'kcat (s-1)' = 242; column 'kcat/Km (mM-1 s-1)' = 127.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.9 mM; the printed unit is already mM, so the value carries over as 1.9 mM. The exported value is 1.9 mM. kcat: printed Table 2 cell 242 s^-1; the printed unit is already s^-1, so the value carries over as 242 s^(-1). The exported value is 242 s^(-1). kcat/Km: printed Table 2 cell 127 mM^-1 s^-1; the printed unit is the canonical ratio unit, so the printed cell is 127 s^-1 mM^-1, the printed-precision rendering of the exact same-row quotient 242 / 1.9 = 127.36842105263159 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 2, substrate block 'Met-Pro-Ala', enzyme row 'Dr-smAPP': Km = 1.9 mM; kcat = 242 s^-1; printed kcat/Km = 127 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUY4 and applied mutation signature D53A to reconstruct the assayed variant sequence.

column_label: Table 4: Michaelis Menten kinetics of wild-type Dr-smAPP and its mutants (Proteins 2019, 87(3):212-225), substrate block 'Arg-Pro-Ala', enzyme row 'D53A'; column 'Km (mM)' = 6.0; column 'kcat (s-1)' = 29; column 'kcat/Km (mM-1 s-1)' = 4.8.

normalized_value_unit_evidence: Km: printed Table 4 cell 6.0 mM; the printed unit is already mM, so the value carries over as 6.0 mM. The exported value is 6.0 mM. kcat: printed Table 4 cell 29 s^-1; the printed unit is already s^-1, so the value carries over as 29 s^(-1). The exported value is 29 s^(-1). kcat/Km: printed Table 4 cell 4.8 mM^-1 s^-1; the printed unit is the canonical ratio unit, so the printed cell is 4.8 s^-1 mM^-1, the printed-precision rendering of the exact same-row quotient 29 / 6.0 = 4.833333333333333 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 4, substrate block 'Arg-Pro-Ala', enzyme row 'D53A': Km = 6.0 mM; kcat = 29 s^-1; printed kcat/Km = 4.8 mM^-1 s^-1.


organism: Escherichia coli

substrate_name: L-Ala-L-Pro-L-Ala

sequence_source: UniProtKB:P15034 canonical sequence fetched directly and used unchanged for wild type.

substrate: L-Ala-L-Pro-L-Ala


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB REST/FASTA I6YDN6, accessed 2026-06-05

column_label: Table 2: Michaelis Menten kinetics (Proteins 2019, 87(3):212-225), substrate block 'Met-Pro-Ala', enzyme row 'Mt-smAPP'; column 'Km (mM)' = 9.0; column 'kcat (s-1)' = 126; column 'kcat/Km (mM-1 s-1)' = 14.

normalized_value_unit_evidence: Km: printed Table 2 cell 9.0 mM; the printed unit is already mM, so the value carries over as 9.0 mM. The exported value is 9.0 mM. kcat: printed Table 2 cell 126 s^-1; the printed unit is already s^-1, so the value carries over as 126 s^(-1). The exported value is 126 s^(-1). kcat/Km: printed Table 2 cell 14 mM^-1 s^-1; the printed unit is the canonical ratio unit, so the printed cell is 14 s^-1 mM^-1, which is the exported value 14.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate block 'Met-Pro-Ala', enzyme row 'Mt-smAPP': Km = 9.0 mM; kcat = 126 s^-1; printed kcat/Km = 14 mM^-1 s^-1.


substrate_name: Met-Ala-Ala

column_label: Table 2: Michaelis Menten kinetics (Proteins 2019, 87(3):212-225), substrate block 'Met-Ala-Ala', enzyme row 'Mt-smAPP'; column 'Km (mM)' = 0.46; column 'kcat (s-1)' = 5.0; column 'kcat/Km (mM-1 s-1)' = 11.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.46 mM; the printed unit is already mM, so the value carries over as 0.46 mM. The exported value is 0.46 mM. kcat: printed Table 2 cell 5.0 s^-1; the printed unit is already s^-1, so the value carries over as 5.0 s^(-1). The exported value is 5.0 s^(-1). kcat/Km: printed Table 2 cell 11 mM^-1 s^-1; the printed unit is the canonical ratio unit, so the printed cell is 11 s^-1 mM^-1, the printed-precision rendering of the exact same-row quotient 5.0 / 0.46 = 10.869565217391305 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 2, substrate block 'Met-Ala-Ala', enzyme row 'Mt-smAPP': Km = 0.46 mM; kcat = 5.0 s^-1; printed kcat/Km = 11 mM^-1 s^-1.

substrate: Met-Ala-Ala


column_label: Table 2: Michaelis Menten kinetics (Proteins 2019, 87(3):212-225), substrate block 'Met-Pro', enzyme row 'Mt-smAPP'; column 'Km (mM)' = 6.3; column 'kcat (s-1)' = 18; column 'kcat/Km (mM-1 s-1)' = 2.85.

normalized_value_unit_evidence: Km: printed Table 2 cell 6.3 mM; the printed unit is already mM, so the value carries over as 6.3 mM. The exported value is 6.3 mM. kcat: printed Table 2 cell 18 s^-1; the printed unit is already s^-1, so the value carries over as 18 s^(-1). The exported value is 18 s^(-1). kcat/Km: printed Table 2 cell 2.85 mM^-1 s^-1; the printed unit is the canonical ratio unit, so the paper value is 2.85 s^-1 mM^-1, while the catalog carries the full-precision quotient 2.857142857142857 s^(-1)*mM^(-1) of the two printed component cells; the printed efficiency cell lies outside the last-place rounding interval of that quotient, so it is adopted as the paper value for this metric.

raw_value_unit_evidence: Table 2, substrate block 'Met-Pro', enzyme row 'Mt-smAPP': Km = 6.3 mM; kcat = 18 s^-1; printed kcat/Km = 2.85 mM^-1 s^-1.


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB REST/FASTA P40051, accessed 2026-06-05


substrate_name: Tyr-Ala-Ala

column_label: Table 2: Enzyme kinetics (FEBS Letters 593 (2019) 443-454); printed column heads Substrate | Vmax (umol min^-1 mg^-1) | Km (mM) | Ki (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) (x 10^3). Table 2, substrate row YAA; column Vmax (umol min^-1 mg^-1) = 1.5; column Km (mM) = 0.72; column Ki (mM) = 5 mM; column kcat (s^-1) = 1.4; column kcat/Km (M^-1 s^-1) (x 10^3) = 1.94. captured primary segment: YAA | Vmax 1.5 umol min^-1 mg^-1 | Km 0.72 mM | Ki 5 mM | kcat 1.4 s^-1 | kcat/Km 1.94 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 0.72 mM; the printed unit is already mM, so no unit conversion applies and the paper value is 0.72 mM. kcat: printed Table 2 kcat cell 1.4 s^-1; the printed unit is already s^-1, so no unit conversion applies and the paper value is 1.4 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 1.94 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1940.0 x 0.001 = 1.94 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.4 / 0.72 = 1.9444444444444444 s^-1 mM^-1, against the printed catalytic-efficiency cell 1.94 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate row YAA: Km = 0.72 mM; kcat = 1.4 s^-1; printed kcat/Km = 1.94 x 10^3 M^-1 s^-1.

row_label: Table 2, substrate row YAA

substrate: Tyr-Ala-Ala


normalized_value_unit_evidence: Km: printed Table 2 Km cell 0.72 mM; the printed unit is already mM, so no unit conversion applies and the exported value is 0.72 mM. kcat: printed Table 2 kcat cell 1.4 s^-1; the printed unit is already s^-1, so no unit conversion applies and the exported value is 1.4 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 1.94 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1940.0 x 0.001 = 1.94 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.4 / 0.72 = 1.9444444444444444 s^-1 mM^-1, against the printed catalytic-efficiency cell 1.94 s^-1 mM^-1.

table_label: Table 2: Enzyme kinetics (FEBS Letters 593 (2019) 443-454); printed column heads Substrate | Vmax (umol min^-1 mg^-1) | Km (mM) | Ki (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) (x 10^3)


substrate_name: Tyr-Pro-Ala

column_label: Table 2: Enzyme kinetics (FEBS Letters 593 (2019) 443-454); printed column heads Substrate | Vmax (umol min^-1 mg^-1) | Km (mM) | Ki (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) (x 10^3). Table 2, substrate row YPA; column Vmax (umol min^-1 mg^-1) = 14.0; column Km (mM) = 1.8; column Ki (mM) = NA; column kcat (s^-1) = 14.0; column kcat/Km (M^-1 s^-1) (x 10^3) = 7.78. captured primary segment: YPA | Vmax 14.0 umol min^-1 mg^-1 | Km 1.8 mM | Ki NA | kcat 14.0 s^-1 | kcat/Km 7.78 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 1.8 mM; the printed unit is already mM, so no unit conversion applies and the exported value is 1.8 mM. kcat: printed Table 2 kcat cell 14.0 s^-1; the printed unit is already s^-1, so no unit conversion applies and the exported value is 14.0 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 7.78 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7780.0 x 0.001 = 7.78 s^(-1)*mM^(-1). Quotient disclosure for this row: 14.0 / 1.8 = 7.777777777777778 s^-1 mM^-1, against the printed catalytic-efficiency cell 7.78 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate row YPA: Km = 1.8 mM; kcat = 14.0 s^-1; printed kcat/Km = 7.78 x 10^3 M^-1 s^-1.

row_label: Table 2, substrate row YPA

substrate: Tyr-Pro-Ala


organism: Arabidopsis thaliana

substrate_name: Unknown

substrate: Unknown


organism: Caenorhabditis elegans

substrate_name: bradykinin

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

substrate: bradykinin


organism: Rattus norvegicus

substrate_name: Arg-Pro-Pro (at pH 8.0)

assay_conditions_summary: pH 8

substrate: Arg-Pro-Pro (at pH 8.0)


organism: Ashbya gossypii

sequence_source: UniProt Q75CD7 FASTA direct check 2026-06-05


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUY4 and applied mutation signature Y56A to reconstruct the assayed variant sequence.

column_label: Table 4: Michaelis Menten kinetics of wild-type Dr-smAPP and its mutants (Proteins 2019, 87(3):212-225), substrate block 'Arg-Pro-Ala', enzyme row 'Y56A'; column 'Km (mM)' = 8.4; column 'kcat (s-1)' = 152; column 'kcat/Km (mM-1 s-1)' = 18.

normalized_value_unit_evidence: Km: printed Table 4 cell 8.4 mM; the printed unit is already mM, so the value carries over as 8.4 mM. The exported value is 8.4 mM. kcat: printed Table 4 cell 152 s^-1; the printed unit is already s^-1, so the value carries over as 152 s^(-1). The exported value is 152 s^(-1). kcat/Km: printed Table 4 cell 18 mM^-1 s^-1; the printed unit is the canonical ratio unit, so the printed cell is 18 s^-1 mM^-1, the printed-precision rendering of the exact same-row quotient 152 / 8.4 = 18.095238095238095 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 4, substrate block 'Arg-Pro-Ala', enzyme row 'Y56A': Km = 8.4 mM; kcat = 152 s^-1; printed kcat/Km = 18 mM^-1 s^-1.


sequence_source: UniProt Q9RUY4 FASTA direct check 2026-06-05

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

column_label: Table 4: Michaelis Menten kinetics of wild-type Dr-smAPP and its mutants (Proteins 2019, 87(3):212-225), substrate block 'Arg-Pro-Ala', enzyme row 'Wild-type'; column 'Km (mM)' = 2.1; column 'kcat (s-1)' = 240; column 'kcat/Km (mM-1 s-1)' = 114.

normalized_value_unit_evidence: Km: printed Table 4 cell 2.1 mM; the printed unit is already mM, so the value carries over as 2.1 mM. The exported value is 2.1 mM. kcat: printed Table 4 cell 240 s^-1; the printed unit is already s^-1, so the value carries over as 240 s^(-1). The exported value is 240 s^(-1). kcat/Km: printed Table 4 cell 114 mM^-1 s^-1; the printed unit is the canonical ratio unit, so the printed cell is 114 s^-1 mM^-1, the printed-precision rendering of the exact same-row quotient 240 / 2.1 = 114.28571428571428 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 4, substrate block 'Arg-Pro-Ala', enzyme row 'Wild-type': Km = 2.1 mM; kcat = 240 s^-1; printed kcat/Km = 114 mM^-1 s^-1.


column_label: Table 4: Michaelis Menten kinetics of wild-type Dr-smAPP and its mutants (Proteins 2019, 87(3):212-225), substrate block 'Met-Pro-Ala', enzyme row 'Y56A'; column 'Km (mM)' = 3.9; column 'kcat (s-1)' = 140; column 'kcat/Km (mM-1 s-1)' = 36.

normalized_value_unit_evidence: Km: printed Table 4 cell 3.9 mM; the printed unit is already mM, so the value carries over as 3.9 mM. The exported value is 3.9 mM. kcat: printed Table 4 cell 140 s^-1; the printed unit is already s^-1, so the value carries over as 140 s^(-1). The exported value is 140 s^(-1). kcat/Km: printed Table 4 cell 36 mM^-1 s^-1; the printed unit is the canonical ratio unit, so the printed cell is 36 s^-1 mM^-1, the printed-precision rendering of the exact same-row quotient 140 / 3.9 = 35.8974358974359 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 4, substrate block 'Met-Pro-Ala', enzyme row 'Y56A': Km = 3.9 mM; kcat = 140 s^-1; printed kcat/Km = 36 mM^-1 s^-1.


column_label: Table 4: Michaelis Menten kinetics of wild-type Dr-smAPP and its mutants (Proteins 2019, 87(3):212-225), substrate block 'Met-Pro-Ala', enzyme row 'R55A'; column 'Km (mM)' = 6.1; column 'kcat (s-1)' = 144; column 'kcat/Km (mM-1 s-1)' = 24.

normalized_value_unit_evidence: Km: printed Table 4 cell 6.1 mM; the printed unit is already mM, so the value carries over as 6.1 mM. The exported value is 6.1 mM. kcat: printed Table 4 cell 144 s^-1; the printed unit is already s^-1, so the value carries over as 144 s^(-1). The exported value is 144 s^(-1). kcat/Km: printed Table 4 cell 24 mM^-1 s^-1; the printed unit is the canonical ratio unit, so the printed cell is 24 s^-1 mM^-1, the printed-precision rendering of the exact same-row quotient 144 / 6.1 = 23.60655737704918 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 4, substrate block 'Met-Pro-Ala', enzyme row 'R55A': Km = 6.1 mM; kcat = 144 s^-1; printed kcat/Km = 24 mM^-1 s^-1.


column_label: Table 2: Michaelis Menten kinetics (Proteins 2019, 87(3):212-225), substrate block 'Met-Ala-Ala', enzyme row 'Dr-smAPP'; column 'Km (mM)' = 0.15; column 'kcat (s-1)' = 10.5; column 'kcat/Km (mM-1 s-1)' = 70.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.15 mM; the printed unit is already mM, so the value carries over as 0.15 mM. The exported value is 0.15 mM. kcat: printed Table 2 cell 10.5 s^-1; the printed unit is already s^-1, so the value carries over as 10.5 s^(-1). The exported value is 10.5 s^(-1). kcat/Km: printed Table 2 cell 70 mM^-1 s^-1; the printed unit is the canonical ratio unit, so the printed cell is 70 s^-1 mM^-1, which is the exported value 70.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate block 'Met-Ala-Ala', enzyme row 'Dr-smAPP': Km = 0.15 mM; kcat = 10.5 s^-1; printed kcat/Km = 70 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProt Q9RUY4 FASTA plus D53A reconstruction direct check 2026-06-05 and applied mutation signature D53A to reconstruct the assayed variant sequence.


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: human hemoglobin peptide HbPep1 (FPHFD) (at pH 7.5 and 37 degrees Celsius)

proof_lines: kcat is 8.6 sec(-1) with for human hemoglobin peptide HbPep1 (FPHFD) as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:19574214). kcat is 5.4 sec(-1) with for human hemoglobin peptide HbPep1 (FPHFD) as substrate (at pH 5.5 and 37 degr


organism: Thermotoga maritima

substrate_name: CoA

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

substrate: CoA


organism: Veillonella parvula


substrate_name: L-tyrosine

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

proof_lines: aspartate aminotransferase with mutations HEX and I73V, pH 8.0, 25°C

substrate: L-tyrosine


proof_lines: aspartate aminotransferase with mutations HEX and A293D, pH 8.0, 25°C


proof_lines: aspartate aminotransferase with mutations HEX and I73V, A293D, pH 8.0, 25°C


proof_lines: aspartate aminotransferase with mutations HEX, pH 8.0, 25°C


organism: Corynebacterium ammoniagenes

substrate_name: pantothenate

assay_conditions_summary: pH 6.5; 310.15 K; cofactor ATP

proof_lines:
pH 6.5, 37°C
oxidized form, pH 6.5, 37°C
reduced form, pH 6.5, 37°C

substrate: pantothenate


substrate_name: (R)-Pantothenate; ATP

assay_conditions_summary: pH 8; 298.15 K; buffer form of MgATP2- Tris-HCl; cofactor ATP

proof_lines:
Tris-HCl buffer, pH 8.0
citrate buffer, pH 6.0
pH 7.4, 25°C

substrate: (R)-Pantothenate; ATP


organism: Helicobacter pylori

substrate_name: ATP

substrate: ATP


organism: Mus musculus

proof_lines: SABIO-RK modifier species: pantothenate kinase(Enzyme) mutant PANK1beta-3-1beta

proof_lines: SABIO-RK modifier species: pantothenate kinase(Enzyme) mutant PANK3-1beta-3


substrate_name: GTP

assay_conditions_summary: pH 6.5; buffer citrate; cofactor ATP

proof_lines: in citrate buffer, pH 6.5, temperature not specified in the publication

substrate: GTP


organism: Plasmodium falciparum

ki_unit: mM


organism: Papaver somniferum


organism: Prunella vulgaris

substrate_name: phenylpyruvate

proof_lines: with L-tyrosine as cosubstrate, at pH 8.0 and 30°C

proof_lines: with L-glutamate as cosubstrate, at pH 8.0 and 30°C

proof_lines: with 2-oxoglutarate as cosubstrate, at pH 8.0 and 30°C

substrate: phenylpyruvate


organism: Trichoderma viride


organism: Trypanosoma cruzi

substrate_name: pyruvate

proof_lines:
pH 7.0, 37°C, tyrosine as co-substrate
pH 7.0, 37°C, pyruvate as co-substrate

substrate: pyruvate


organism: Bacillus anthracis

substrate_name: dCTP

substrate: dCTP


organism: Bacillus subtilis


organism: Escherichia coli

substrate_name: L-Phenylalanine; 2-Oxoglutarate

substrate: L-Phenylalanine; 2-Oxoglutarate


organism: Felis catus


organism: Homo sapiens

substrate_name: L-glutamate

substrate: L-glutamate


organism: Oncorhynchus mykiss

proof_lines:
in liver
in white muscle


enzyme_display_name: dihydropteroate synthase

organism: Arabidopsis thaliana

sequence_source: UniProtKB Q1ENB6 REST direct check 2026-06-05

enzyme: dihydropteroate synthase


substrate_name: sulfanilamide

sequence_source: UniProtKB Q81VW8 REST direct check 2026-06-05

proof_lines:
in absence of 4-aminobenzoate
100 microM DHP-PP, 25 °C
20 microM DHP-PP, 25 °C

substrate: sulfanilamide


sequence_source: UniProtKB P0AC13 REST direct check 2026-06-05


organism: Escherichia coli MC4100


organism: Mycobacterium leprae

sequence_source: UniProtKB P0C0X1 REST direct check 2026-06-05


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB P9WND1 REST direct check 2026-06-05


organism: Rattus norvegicus

substrate_name: ATP; (R)-Pantothenate

proof_lines:
pH 7.0, 37°C
ATP in form of MgATP2-
pH 6.1, 37°C

substrate: ATP; (R)-Pantothenate


organism: Spinacia oleracea

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines:
isoform 1, 37°C, pH 8.0
isoform 2, 37°C, pH 8.0


organism: Staphylococcus aureus

sequence_source: UniProtKB reviewed Q2FWC7; direct lit_pubmed:15548531 EC+organism lookup.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines:
pH 7.5, 37°C, recombinant enzyme
pH 7.5, 25°C


organism: Thermotoga maritima

substrate_name: (R)-pantothenate

sequence_source: UniProtKB reviewed Q9WZY5; direct lit_pubmed:16855243 structural PanK-III lookup.

assay_conditions_summary: pH 7.6; 323.15 K; cofactor ATP

proof_lines: in 100 mM HEPES, pH 7.6, 20 mM KCl, 10 mM MgCl2, 2 mM phosphoenolpyruvate, 0.3 mM NADH, 5 units of lactate dehydrogenase, 2.5 units of pyruvate kinase, and 0.00027 mM of the PanK-III protein, at 50°C

substrate: (R)-pantothenate


enzyme_display_name: UMP kinase

organism: Haemophilus influenzae

sequence_source: UniProtKB reviewed P43890; direct lit_pubmed:17210578 EC+organism lookup.

assay_conditions_summary: cofactor ATP

proof_lines: in presence of 1.0 mM UMP and 0.5 mM GTP

proof_lines: in presence of 1.0 mM ATP and 0.5 mM GTP

enzyme: UMP kinase


organism: Saccharolobus solfataricus

sequence_source: UniProtKB reviewed Q97ZE2; direct lit_pubmed:17297917 structural uridylate kinase lookup.

assay_conditions_summary: 333.15 K; cofactor ATP

proof_lines:
in presence of 0.1 mM UMP, at 60°C
in presence of 0.5 mM ATP at 60°C
in presence of 0.5 mM ATP


organism: Plasmodium falciparum

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 canonical sequence reconstructed with RCSB/PDB 6JWS mutation A437G and applied mutation signature A437G to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 canonical sequence reconstructed with RCSB/PDB 6KCL mutations A437G,K540E and applied mutation signature A437G/K540E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A437G/K540E, at pH 9.0 and 37°C


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB:Q25704 canonical sequence

source: skid


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:P53848 canonical sequence

proof_lines: recombinant bifunctional fusion protein encoding dihydropterin pyrophosphokinase and dihyropteroate synthase domains of the trifunctional enzyme dihydroneopterin aldolase-dihydropterin pyrophosphokinase-dihydropteroate synthase


substrate_name: p-Aminobenzoic acid

sequence_variant_note: Resolved canonical sequence from UniProtKB:P53848 canonical sequence reconstructed with source mutation note T557A and applied mutation signature T557A to reconstruct the assayed variant sequence.

substrate: p-Aminobenzoic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB:P53848 canonical sequence reconstructed with source mutation note T557A/P559S and applied mutation signature T557A/P559S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P53848 canonical sequence reconstructed with source mutation note P559S and applied mutation signature P559S to reconstruct the assayed variant sequence.


organism: Pisum sativum


organism: Pneumocystis carinii


sequence_variant_note: Resolved canonical sequence from direct_uniprot_q25704_variant_reconstruction and applied mutation signature S436A/A437G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct_uniprot_q25704_variant_reconstruction and applied mutation signature A613T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct_uniprot_q25704_variant_reconstruction and applied mutation signature S436F/A437G/A613T to reconstruct the assayed variant sequence.


proof_lines: mutant enzyme S436F/A437G/A613T, at pH 9.0 and 37°C


sequence_variant_note: Resolved canonical sequence from direct_uniprot_q25704_variant_reconstruction and applied mutation signature S436F/A437G/A613S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S436F/A437G/A613S, at pH 9.0 and 37°C


sequence_variant_note: Resolved canonical sequence from direct_uniprot_q25704_variant_reconstruction and applied mutation signature K540E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct_uniprot_q25704_variant_reconstruction and applied mutation signature A437G/K540E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P9WND1 direct FASTA/JSON lookup on 2026-06-05


sequence_source: UniProtKB:O04862 direct FASTA/JSON lookup on 2026-06-05


sequence_source: UniProtKB:Q25704 direct FASTA/JSON lookup on 2026-06-05


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 direct FASTA/JSON lookup plus local A613S reconstruction on 2026-06-05 and applied mutation signature A613S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 direct FASTA/JSON lookup plus local A437G reconstruction on 2026-06-05 and applied mutation signature A437G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q25704 direct FASTA/JSON lookup plus local S436F/A613S reconstruction on 2026-06-05 and applied mutation signature S436F/A613S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S436F/A613S, at pH 9.0 and 37°C


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P53848 canonical sequence with source-stated T557V/P559S substitutions applied after residue check and applied mutation signature T557V/P559S to reconstruct the assayed variant sequence.


proof_lines:
wild type
wild tpye


sequence_source: UniProtKB:O05701 canonical sequence


organism: Streptococcus pneumoniae

sequence_source: UniProtKB:P05382 canonical sequence

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


sequence_source: UniProtKB:P05382 canonical sequence checked as context only; row-specific variant sequence not resolved

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: dihydropteroate synthase(Enzyme) mutant


organism: Streptococcus pyogenes

sequence_source: UniProtKB:P0C0G1 canonical sequence


sequence_source: UniProtKB:P0C0G0 canonical sequence


organism: Escherichia coli

sequence_source: UniProtKB:P15034 canonical sequence checked as context only; H350A coordinate did not match canonical residue 350


substrate_name: Met-Pro-Ala

substrate: Met-Pro-Ala


substrate_name: Met-Pro

column_label: Table 2: Michaelis Menten kinetics (Proteins 2019, 87(3):212-225), substrate block 'Met-Pro', enzyme row 'Ec-smAPP'; column 'Km (mM)' = 7.9; column 'kcat (s-1)' = 33; column 'kcat/Km (mM-1 s-1)' = 4.17.

normalized_value_unit_evidence: Km: printed Table 2 cell 7.9 mM; the printed unit is already mM, so the value carries over as 7.9 mM. The exported value is 7.9 mM. kcat: printed Table 2 cell 33 s^-1; the printed unit is already s^-1, so the value carries over as 33 s^(-1). The exported value is 33 s^(-1). kcat/Km: printed Table 2 cell 4.17 mM^-1 s^-1; the printed unit is the canonical ratio unit, so the paper value is 4.17 s^-1 mM^-1, while the catalog carries the full-precision quotient 4.177215189873418 s^(-1)*mM^(-1) of the two printed component cells; the printed efficiency cell lies outside the last-place rounding interval of that quotient, so it is adopted as the paper value for this metric.

raw_value_unit_evidence: Table 2, substrate block 'Met-Pro', enzyme row 'Ec-smAPP': Km = 7.9 mM; kcat = 33 s^-1; printed kcat/Km = 4.17 mM^-1 s^-1.

substrate: Met-Pro


substrate_name: Met-Ala-Ala

column_label: Table 2: Michaelis Menten kinetics (Proteins 2019, 87(3):212-225), substrate block 'Met-Ala-Ala', enzyme row 'Ec-smAPP'; column 'Km (mM)' = 0.23; column 'kcat (s-1)' = 1.5; column 'kcat/Km (mM-1 s-1)' = 6.5.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.23 mM; the printed unit is already mM, so the value carries over as 0.23 mM. The exported value is 0.23 mM. kcat: printed Table 2 cell 1.5 s^-1; the printed unit is already s^-1, so the value carries over as 1.5 s^(-1). The exported value is 1.5 s^(-1). kcat/Km: printed Table 2 cell 6.5 mM^-1 s^-1; the printed unit is the canonical ratio unit, so the printed cell is 6.5 s^-1 mM^-1, the printed-precision rendering of the exact same-row quotient 1.5 / 0.23 = 6.521739130434782 s^(-1)*mM^(-1) that the catalog carries for this measurement.

raw_value_unit_evidence: Table 2, substrate block 'Met-Ala-Ala', enzyme row 'Ec-smAPP': Km = 0.23 mM; kcat = 1.5 s^-1; printed kcat/Km = 6.5 mM^-1 s^-1.

substrate: Met-Ala-Ala


organism: Gibberella zeae

substrate_name: Met-Pro-Ala; H2O

substrate: Met-Pro-Ala; H2O


organism: Homo sapiens

substrate_name: bradykinin

proof_lines: pH 8.2, 37°C, recombinant wild-type enzyme

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

substrate: bradykinin


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprotkb_Q25704_direct_lookup_2026-06-05 and applied mutation signature S436F/A613T to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S436F/A613T, at pH 9.0 and 37°C


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprotkb_Q25704_direct_lookup_2026-06-05 and applied mutation signature A581G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprotkb_Q25704_direct_lookup_2026-06-05 and applied mutation signature A613S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprotkb_Q25704_direct_lookup_2026-06-05 and applied mutation signature S436F/A613S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprotkb_Q25704_direct_lookup_2026-06-05 and applied mutation signature S436A/A437G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S436A/A437G, at pH 9.0 and 37°C


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprotkb_Q25704_direct_lookup_2026-06-05 and applied mutation signature K540E to reconstruct the assayed variant sequence.


substrate_name: 4-aminobenzoate (at pH 7.5 and 37 degrees Celsius)

proof_lines: kcat is 0.46 sec(-1) for 4-aminobenzoate as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:37419898). kcat is 0.28 sec(-1) for sulfamethoxazole as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:37419898).


proof_lines: kcat is 0.38 sec(-1) for 4-aminobenzoate as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:37419898). kcat is 0.26 sec(-1) for sulfamethoxazole as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:37419898).

substrate: 4-aminobenzoate (at pH 7.5 and 37 degrees Celsius)


proof_lines: kcat is 0.42 sec(-1) for 4-aminobenzoate as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:37419898). kcat is 0.25 sec(-1) for sulfamethoxazole as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:37419898).


organism: Escherichia coli (strain K12)

proof_lines: kcat is 0.38 sec(-1) for 4-aminobenzoate as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:37419898). kcat is 0.46 sec(-1) for sulfamethoxazole as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:37419898).


organism: Mycobacterium leprae (strain TN)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 35 min(-1) (PubMed:10542185). kcat is 28 min(-1) with pABA as substrate, and 45 min(-1) with PAS as substrate (PubMed:23118010).


substrate_name: ATP

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

proof_lines: in presence of 1.0 mM UMP and 0.5 mM GTP

substrate: ATP


enzyme_display_name: holo-[acyl-carrier-protein] synthase

substrate_name: apo-[Streptomyces sp. granaticin-acyl-carrier protein]

proof_lines:
pH 7.0, 37°C, E. coli ACP
pH 8.8, 37°C
pH 8.8, 37°C, 250 mM NaCl

enzyme: holo-[acyl-carrier-protein] synthase


substrate_name: apo-ACP

proof_lines: pH 7.0, 37°C, Bacillus subtilis acyl carrier protein-A as substrate

proof_lines: pH 7.0, 37°C, human acyl carrier protein f as as substrate

proof_lines: pH 7.0, 37°C, human acyl carrier protein mit as substrate

substrate: apo-ACP


organism: Mycoplasmoides pneumoniae

substrate_name: crotonyl-CoA

assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA

substrate: crotonyl-CoA


organism: Pseudomonas aeruginosa

substrate_name: CoA

assay_conditions_summary: pH 7.8; 303.15 K; cofactor CoA

proof_lines: in the presence of 0.0025 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30°C

proof_lines: in the presence of 0.01 mM CoA, in 100 mM Tris-HCl, pH 7.8, at 30°C

substrate: CoA


organism: Pseudomonas putida

substrate_name: apo-[BpsA protein]

substrate: apo-[BpsA protein]


organism: Campylobacter jejuni

proof_lines:
sulfonamide resistant enzyme
resistant enzyme


substrate_name: sulfathiazole

substrate: sulfathiazole


organism: Lactiplantibacillus plantarum

substrate_name: Unknown

substrate: Unknown


organism: Lathyrus oleraceus

proof_lines: inhibitor of 6-hydroxymethyl-7,8-dihydropteridine diphosphate


organism: Plasmodium berghei


organism: Plasmodium chabaudi


organism: Plasmodium vivax

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


proof_lines: mutant enzyme S382A/A383G/A553G, pH 9.0, 37°C


organism: Streptococcus pneumoniae


organism: Staphylococcus aureus

substrate_name: UMP

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP

proof_lines:
pH 7.5, 22°C, ordered BiBi mechanism
in presence of 1.0 mM UMP without GTP
pH 7.5, 22°C, random BiBi mechanism

substrate: UMP


organism: Spinacia oleracea

substrate_name: apo-acyl-carrier protein

substrate: apo-acyl-carrier protein


substrate_name: myristoyl-CoA

substrate: myristoyl-CoA


organism: Streptomyces pneumoniae

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

proof_lines: pH 7.0, 37°C, trichloroacetic acid precipitation method


enzyme_display_name: licheninase

organism: Bacillus sp. (in: firmicutes)

substrate_name: Laminarin

enzyme: licheninase

substrate: Laminarin


organism: Plasmodium falciparum


mutation_type: deletion


substrate_name: lichenan

substrate: lichenan


enzyme_display_name: fatty acid amide hydrolase

organism: Unknown

enzyme: fatty acid amide hydrolase


organism: Rattus norvegicus

substrate_name: oleamide ((9Z)-octadecenamide)

proof_lines: kcat is 7.1 sec(-1) with oleamide ((9Z)-octadecenamide) (PubMed:9790682). kcat is 28 min(-1) with 2-arachidonoylglycerol (2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol) (PubMed:17649977). kcat is 16 min(-1) with anandamide (N-(5Z,8Z,11Z,14Z-e

substrate: oleamide ((9Z)-octadecenamide)


organism: Arabidopsis thaliana

substrate_name: N-acylethanolamine 20:4

substrate: N-acylethanolamine 20:4


organism: Caenorhabditis elegans


organism: Homo sapiens


organism: Sus scrofa


organism: Bacillus tequilensis

substrate_name: azo blue barley beta-glucan

proof_lines: mutant N31C/T187C/P102C/N125C, at pH 6.5 and 40°C

substrate: azo blue barley beta-glucan


substrate_name: Barley beta-glucan

substrate: Barley beta-glucan


organism: Bispora sp. MEY-1

substrate_name: lichenin

substrate: lichenin


substrate_name: Barley glucan

substrate: Barley glucan


organism: Fibrobacter succinogenes


organism: Bacillus sp. SJ-10


organism: Bacillus subtilis


proof_lines:
wild-type, pH 6.5, 40°C
wild type enzyme, at pH 6.5 and 40°C


sequence_source: UniProtKB P17989 canonical sequence; M39F reconstructed from PMID 11279139 mutation label using paper-position +23 to UniProt precursor-position offset.

sequence_variant_note: Mutation signature M39F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB P17989 canonical sequence; D58N reconstructed from PMID 11279139 mutation label using paper-position +23 to UniProt precursor-position offset.

sequence_variant_note: Mutation signature D58N matches the mutant residue at offset +9 and the reference residue at offset +15; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB P17989 canonical sequence; G63A reconstructed from PMID 11279139 mutation label using paper-position +23 to UniProt precursor-position offset.

sequence_variant_note: Mutation signature G63A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB P17989 canonical sequence; E56D reconstructed from PMID 11279139 mutation label using paper-position +23 to UniProt precursor-position offset.

sequence_variant_note: Mutation signature E56D could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB P17989 canonical sequence for Fibrobacter succinogenes beta-glucanase, EC 3.2.1.73.

proof_lines:
wild type
pH 6.0, 40°C, wild type


proof_lines:
expressed in Pichia pastoris
expressed in Escherichia coli


substrate_name: Palmitoylethanolamide

sequence_source: UniProtKB REST Q7XJJ7 and identity reuse cache accession:Q7XJJ7

smiles: CCCCCCCCCCCCCCCC(O)=NCCO

substrate: Palmitoylethanolamide


substrate_name: Dodecanoyl ethanolamide

smiles: CCCCCCCCCCCC(=O)NCCO

substrate: Dodecanoyl ethanolamide


substrate_name: Linoleoylethanolamide

smiles: CCCCCC=CCC=CCCCCCCCC(=O)NCCO

substrate: Linoleoylethanolamide


substrate_name: Anandamide

substrate: Anandamide


substrate_name: H2O; Anandamide

proof_lines:
at 9.0 pH and 30°C
at pH 9.0 and 30°C

substrate: H2O; Anandamide


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from UniProtKB REST O00519, identity reuse cache accession:O00519, and selected BRENDA P129T note and applied mutation signature P129T to reconstruct the assayed variant sequence.

substrate: Unknown


sequence_source: UniProtKB REST O00519 and identity reuse cache accession:O00519

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


substrate_name: Anandamide; H2O

sequence_source: UniProtKB REST P97612 and identity reuse cache accession:P97612

proof_lines:
at 9.0 pH and 30°C
at pH 9.0 and 30°C
pH 9.0, 22°C

substrate: Anandamide; H2O


organism: Secale cereale

substrate_name: H2O; DIBOA glucoside

sequence_source: UniProtKB Q9FYS3 FASTA/JSON direct check, 2026-06-05

proof_lines: pH and temperature not specified in the publication

substrate: H2O; DIBOA glucoside


substrate_name: DIBOA glucoside

sequence_variant_note: Mutation signature Y378F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: DIBOA glucoside


substrate_name: DIMBOA glucoside

sequence_variant_note: Mutation signature G464F 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.

substrate: DIMBOA glucoside


sequence_variant_note: Mutation signature F198A matches the mutant residue at offset +2 and the reference residue at offset +10; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


substrate_name: DIBOA glucoside; H2O

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +9, so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant F471Y His-tagged

substrate: DIBOA glucoside; H2O


proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant G464F His-tagged


sequence_variant_note: Mutation signature S465L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Triticum aestivum

sequence_source: Canonical context only from UniProtKB reviewed accession Q1XIR9 (HGL1A_WHEAT) direct REST check, 2026-06-05

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: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant F198 His-tagged


sequence_source: Reconstructed from UniProtKB reviewed accession Q1XIR9 (HGL1A_WHEAT) plus PMID 16751439 mutation label Y378F


substrate_name: DIBOA-glucoside

sequence_source: Reconstructed from UniProtKB reviewed accession Q1XH05 (HGL1B_WHEAT) plus PMID 16751439 mutation label S464F

sequence_variant_note: Mutation signature S464F matches the mutant residue at offset -11 and the reference residue at offset +3; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: DIBOA-glucoside


sequence_source: UniProtKB reviewed accession Q1XH05 (HGL1B_WHEAT) direct REST check, 2026-06-05


substrate_name: DIMBOA-glucoside

sequence_source: Reconstructed from UniProtKB reviewed accession Q1XH05 (HGL1B_WHEAT) plus PMID 16751439 mutation label Y378A

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -6, so it is treated as a source-provided variant sequence.

substrate: DIMBOA-glucoside


sequence_source: Reconstructed from UniProtKB reviewed accession Q1XIR9 (HGL1A_WHEAT) plus PMID 16751439 mutation label F471Y


substrate_name: 4-nitrophenyl beta-D-glucoside

sequence_source: Reconstructed from UniProtKB reviewed accession Q1XH05 (HGL1B_WHEAT) plus PMID 16751439 mutation label F198A

substrate: 4-nitrophenyl beta-D-glucoside


column_label: Table II: Kinetic parameters of the TaGlu1s and TaGlu1a mutants (Plant Physiology 2006, 141(4):1237-1247), row 'TaGlu1b', DIMBOA-Glc block; column 'Km (mM)' = 0.29; column 'kcat (s^-1)' = 1,201; column 'kcat/Km (s^-1/mM)' = 4,138.

normalized_value_unit_evidence: kcat: printed Table II cell 1,201 under the column head s^-1; that printed unit is already canonical, so no unit conversion applies and kcat = 1201.0 s^(-1). Km: printed cell 0.29 under the column head mM; that printed unit is already canonical, so no unit conversion applies and Km = 0.29 mM. kcat/Km: printed cell 4,138 under the column head s^-1/mM, the canonical per second per millimolar unit, so no unit conversion applies and kcat/Km = 4138.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, row TaGlu1b, DIMBOA-Glc block: Km cell 0.29 mM; kcat cell 1,201 s^-1; printed kcat/Km cell 4,138 s^-1/mM.

row_label: Table II, row TaGlu1b, DIMBOA-Glc block


sequence_source: UniProtKB Q1XIR9 canonical sequence fetched 2026-06-05 by direct accession lookup.

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


sequence_source: UniProtKB Q1XH04 canonical sequence fetched 2026-06-05 by direct accession lookup.

column_label: Table II: Kinetic parameters of the TaGlu1s and TaGlu1a mutants (Plant Physiology 2006, 141(4):1237-1247), row 'TaGlu1c', DIMBOA-Glc block; column 'Km (mM)' = 0.39; column 'kcat (s^-1)' = 773; column 'kcat/Km (s^-1/mM)' = 1979.

normalized_value_unit_evidence: kcat: printed Table II cell 773 under the column head s^-1; that printed unit is already canonical, so no unit conversion applies and kcat = 773.0 s^(-1). Km: printed cell 0.39 under the column head mM; that printed unit is already canonical, so no unit conversion applies and Km = 0.39 mM. kcat/Km: printed cell 1979 under the column head s^-1/mM, the canonical per second per millimolar unit, so no unit conversion applies and kcat/Km = 1979.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, row TaGlu1c, DIMBOA-Glc block: Km cell 0.39 mM; kcat cell 773 s^-1; printed kcat/Km cell 1979 s^-1/mM.

row_label: Table II, row TaGlu1c, DIMBOA-Glc block


sequence_source: UniProtKB Q1XH05 canonical sequence fetched 2026-06-05; row-specific Y378F variant reconstructed with checked UniProt residue 427.


sequence_source: UniProtKB Q1XIR9 canonical sequence fetched 2026-06-05; row-specific Y378F variant reconstructed with checked UniProt residue 427.


sequence_source: UniProtKB Q1XH05 canonical sequence fetched 2026-06-05; row-specific S464F variant reconstructed with checked UniProt residue 513.


sequence_source: UniProtKB Q1XH05 canonical sequence fetched 2026-06-05 by direct accession lookup.


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

sequence_source: UniProtKB reviewed entry Q1XH05 (HGL1B_WHEAT) direct REST FASTA/JSON check


sequence_source: UniProtKB reviewed entry Q1XH04 (HGL1C_WHEAT) direct REST FASTA/JSON check

column_label: Table II: Kinetic parameters of the TaGlu1s and TaGlu1a mutants (Plant Physiology 2006, 141(4):1237-1247), row 'TaGlu1c', DIBOA-Glc block; column 'Km (mM)' = 1.05; column 'kcat (s^-1)' = 137; column 'kcat/Km (s^-1/mM)' = 131.

normalized_value_unit_evidence: kcat: printed Table II cell 137 under the column head s^-1; that printed unit is already canonical, so no unit conversion applies and kcat = 137.0 s^(-1). Km: printed cell 1.05 under the column head mM; that printed unit is already canonical, so no unit conversion applies and Km = 1.05 mM. kcat/Km: printed cell 131 under the column head s^-1/mM, the canonical per second per millimolar unit, so no unit conversion applies and kcat/Km = 131.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, row TaGlu1c, DIBOA-Glc block: Km cell 1.05 mM; kcat cell 137 s^-1; printed kcat/Km cell 131 s^-1/mM.

row_label: Table II, row TaGlu1c, DIBOA-Glc block


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed entry Q1XIR9 (HGL1A_WHEAT) direct REST FASTA/JSON check and applied mutation signature S464F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant S464F His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1XH05 canonical sequence; variant reconstructed from selected mutation_signature Y378A and applied mutation signature Y378A with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q1XIR9 canonical sequence; variant reconstructed from selected mutation_signature S464F

sequence_variant_note: Mutation signature S464F 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_source: UniProtKB:Q1XIR9 canonical sequence

column_label: Table II: Kinetic parameters of the TaGlu1s and TaGlu1a mutants (Plant Physiology 2006, 141(4):1237-1247), row 'TaGlu1a', DIBOA-Glc block; column 'Km (mM)' = 1.40; column 'kcat (s^-1)' = 48.8; column 'kcat/Km (s^-1/mM)' = 34.6.

normalized_value_unit_evidence: kcat: printed Table II cell 48.8 under the column head s^-1; that printed unit is already canonical, so no unit conversion applies and kcat = 48.8 s^(-1). Km: printed cell 1.40 under the column head mM; that printed unit is already canonical, so no unit conversion applies and Km = 1.4 mM. kcat/Km: printed cell 34.6 under the column head s^-1/mM, the canonical per second per millimolar unit, so no unit conversion applies and kcat/Km = 34.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, row TaGlu1a, DIBOA-Glc block: Km cell 1.40 mM; kcat cell 48.8 s^-1; printed kcat/Km cell 34.6 s^-1/mM.

row_label: Table II, row TaGlu1a, DIBOA-Glc block


sequence_source: UniProtKB:Q1XH05 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1XH05 canonical sequence; variant reconstructed from selected mutation_signature F471Y and applied mutation signature F471Y with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1XIR9 canonical sequence; variant reconstructed from selected mutation_signature Y378F and applied mutation signature Y378F with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant Y378F His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1XIR9 canonical sequence; variant reconstructed from selected mutation_signature Y378A and applied mutation signature Y378A with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant Y378A His-tagged


sequence_source: UniProtKB:Q1XIR9 canonical sequence; variant reconstructed from selected mutation_signature Y378A


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3 direct lookup; ScGlu mature-protein mutation numbering mapped to Q9FYS3 with +49 offset using PDBe/RCSB 3AIU alignment and applied mutation signature G464S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3 direct lookup; ScGlu mature-protein mutation numbering mapped to Q9FYS3 with +49 offset using PDBe/RCSB 3AIU alignment and applied mutation signature F198A with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant F198A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3 direct lookup; ScGlu mature-protein mutation numbering mapped to Q9FYS3 with +49 offset using PDBe/RCSB 3AIU alignment and applied mutation signature G464S/S465L with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3 direct lookup; ScGlu mature-protein mutation numbering mapped to Q9FYS3 with +49 offset using PDBe/RCSB 3AIU alignment and applied mutation signature Y378F with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q9FYS3 direct lookup; ScGlu mature-protein mutation numbering mapped to Q9FYS3 with +49 offset using PDBe/RCSB 3AIU alignment


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3 direct lookup; ScGlu mature-protein mutation numbering mapped to Q9FYS3 with +49 offset using PDBe/RCSB 3AIU alignment and applied mutation signature S465L with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant S465L His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3 direct lookup; ScGlu mature-protein mutation numbering mapped to Q9FYS3 with +49 offset using PDBe/RCSB 3AIU alignment and applied mutation signature Y378A with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3; reconstructed F471Y variant as canonical residue F520Y with +49 offset and applied mutation signature F471Y with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3; reconstructed Y378F variant as canonical residue Y427F with +49 offset and applied mutation signature Y378F with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FYS3; reconstructed G464S variant as canonical residue G513S with +49 offset and applied mutation signature G464S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant G464S His-tagged


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


substrate_name: DIMBOA glucoside; H2O

substrate: DIMBOA glucoside; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1XH05; reconstructed F198A variant as canonical residue F247A with +49 offset and applied mutation signature F198A with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1XH05; reconstructed F471Y variant as canonical residue F520Y with +49 offset and applied mutation signature F471Y with inferred residue-numbering offset +49 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q1XIR9; reconstructed S464F variant as canonical residue S513F with +49 offset


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 Q1XH05

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


organism: Zea mays

substrate_name: H2O; DIMBOA glucoside

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant Chim 2

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant Chim 15

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant Chim 16

substrate: H2O; DIMBOA glucoside


sequence_source: UniProtKB reviewed accession P49235


sequence_source: UniProtKB:P49235 direct REST lookup; reviewed Swiss-Prot HGGL1_MAIZE


substrate_name: p-nitrophenyl beta-D-glucopyranoside (PNPG) (with recombinant enzyme)


enzyme_display_name: methylthioadenosine nucleosidase

organism: Brucella melitensis

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8YBL1 FASTA direct lookup; M144A reconstructed after residue M144 matched the canonical sequence. and applied mutation signature M144A to reconstruct the assayed variant sequence.

enzyme: methylthioadenosine nucleosidase


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8YBL1 FASTA direct lookup; S167A reconstructed after residue S167 matched the canonical sequence. and applied mutation signature S167A to reconstruct the assayed variant sequence.


substrate_name: S-adenosyl-L-homocysteine

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8YBL1 FASTA direct lookup; R164A reconstructed after residue R164 matched the canonical sequence. and applied mutation signature R164A to reconstruct the assayed variant sequence.

substrate: S-adenosyl-L-homocysteine


sequence_source: UniProtKB Q8YBL1 FASTA direct lookup.

column_label: Table 2 (Kinetic parameters for purine binding subsite mutants), Enzyme column 'WT', Substrate column 'SAH'; column 'Km (uM)' = 4.0; column 'Kcat (s^-1)' = 7.1; column 'kcat/Km (s^-1 M^-1)' = 1.8 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 4.0 uM; 4.0 / 1000 = 0.004 mM; the catalog value is 0.004 mM. kcat: printed Table 2 cell 7.1 s^-1; already in s^-1, so no unit conversion applies; the catalog value is 7.1 s^(-1). kcat/Km: printed Table 2 cell 1.8 x 10^6 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.8 x 10^6 x 0.001 = 1800.0 s^-1 mM^-1. The quotient of the two printed component cells is 7.1 / 0.004 = 1774.9999999999998 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, row WT, substrate SAH: Km = 4.0 uM; Kcat = 7.1 s^-1; printed kcat/Km = 1.8 x 10^6 s^-1 M^-1.

row_label: Table 2, row WT, SAH line

table_label: Table 2: Kinetic parameters for purine binding subsite mutants (Biochem Biophys Res Commun 2014, 446(4):965-970)


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8YBL1 FASTA direct lookup; R85A reconstructed after residue R85 matched the canonical sequence. and applied mutation signature R85A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q8YBL1 FASTA direct lookup; M144A reconstructed after residue M144 matched the canonical sequence.

proof_lines: mutant enzyme M144A, in 100 mM HEPES (pH 7.5), at 25°C


proof_lines: wild type enzyme, in 100 mM HEPES (pH 7.5), at 25°C


sequence_source: UniProtKB Q8YBL1 FASTA direct lookup; S167A reconstructed after residue S167 matched the canonical sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 canonical sequence reconstructed with mutation Y134A and applied mutation signature Y134A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 canonical sequence reconstructed with mutation Y134F and applied mutation signature Y134F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 canonical sequence reconstructed with mutation V34A and applied mutation signature V34A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 canonical sequence reconstructed with mutation W179F and applied mutation signature W179F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 canonical sequence reconstructed with mutation A15M and applied mutation signature A15M to reconstruct the assayed variant sequence.


sequence_source: UniProt Q8YBL1 canonical sequence reconstructed with mutation V34A

proof_lines: mutant enzyme V34A, in 100 mM HEPES (pH 7.5), at 25°C


sequence_source: UniProt Q8YBL1 canonical sequence reconstructed with mutation Y134F


sequence_source: UniProt Q8YBL1 canonical sequence reconstructed with mutation Y134A


sequence_source: UniProtKB Q9FYS3 FASTA fetched 2026-06-05; reviewed Swiss-Prot HGGL_SECCE canonical sequence.


sequence_source: UniProtKB Q9FYS3 FASTA fetched 2026-06-05; variant sequence reconstructed from selected mutation_signature using RCSB/UniProt mature-chain offset +49.

sequence_variant_note: Mutation signature Y378A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +9, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature G464S/S465L could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase(Enzyme) mutant G464S/S465L His-tagged


sequence_variant_note: Mutation signature G464F 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 Q8YBL1 canonical sequence plus checked residue substitution reconstruction and applied mutation signature R85A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R85A, in 100 mM HEPES (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 canonical sequence plus checked residue substitution reconstruction and applied mutation signature Y134A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y134A, in 100 mM HEPES (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 canonical sequence plus checked residue substitution reconstruction and applied mutation signature V34I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V34I, in 100 mM HEPES (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 canonical sequence plus checked residue substitution reconstruction and applied mutation signature A15M to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A15M, in 100 mM HEPES (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 canonical sequence plus checked residue substitution reconstruction and applied mutation signature W179A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 canonical sequence plus checked residue substitution reconstruction and applied mutation signature R164A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R164A, in 100 mM HEPES (pH 7.5), at 25°C


sequence_source: UniProt Q8YBL1 canonical sequence plus checked residue substitution reconstruction


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 canonical sequence, variant reconstructed by applying V34I after direct residue check and applied mutation signature V34I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 canonical sequence, variant reconstructed by applying W179A after direct residue check and applied mutation signature W179A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W179A, in 100 mM HEPES (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 canonical sequence, variant reconstructed by applying R85A after direct residue check and applied mutation signature R85A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 canonical sequence, variant reconstructed by applying R85H after direct residue check and applied mutation signature R85H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q8YBL1 canonical sequence, variant reconstructed by applying V34A after direct residue check and applied mutation signature V34A to reconstruct the assayed variant sequence.


sequence_source: UniProt Q8YBL1 canonical sequence, variant reconstructed by applying R85H after direct residue check

proof_lines: mutant enzyme R85H, in 100 mM HEPES (pH 7.5), at 25°C


sequence_source: UniProt Q8YBL1 canonical sequence

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

column_label: Table 2 (Kinetic parameters for purine binding subsite mutants), Enzyme column 'WT', Substrate column 'MTA'; column 'Km (uM)' = 2.2; column 'Kcat (s^-1)' = 8.8; column 'kcat/Km (s^-1 M^-1)' = 4.0 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 2.2 uM; 2.2 / 1000 = 0.0022 mM; the catalog value is 0.0022 mM. kcat: printed Table 2 cell 8.8 s^-1; already in s^-1, so no unit conversion applies; the catalog value is 8.8 s^(-1). kcat/Km: printed Table 2 cell 4.0 x 10^6 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.0 x 10^6 x 0.001 = 4000.0 s^-1 mM^-1. The quotient of the two printed component cells is 8.8 / 0.0022 = 4000.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, row WT, substrate MTA: Km = 2.2 uM; Kcat = 8.8 s^-1; printed kcat/Km = 4.0 x 10^6 s^-1 M^-1.

row_label: Table 2, row WT, MTA line


organism: Escherichia coli

sequence_source: UniProt P0AF14 canonical sequence

assay_conditions_summary: pH 7

proof_lines: recombinant enzyme, in 50 mM potassium phosphate, pH 7.0


organism: Helicobacter pylori

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9ZMY2 canonical sequence plus selected source F107A mutation; residue 107 changed from F to A. and applied mutation signature F107A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9ZMY2 canonical sequence plus PMID 23148563/source F107A mutation; residue 107 changed from F to A. and applied mutation signature F107A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9ZMY2 canonical sequence plus PMID 23148563/source F107A mutation; residue 107 changed from F to A.


sequence_source: UniProtKB Q9ZMY2 canonical sequence from direct accession lookup.


organism: Lupinus luteus

substrate_name: 5'-Deoxy-5'-(methylthio)adenosine; H2O

sequence_source: UniProtKB B6DX57 canonical sequence from direct accession lookup.

substrate: 5'-Deoxy-5'-(methylthio)adenosine; H2O


organism: Oryza sativa

sequence_source: UniProtKB Q8W162 canonical sequence from direct accession lookup.


organism: Staphylococcus aureus

source_db: brenda;skid

sequence_source: UniProtKB Q99TQ0 canonical sequence from direct accession lookup.

source: brenda;skid


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8YBL1 and applied mutation signature R85H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8YBL1 and applied mutation signature S167A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S167A, in 100 mM HEPES (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8YBL1 and applied mutation signature Y134F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y134F, in 100 mM HEPES (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8YBL1 and applied mutation signature R164A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8YBL1 and applied mutation signature M144A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8YBL1 and applied mutation signature W179A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8YBL1 and applied mutation signature W179F to reconstruct the assayed variant sequence.


proof_lines: mutant enzyme W179F, in 100 mM HEPES (pH 7.5), at 25°C


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


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

proof_lines: mutant enzyme F104C/C186S, at pH 7.2 and 25°C


organism: Streptococcus pneumoniae

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


organism: Vibrio cholerae


proof_lines: mutant enzyme A113P/V153I/R158G, at pH 7.7 and 25°C


organism: Consolida orientalis

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


substrate_name: 4-nitrophenyl beta-D-galactoside

proof_lines:
pH 5.8, 37°C, recombinant protein
pH 5.8, 37°C, native protein
pH 5.5, 25°C

substrate: 4-nitrophenyl beta-D-galactoside


sequence_variant_note: Resolved canonical sequence from UniProtKB:A5F5R2 canonical sequence reconstructed with RCSB:4X24 SEQADV substitutions and applied mutation signature A113P/V153I/R158G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A5F5R2 canonical sequence reconstructed with selected V153I mutation and applied mutation signature V153I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A5F5R2 canonical sequence reconstructed with selected A113P mutation and applied mutation signature A113P to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A5F5R2 FASTA; RCSB:4WKB no-mutation A5F5R2 structure context


sequence_variant_note: Resolved canonical sequence from UniProtKB:A5F5R2 canonical sequence reconstructed with selected A113P/V153I mutations and applied mutation signature A113P/V153I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A113P/V153I, at pH 7.7 and 25°C


sequence_source: UniProtKB:A5F5R2 canonical sequence reconstructed with selected V153I mutation


enzyme_display_name: alcohol sulfotransferase

organism: Arabidopsis thaliana

sequence_source: UniProtKB:P52839 FASTA/JSON direct lookup 2026-06-05

enzyme: alcohol sulfotransferase


substrate_name: p-Cresol

substrate: p-Cresol