sequence_variant_note: Resolved canonical sequence from UniProt REST/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence and applied mutation signature Y196F to reconstruct the assayed variant sequence.


organism: Homo sapiens

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UBV7 and applied mutation signature R270A to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7; 310.15 K; buffer 100 mm sodium cacodylate

column_label: Table 1: Kinetic parameters of wild-type and mutant GST-b4GalT7 (J. Biol. Chem. 2015, 290(12):7658). Enzyme row R270A; shared kcat column cell = 46.4 min^-1; 4-MUX Km column cell = 0.60 mm; 4-MUX kcat/Km column cell = 72 min^-1 mm^-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 46.4 under the column head kcat (min-1); one min^-1 is 1/60 s^-1, so 46.4 / 60 = 0.7733333333333333 s^-1; the exported value is 0.77 s^(-1). Km: printed Table 1 cell 0.60 under the 4-MUX column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.6 mM; the exported value is 0.6 mM. kcat/Km: printed Table 1 cell 72 under the 4-MUX column head kcat/Km (min-1.mm-1); one min^-1 mm^-1 is 1/60 s^-1 mM^-1, so 72 / 60 = 1.2 s^-1 mM^-1; the exported value is 1.2833333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R270A, 4-MUX columns: kcat = 46.4 min^-1 (printed with its tolerance +/- 0.2); Km = 0.60 mm (printed with its tolerance +/- 0.02); kcat/Km = 72 min^-1 mm^-1. The printed column heads are kcat (min-1), Km (mm) and kcat/Km (min-1.mm-1), and Table 1 prints one shared kcat column that serves both the UDP-Gal and the 4-MUX columns of the enzyme row.

data_origin: experimental

status: corrected

source: oed


substrate_name: UDP-alpha-D-galactose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UBV7 and applied mutation signature H195R to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wild-type and mutant GST-b4GalT7 (J. Biol. Chem. 2015, 290(12):7658). Enzyme row H195R; shared kcat column cell = 89.6 min^-1; UDP-Gal Km column cell = 0.32 mm; UDP-Gal kcat/Km column cell = 295 min^-1 mm^-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 89.6 under the column head kcat (min-1); one min^-1 is 1/60 s^-1, so 89.6 / 60 = 1.4933333333333332 s^-1; the exported value is 1.49 s^(-1). Km: printed Table 1 cell 0.32 under the UDP-Gal column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.32 mM; the exported value is 0.32 mM. kcat/Km: printed Table 1 cell 295 under the UDP-Gal column head kcat/Km (min-1.mm-1); one min^-1 mm^-1 is 1/60 s^-1 mM^-1, so 295 / 60 = 4.916666666666667 s^-1 mM^-1; the exported value is 4.65625 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row H195R, UDP-Gal columns: kcat = 89.6 min^-1 (printed with its tolerance +/- 1.3); Km = 0.32 mm (printed with its tolerance +/- 0.02); kcat/Km = 295 min^-1 mm^-1. The printed column heads are kcat (min-1), Km (mm) and kcat/Km (min-1.mm-1), and Table 1 prints one shared kcat column that serves both the UDP-Gal and the 4-MUX columns of the enzyme row.

substrate: UDP-alpha-D-galactose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UBV7 and applied mutation signature H195A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wild-type and mutant GST-b4GalT7 (J. Biol. Chem. 2015, 290(12):7658). Enzyme row H195A; shared kcat column cell = 115.9 min^-1; 4-MUX Km column cell = 0.64 mm; 4-MUX kcat/Km column cell = 180 min^-1 mm^-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 115.9 under the column head kcat (min-1); one min^-1 is 1/60 s^-1, so 115.9 / 60 = 1.9316666666666669 s^-1; the exported value is 1.93 s^(-1). Km: printed Table 1 cell 0.64 under the 4-MUX column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.64 mM; the exported value is 0.64 mM. kcat/Km: printed Table 1 cell 180 under the 4-MUX column head kcat/Km (min-1.mm-1); one min^-1 mm^-1 is 1/60 s^-1 mM^-1, so 180 / 60 = 3.0 s^-1 mM^-1; the exported value is 3.015625 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row H195A, 4-MUX columns: kcat = 115.9 min^-1 (printed with its tolerance +/- 9.7); Km = 0.64 mm (printed with its tolerance +/- 0.02); kcat/Km = 180 min^-1 mm^-1. The printed column heads are kcat (min-1), Km (mm) and kcat/Km (min-1.mm-1), and Table 1 prints one shared kcat column that serves both the UDP-Gal and the 4-MUX columns of the enzyme row.


source_db: brenda

kcat_over_km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProt REST/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence and applied mutation signature R270K to reconstruct the assayed variant sequence.

source: brenda


kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from UniProt REST/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence and applied mutation signature H195Q to reconstruct the assayed variant sequence.


column_label: Table 1: Kinetic parameters of wild-type and mutant GST-b4GalT7 (J. Biol. Chem. 2015, 290(12):7658). Enzyme row H195A; shared kcat column cell = 115.9 min^-1; UDP-Gal Km column cell = 0.40 mm; UDP-Gal kcat/Km column cell = 291 min^-1 mm^-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 115.9 under the column head kcat (min-1); one min^-1 is 1/60 s^-1, so 115.9 / 60 = 1.9316666666666669 s^-1; the exported value is 1.93 s^(-1). Km: printed Table 1 cell 0.40 under the UDP-Gal column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.4 mM; the exported value is 0.4 mM. kcat/Km: printed Table 1 cell 291 under the UDP-Gal column head kcat/Km (min-1.mm-1); one min^-1 mm^-1 is 1/60 s^-1 mM^-1, so 291 / 60 = 4.85 s^-1 mM^-1; the exported value is 4.824999999999999 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row H195A, UDP-Gal columns: kcat = 115.9 min^-1 (printed with its tolerance +/- 9.7); Km = 0.40 mm (printed with its tolerance +/- 0.02); kcat/Km = 291 min^-1 mm^-1. The printed column heads are kcat (min-1), Km (mm) and kcat/Km (min-1.mm-1), and Table 1 prints one shared kcat column that serves both the UDP-Gal and the 4-MUX columns of the enzyme row.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UBV7 and applied mutation signature Y199F to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wild-type and mutant GST-b4GalT7 (J. Biol. Chem. 2015, 290(12):7658). Enzyme row Y199F; shared kcat column cell = 72.3 min^-1; UDP-Gal Km column cell = 0.32 mm; UDP-Gal kcat/Km column cell = 243 min^-1 mm^-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 72.3 under the column head kcat (min-1); one min^-1 is 1/60 s^-1, so 72.3 / 60 = 1.2049999999999998 s^-1; the exported value is 1.21 s^(-1). Km: printed Table 1 cell 0.32 under the UDP-Gal column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.32 mM; the exported value is 0.32 mM. kcat/Km: printed Table 1 cell 243 under the UDP-Gal column head kcat/Km (min-1.mm-1); one min^-1 mm^-1 is 1/60 s^-1 mM^-1, so 243 / 60 = 4.05 s^-1 mM^-1; the exported value is 3.78125 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row Y199F, UDP-Gal columns: kcat = 72.3 min^-1 (printed with its tolerance +/- 5.8); Km = 0.32 mm (printed with its tolerance +/- 0.02); kcat/Km = 243 min^-1 mm^-1. The printed column heads are kcat (min-1), Km (mm) and kcat/Km (min-1.mm-1), and Table 1 prints one shared kcat column that serves both the UDP-Gal and the 4-MUX columns of the enzyme row.


substrate_name: 2-naphthyl 5-thio-beta-D-xylopyranoside

verification_status: unverified

mutation_signature: Unknown

sequence_source: UniProtKB direct lookup Q9UBV7, retrieved 2026-06-16

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

substrate: 2-naphthyl 5-thio-beta-D-xylopyranoside

status: unverified


enzyme_display_name: xanthine phosphoribosyltransferase

organism: Bacillus subtilis

substrate_name: hypoxanthine; xanthine; guanine; 5-phospho-alpha-D-ribose 1-diphosphate

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

sequence_source: UniProtKB direct lookup P42085, retrieved 2026-06-16

proof_lines:
cosubstrate: xanthine
at pH 7.6 and 25°C
Kis

source_databases_merged: brenda skid

enzyme: xanthine phosphoribosyltransferase


organism: Enterococcus faecalis

substrate_name: Xanthine; 5-Phospho-alpha-D-ribose 1-diphosphate; Xanthine; 5-Phospho-alpha-D-ribose 1-diphosphate; XMP; Diphosphate; 5-Phospho-alpha-D-ribose 1-diphosphate; Xanthine

kcat_display: Not reported

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

sequence_source: UniProtKB direct lookup Q831Y0, retrieved 2026-06-16


organism: Escherichia coli

substrate_name: Guanine; 5-Phospho-alpha-D-ribose 1-diphosphate; Guanine; 5-Phospho-alpha-D-ribose 1-diphosphate; GMP; Diphosphate; Xanthine; 5-Phospho-alpha-D-ribose 1-diphosphate; Xanthine; XMP; 5-Phospho-alpha-D-ribose 1-diphosphate; Hypoxanthine; Hypoxanthine; IMP; xanthine

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 direct lookup P0A9M5, retrieved 2026-06-16

proof_lines: pH and temperature not specified in the publication

source_databases_merged: sabio_rk brenda skid


organism: Leishmania donovani

substrate_name: hypoxanthine; 5-phospho-alpha-D-ribose 1-diphosphate; guanine; xanthine

sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup Q9U6Y2, retrieved 2026-06-16 and applied mutation signature I209V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7

proof_lines: mutant enzyme I209V, at pH 7.0, temperature not specified in the publication

proof_lines: mutant enzyme I209V, with hypoxanthine as cosubstrate, at pH 7.0, temperature not specified in the publication

proof_lines: mutant enzyme I209V, with xanthine as cosubstrate, at pH 7.0, temperature not specified in the publication


substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate; guanine; hypoxanthine; xanthine

sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup Q9U6Y2, retrieved 2026-06-16 and applied mutation signature Y208F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y208F, with hypoxanthine as cosubstrate, at pH 7.0, temperature not specified in the publication

proof_lines: mutant enzyme Y208F, with xanthine as cosubstrate, at pH 7.0, temperature not specified in the publication

proof_lines: mutant enzyme Y208F, at pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup Q9U6Y2, retrieved 2026-06-16 and applied mutation signature I209V/E215D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I209V/E215D, at pH 7.0, temperature not specified in the publication

proof_lines: mutant enzyme I209V/E215D, with hypoxanthine as cosubstrate, at pH 7.0, temperature not specified in the publication

proof_lines: mutant enzyme I209V/E215D, with xanthine as cosubstrate, at pH 7.0, temperature not specified in the publication

substrate: hypoxanthine; 5-phospho-alpha-D-ribose 1-diphosphate; guanine; xanthine


substrate_name: hypoxanthine; 5-phospho-alpha-D-ribose 1-diphosphate; xanthine; guanine

sequence_source: UniProtKB direct lookup Q9U6Y2, retrieved 2026-06-16

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

proof_lines: wild type enzyme, with hypoxanthine as cosubstrate, at pH 7.0, temperature not specified in the publication

proof_lines: wild type enzyme, with xanthine as cosubstrate, at pH 7.0, temperature not specified in the publication


organism: Plasmodium falciparum

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

sequence_source: UniProtKB direct lookup Q8IJS1, retrieved 2026-06-16

proof_lines: pH 7.4, temperature not specified in the publication

substrate: Unknown


enzyme_display_name: carnitine O-acetyltransferase

organism: Columba livia

substrate_name: CoA

sequence_source: UniProt P52826 reviewed canonical sequence

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

assay_conditions_summary: pH 7.8; 298.15 K; cofactor CoA

proof_lines:
at pH 7.8 and 25°C
at pH 7.6 and 37°C

enzyme: carnitine O-acetyltransferase

substrate: CoA


substrate_name: acetyl-CoA

sequence_source: UniProt P43155 canonical sequence checked; row-specific variant not reconstructed

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

assay_conditions_summary: pH 8; cofactor CoA

substrate: acetyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProt P43155 canonical sequence with direct one-based reconstruction of R497Q and applied mutation signature R497Q to reconstruct the assayed variant sequence.


sequence_source: UniProt P43155 reviewed canonical sequence


substrate_name: Acetyl-CoA; L-Carnitine

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

substrate: Acetyl-CoA; L-Carnitine


organism: Mus musculus

sequence_variant_note: Resolved canonical sequence from UniProt P47934 canonical sequence with direct one-based reconstruction of S554A and applied mutation signature S554A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; 294.15 K; cofactor CoA


sequence_source: UniProt P47934 reviewed canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProt P47934 canonical sequence with direct one-based reconstruction of S554A/M564G and applied mutation signature S554A/M564G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P47934 canonical sequence with direct one-based reconstruction of H343E and applied mutation signature H343E to reconstruct the assayed variant sequence.


substrate_name: hexanoyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProt P47934 canonical sequence with direct one-based reconstruction of M564G and applied mutation signature M564G to reconstruct the assayed variant sequence.

substrate: hexanoyl-CoA


substrate_name: carnitine

assay_conditions_summary: pH 8; 294.15 K; cofactor CoA

proof_lines: mitochondria from liver, pH 8.0, temperature not specified in the publication

proof_lines: liver homogenate, pH 8.0, temperature not specified in the publication

proof_lines: heart homogenate, pH 8.0, temperature not specified in the publication

substrate: carnitine


organism: Rattus norvegicus

substrate_name: Acetyl-CoA; Carnitine

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

sequence_source: UniProt Q704S8 reviewed canonical sequence

assay_conditions_summary: pH 7.8; 303.15 K; cofactor CoA

proof_lines: recombinant enzyme from yeast, pH 7.8, 30°C

proof_lines: recombinant enzyme from yeast with butyryl-CoA as second substrate, pH 7.8, 30°C

proof_lines: recombinant enzyme from yeast with hexanoyl-CoA as second substrate, pH 7.8, 30°C

substrate: Acetyl-CoA; Carnitine


substrate_name: Octanoyl-CoA; L-Carnitine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q704S8 reviewed sequence version 1; direct REST/FASTA check 2026-06-16 and applied mutation signature M564G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: carnitine O-acetyltransferase(Enzyme) mutant M564G

proof_lines: M564G mutant enzyme from yeast with butyryl-CoA as second substrate, pH 7.8, 30°C

proof_lines: M564G mutant enzyme from yeast, pH 7.8, 30°C

substrate: Octanoyl-CoA; L-Carnitine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9UBV7 reviewed sequence version 1; direct REST/FASTA check 2026-06-16 and applied mutation signature H195A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9UBV7 reviewed sequence version 1; direct REST/FASTA check 2026-06-16 and applied mutation signature R270A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UBV7 and applied mutation signature H195R to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wild-type and mutant GST-b4GalT7 (J. Biol. Chem. 2015, 290(12):7658). Enzyme row H195R; shared kcat column cell = 89.6 min^-1; 4-MUX Km column cell = 0.35 mm; 4-MUX kcat/Km column cell = 242 min^-1 mm^-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 89.6 under the column head kcat (min-1); one min^-1 is 1/60 s^-1, so 89.6 / 60 = 1.4933333333333332 s^-1; the exported value is 1.49 s^(-1). Km: printed Table 1 cell 0.35 under the 4-MUX column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.35 mM; the exported value is 0.35 mM. kcat/Km: printed Table 1 cell 242 under the 4-MUX column head kcat/Km (min-1.mm-1); one min^-1 mm^-1 is 1/60 s^-1 mM^-1, so 242 / 60 = 4.033333333333333 s^-1 mM^-1; the exported value is 4.257142857142857 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row H195R, 4-MUX columns: kcat = 89.6 min^-1 (printed with its tolerance +/- 1.3); Km = 0.35 mm (printed with its tolerance +/- 0.03); kcat/Km = 242 min^-1 mm^-1. The printed column heads are kcat (min-1), Km (mm) and kcat/Km (min-1.mm-1), and Table 1 prints one shared kcat column that serves both the UDP-Gal and the 4-MUX columns of the enzyme row.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9UBV7 reviewed sequence version 1; direct REST/FASTA check 2026-06-16 and applied mutation signature R226A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9UBV7 reviewed sequence version 1; direct REST/FASTA check 2026-06-16 and applied mutation signature Y196F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UBV7 and applied mutation signature Y199F to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wild-type and mutant GST-b4GalT7 (J. Biol. Chem. 2015, 290(12):7658). Enzyme row Y199F; shared kcat column cell = 72.3 min^-1; 4-MUX Km column cell = 0.59 mm; 4-MUX kcat/Km column cell = 113 min^-1 mm^-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 72.3 under the column head kcat (min-1); one min^-1 is 1/60 s^-1, so 72.3 / 60 = 1.2049999999999998 s^-1; the exported value is 1.21 s^(-1). Km: printed Table 1 cell 0.59 under the 4-MUX column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.59 mM; the exported value is 0.59 mM. kcat/Km: printed Table 1 cell 113 under the 4-MUX column head kcat/Km (min-1.mm-1); one min^-1 mm^-1 is 1/60 s^-1 mM^-1, so 113 / 60 = 1.8833333333333333 s^-1 mM^-1; the exported value is 2.0508474576271185 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row Y199F, 4-MUX columns: kcat = 72.3 min^-1 (printed with its tolerance +/- 5.8); Km = 0.59 mm (printed with its tolerance +/- 0.06); kcat/Km = 113 min^-1 mm^-1. The printed column heads are kcat (min-1), Km (mm) and kcat/Km (min-1.mm-1), and Table 1 prints one shared kcat column that serves both the UDP-Gal and the 4-MUX columns of the enzyme row.


sequence_source: UniProtKB:Q9UBV7 reviewed sequence version 1; direct REST/FASTA check 2026-06-16

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 uniprot_rest_accession:Q9UBV7 and applied mutation signature R226K to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wild-type and mutant GST-b4GalT7 (J. Biol. Chem. 2015, 290(12):7658). Enzyme row R226K; shared kcat column cell = 81.1 min^-1; UDP-Gal Km column cell = 0.29 mm; UDP-Gal kcat/Km column cell = 282 min^-1 mm^-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 81.1 under the column head kcat (min-1); one min^-1 is 1/60 s^-1, so 81.1 / 60 = 1.3516666666666666 s^-1; the exported value is 1.35 s^(-1). Km: printed Table 1 cell 0.29 under the UDP-Gal column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.29 mM; the exported value is 0.29 mM. kcat/Km: printed Table 1 cell 282 under the UDP-Gal column head kcat/Km (min-1.mm-1); one min^-1 mm^-1 is 1/60 s^-1 mM^-1, so 282 / 60 = 4.7 s^-1 mM^-1; the exported value is 4.655172413793104 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R226K, UDP-Gal columns: kcat = 81.1 min^-1 (printed with its tolerance +/- 2.9); Km = 0.29 mm (printed with its tolerance +/- 0.02); kcat/Km = 282 min^-1 mm^-1. The printed column heads are kcat (min-1), Km (mm) and kcat/Km (min-1.mm-1), and Table 1 prints one shared kcat column that serves both the UDP-Gal and the 4-MUX columns of the enzyme row.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9UBV7 reviewed sequence version 1; direct REST/FASTA check 2026-06-16 and applied mutation signature Y199F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UBV7 and applied mutation signature R226A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wild-type and mutant GST-b4GalT7 (J. Biol. Chem. 2015, 290(12):7658). Enzyme row R226A; shared kcat column cell = 53.6 min^-1; UDP-Gal Km column cell = 0.34 mm; UDP-Gal kcat/Km column cell = 171 min^-1 mm^-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 53.6 under the column head kcat (min-1); one min^-1 is 1/60 s^-1, so 53.6 / 60 = 0.8933333333333333 s^-1; the exported value is 0.89 s^(-1). Km: printed Table 1 cell 0.34 under the UDP-Gal column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.34 mM; the exported value is 0.34 mM. kcat/Km: printed Table 1 cell 171 under the UDP-Gal column head kcat/Km (min-1.mm-1); one min^-1 mm^-1 is 1/60 s^-1 mM^-1, so 171 / 60 = 2.85 s^-1 mM^-1; the exported value is 2.6176470588235294 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R226A, UDP-Gal columns: kcat = 53.6 min^-1 (printed with its tolerance +/- 2.0); Km = 0.34 mm (printed with its tolerance +/- 0.03); kcat/Km = 171 min^-1 mm^-1. The printed column heads are kcat (min-1), Km (mm) and kcat/Km (min-1.mm-1), and Table 1 prints one shared kcat column that serves both the UDP-Gal and the 4-MUX columns of the enzyme row.


column_label: Table 1: Kinetic parameters of wild-type and mutant GST-b4GalT7 (J. Biol. Chem. 2015, 290(12):7658). Enzyme row R226K; shared kcat column cell = 81.1 min^-1; 4-MUX Km column cell = 0.46 mm; 4-MUX kcat/Km column cell = 175 min^-1 mm^-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 81.1 under the column head kcat (min-1); one min^-1 is 1/60 s^-1, so 81.1 / 60 = 1.3516666666666666 s^-1; the exported value is 1.35 s^(-1). Km: printed Table 1 cell 0.46 under the 4-MUX column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.46 mM; the exported value is 0.46 mM. kcat/Km: printed Table 1 cell 175 under the 4-MUX column head kcat/Km (min-1.mm-1); one min^-1 mm^-1 is 1/60 s^-1 mM^-1, so 175 / 60 = 2.9166666666666665 s^-1 mM^-1; the exported value is 2.9347826086956523 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R226K, 4-MUX columns: kcat = 81.1 min^-1 (printed with its tolerance +/- 2.9); Km = 0.46 mm (printed with its tolerance +/- 0.01); kcat/Km = 175 min^-1 mm^-1. The printed column heads are kcat (min-1), Km (mm) and kcat/Km (min-1.mm-1), and Table 1 prints one shared kcat column that serves both the UDP-Gal and the 4-MUX columns of the enzyme row.


column_label: Table 1: Kinetic parameters of wild-type and mutant GST-b4GalT7 (J. Biol. Chem. 2015, 290(12):7658). Enzyme row R226A; shared kcat column cell = 53.6 min^-1; 4-MUX Km column cell = 0.44 mm; 4-MUX kcat/Km column cell = 112 min^-1 mm^-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 53.6 under the column head kcat (min-1); one min^-1 is 1/60 s^-1, so 53.6 / 60 = 0.8933333333333333 s^-1; the exported value is 0.89 s^(-1). Km: printed Table 1 cell 0.44 under the 4-MUX column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.44 mM; the exported value is 0.44 mM. kcat/Km: printed Table 1 cell 112 under the 4-MUX column head kcat/Km (min-1.mm-1); one min^-1 mm^-1 is 1/60 s^-1 mM^-1, so 112 / 60 = 1.8666666666666667 s^-1 mM^-1; the exported value is 2.022727272727273 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R226A, 4-MUX columns: kcat = 53.6 min^-1 (printed with its tolerance +/- 2.0); Km = 0.44 mm (printed with its tolerance +/- 0.05); kcat/Km = 112 min^-1 mm^-1. The printed column heads are kcat (min-1), Km (mm) and kcat/Km (min-1.mm-1), and Table 1 prints one shared kcat column that serves both the UDP-Gal and the 4-MUX columns of the enzyme row.


substrate_name: naphthalen-2-yl beta-D-xylopyranoside

substrate: naphthalen-2-yl beta-D-xylopyranoside


enzyme_display_name: alanine--glyoxylate transaminase

substrate_name: glyoxylate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P21549 direct REST/FASTA lookup; variant reconstructed from selected mutation_signature and applied mutation signature R118A to reconstruct the assayed variant sequence.

smiles: O=CC(=O)O

enzyme: alanine--glyoxylate transaminase

substrate: glyoxylate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P21549 direct REST/FASTA lookup; variant reconstructed from selected mutation_signature and applied mutation signature F240S to reconstruct the assayed variant sequence.


substrate_name: L-alanine

sequence_source: UniProtKB reviewed P21549 direct REST/FASTA lookup; variant reconstructed from selected mutation_signature

substrate: L-alanine


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P21549 direct REST/FASTA lookup; variant reconstructed from selected mutation_signature and applied mutation signature F238S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed P21549 direct REST/FASTA lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P21549 direct REST/FASTA lookup; variant reconstructed from selected mutation_signature and applied mutation signature I56N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P21549 direct REST/FASTA lookup; variant reconstructed from selected mutation_signature and applied mutation signature P11R/I56N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P21549 direct REST/FASTA lookup; variant reconstructed from selected mutation_signature and applied mutation signature P11R to reconstruct the assayed variant sequence.


proof_lines: recombinant mutant P11R-Ma, pH 7.4, 25°C


proof_lines: recombinant mutant P11R/I56N-Ma, pH 7.4, 25°C


sequence_source: UniProtKB REST direct lookup accession Q9UBV7 on 2026-06-16


organism: Aedes aegypti

sequence_source: UniProtKB REST direct lookup accession Q3LSM4 on 2026-06-16

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

assay_conditions_summary: pH 7.5; 318.15 K; buffer 100 mM potassium phosphate

proof_lines: in 100 mM potassium phosphate buffer (pH 7.5) for 5 min at 45°C


organism: Arabidopsis thaliana

substrate_name: L-Alanine; Glyoxylate

sequence_source: UniProtKB REST direct lookup accession Q56YA5 on 2026-06-16

proof_lines: pH 7.0, 37°C, SGT activity, pyruvate as amino acceptor

proof_lines: pH 7.0, 37°C, SGT activity, glyoxylate as amino acceptor

proof_lines: pH 7.0, 37°C, glyoxylate as amino acceptor

substrate: L-Alanine; Glyoxylate


sequence_source: UniProtKB REST direct lookup accession Q9S7E9 on 2026-06-16

proof_lines:
cosubstrate L-glutamate, pH 7.5, 25°C
cosubstrate L-alanine, pH 7.5, 25°C
pH 7.5, 25°C


sequence_source: UniProtKB REST direct lookup accession Q9SR86 on 2026-06-16


organism: Drosophila melanogaster

sequence_source: UniProtKB REST direct lookup accession Q9W3Z3 on 2026-06-16

proof_lines: pH 7.0, 50°C, glyoxylate as amino acceptor


organism: Felis silvestris catus

sequence_source: UniProtKB REST direct lookup accession P41689 on 2026-06-16


sequence_source: UniProtKB REST direct lookup accession P21549 on 2026-06-16

proof_lines: pH 7.4, Km value of L-cysteine is decreased by 40fold and 200fold in comparison with those of L-alanine and L-serine


sequence_source: UniProtKB REST direct lookup accession A2V838 on 2026-06-16

proof_lines: with L-alanine as varied substrate and glyoxylate as fixed substrate, Kis

proof_lines: with glyoxylate as varied substrate and L-alanine as fixed substrate, Kii


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup accession A2V838 on 2026-06-16 and applied mutation signature G82E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup accession P21549 on 2026-06-16 and applied mutation signature F152I to reconstruct the assayed variant sequence.

proof_lines:
minor allele mutant enzyme F152I
major allele mutant enzyme F152I


proof_lines: recombinant wild-type enzyme AGT-Mi, pH 7.4, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup accession P21549 on 2026-06-16 and applied mutation signature F152A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup accession P21549 on 2026-06-16 and applied mutation signature F240S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST accession P21549, checked 2026-06-16 and applied mutation signature P11R/I56N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST accession P21549, checked 2026-06-16 and applied mutation signature I56N to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant I56N-Mi, pH 7.4, 25°C

proof_lines: recombinant mutant I56N-Ma, pH 7.4, 25°C


organism: Hydrogenobacter thermophilus

sequence_source: UniProt REST accession D2Z0I0, checked 2026-06-16

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


sequence_source: UniProt REST accession Q3UEG6, checked 2026-06-16


substrate_name: Glyoxylate; L-Alanine

sequence_source: UniProt REST accession O35423, checked 2026-06-16

substrate: Glyoxylate; L-Alanine


sequence_source: UniProt REST accession Q64565, checked 2026-06-16


sequence_source: UniProt REST accession P09139, checked 2026-06-16


organism: Saccharomyces cerevisiae

sequence_source: UniProt REST accession P43567, checked 2026-06-16

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


enzyme_display_name: UMP/CMP kinase

substrate_name: UMP

sequence_source: UniProt REST accession O04905, checked 2026-06-16

assay_conditions_summary: pH 6.5; cofactor ATP

proof_lines:
pH 6.5
pH 6.5, when UMP is the other substrate
pH 6.5, reaction with CMP

enzyme: UMP/CMP kinase

substrate: UMP


organism: Dictyostelium discoideum

substrate_name: CMP

sequence_source: UniProt REST accession P20425, checked 2026-06-16

substrate: CMP


substrate_name: UMP; ATP

assay_conditions_summary: cofactor ATP

substrate: UMP; ATP


substrate_name: dCMP

substrate: dCMP


substrate_name: ATP; CMP

sequence_source: UniProt REST accession P30085, checked 2026-06-16

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines:
pH 8.0, 37°C
L-enantiomers have lower reaction rates

substrate: ATP; CMP


sequence_source: UniProtKB reviewed accession P30085 (KCY_HUMAN); REST lookup 2026-06-16; sequence version 3.


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

mutation_type: deletion

proof_lines: SABIO-RK modifier species: UMP/CMP kinase(Enzyme) wildtype CMPK2delta21-6His


substrate_name: dUMP

sequence_source: UniProtKB reviewed accession Q5EBM0 (CMPK2_HUMAN); REST lookup 2026-06-16; sequence version 3.

substrate: dUMP


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P30085 (KCY_HUMAN); REST lookup 2026-06-16; sequence version 3. Variant reconstructed from selected mutation annotation. and applied mutation signature P64T to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, recombinant mutant P64T


substrate_name: cytarabine

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

substrate: cytarabine


enzyme_display_name: nucleoside-diphosphate kinase

organism: Acanthamoeba polyphaga mimivirus

substrate_name: ATP; dGDP

sequence_source: UniProtKB reviewed accession Q5UQL3 (NDK_MIMIV); REST lookup 2026-06-16; sequence version 1.

enzyme: nucleoside-diphosphate kinase

substrate: ATP; dGDP


organism: Aspergillus fumigatus

substrate_name: ATP

sequence_source: UniProtKB reviewed accession Q7Z8P9 (NDK_ASPFU); REST lookup 2026-06-16; sequence version 1.

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

substrate: ATP


substrate_name: CTP

substrate: CTP


substrate_name: GTP

substrate: GTP


substrate_name: UTP

substrate: UTP


substrate_name: TTP

substrate: TTP


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


substrate_name: ITP

substrate: ITP


organism: Halobacterium salinarum

substrate_name: ADP

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P61136 (NDK_HALSA); REST lookup 2026-06-16; sequence version 1. Variant reconstructed from selected mutation annotation. and applied mutation signature G114R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ADP

proof_lines: mutant G114R, pH 7.5, 30°C, presence of 3.8 M NaCl

substrate: ADP


sequence_source: UniProtKB reviewed accession P61136 (NDK_HALSA); REST lookup 2026-06-16; sequence version 1.

proof_lines: wild-type, pH 7.5, 30°C, presence of 3.8 M NaCl


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB:P61136; REST accession lookup checked 2026-06-16

source: skid


organism: Lathyrus oleraceus

substrate_name: dCDP

sequence_source: UniProtKB:Q9SP13; REST accession lookup checked 2026-06-16

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

substrate: dCDP


substrate_name: dTDP

sequence_variant_note: Mutation signature S119A matches the mutant residue at offset +8 and the reference residue at offset -14; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: dTDP


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB:P9WJH7; REST accession lookup checked 2026-06-16

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP

proof_lines: competitive inhibition of nuclease activity


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WJH7; REST accession lookup checked 2026-06-16 and applied mutation signature D93N to reconstruct the assayed variant sequence.


organism: Pisum sativum

substrate_name: ATP; dCDP

proof_lines: SABIO-RK modifier species: nucleoside-diphosphate kinase(Enzyme) mutant S69A

substrate: ATP; dCDP


substrate_name: dCDP; ATP

assay_conditions_summary: 295.15 K; cofactor ATP

substrate: dCDP; ATP


proof_lines: SABIO-RK modifier species: nucleoside-diphosphate kinase(Enzyme) mutant S119A


substrate_name: GDP; ATP

sequence_source: UniProtKB:Q05982; REST accession lookup checked 2026-06-16

substrate: GDP; ATP


sequence_source: UniProtKB:P19804; REST accession lookup checked 2026-06-16


substrate_name: ATP; UDP

sequence_source: UniProtKB:P36010; REST accession lookup checked 2026-06-16

substrate: ATP; UDP


organism: Solanum chacoense

substrate_name: UDP

sequence_source: UniProtKB:Q3Y5A4; REST accession lookup checked 2026-06-16

substrate: UDP


organism: Trypanosoma cruzi

sequence_source: UniProtKB:Q4E256; REST accession lookup checked 2026-06-16

proof_lines: pH and temperature not specified in the publication


organism: Trypanosoma cruzi strain CL Brener

proof_lines:
pH 7.5, 35°C, isozyme NDPK2
pH 7.5, 35°C, isozyme NDPK1
Raw SKiD Env: Temp=35°C, pH=7.5


organism: Bos taurus

sequence_source: UniProtKB:A5D7T4 canonical sequence direct REST check on 2026-06-16.

proof_lines:
membrane-bound protein, at 37°C
soluble protein, at 37°C


organism: Homo sapiens

sequence_source: UniProtKB:P15907 canonical sequence direct REST check on 2026-06-16.

assay_conditions_summary: pH 6; 310.15 K; buffer 50 mM MES-NaOH

proof_lines: apparent value, recombinant enzyme, using pyridylamine-type 2H as cosubstrate, in 50 mM MES-NaOH buffer (pH 6.0), 1 mM MnCl2, at 37°C

proof_lines: apparent value, recombinant enzyme, using pyridylaminyl-lacto-N-neotetraose as cosubstrate, in 50 mM MES-NaOH buffer (pH 6.0), 1 mM MnCl2, at 37°C


organism: Photobacterium damselae

substrate_name: AA-labeled G2 glycan

sequence_source: UniProtKB:O66375 canonical sequence direct REST check on 2026-06-16.

substrate: AA-labeled G2 glycan


organism: Photobacterium leiognathi

sequence_source: UniProtKB:A8R0T5 canonical sequence direct REST check on 2026-06-16.


organism: Photobacterium sp.

sequence_source: UniProtKB:A8QYL1 canonical sequence direct REST check on 2026-06-16.

proof_lines:
at pH 8.0 and 30°C
Raw SKiD Env: Temp=-----, pH=-----


organism: Rattus norvegicus

sequence_source: UniProtKB:P13721 canonical sequence direct REST check on 2026-06-16.

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


substrate_name: CMP-N-acetylneuraminate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P13721 canonical sequence direct REST check on 2026-06-16; D271A reconstructed from selected source mutation label after residue-coordinate check. and applied mutation signature D271A to reconstruct the assayed variant sequence.

substrate: CMP-N-acetylneuraminate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13721 and applied mutation signature D271A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters for wild type rat ST6GAL1 and mutants using CMP-Neu5Ac as donor and N-acetyllactosamine as acceptor substrate (J. Biol. Chem. 2013, 288(48):34680-34698); enzyme-form row 'D271A'; donor CMP-NeuAc block: column 'Km (uM)' = 365; column 'kcat (min^-1)' = 2.9; column 'kcat/Km (mM^-1 min^-1)' = 8. The GFP fluorescence cell and the last three cells of the same printed row belong to the expression readout and to the acceptor Gal-beta-1,4-GlcNAc block.

raw_value_unit_evidence: Table 2, enzyme-form row 'D271A', donor CMP-Neu5Ac columns: Km = 365 uM; kcat = 2.9 min^-1; kcat/Km = 8 mM^-1 min^-1.

row_label: Table 2, enzyme-form row 'D271A', the three donor CMP-Neu5Ac cells (Km, kcat, kcat/Km)


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13721 and applied mutation signature Y119F to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters for wild type rat ST6GAL1 and mutants using CMP-Neu5Ac as donor and N-acetyllactosamine as acceptor substrate (J. Biol. Chem. 2013, 288(48):34680-34698); enzyme-form row 'Y119F'; donor CMP-NeuAc block: column 'Km (uM)' = 78; column 'kcat (min^-1)' = 23.4; column 'kcat/Km (mM^-1 min^-1)' = 300. The GFP fluorescence cell and the last three cells of the same printed row belong to the expression readout and to the acceptor Gal-beta-1,4-GlcNAc block.

raw_value_unit_evidence: Table 2, enzyme-form row 'Y119F', donor CMP-Neu5Ac columns: Km = 78 uM; kcat = 23.4 min^-1; kcat/Km = 300 mM^-1 min^-1.

row_label: Table 2, enzyme-form row 'Y119F', the three donor CMP-Neu5Ac cells (Km, kcat, kcat/Km)

status: verified


proof_lines: recombinant wild type enzyme from 293-F cells, at pH 6.5 and 37°C

proof_lines: recombinant wild type enzyme from HEK-293 cells, at pH 6.5 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13721 and applied mutation signature Y272A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters for wild type rat ST6GAL1 and mutants using CMP-Neu5Ac as donor and N-acetyllactosamine as acceptor substrate (J. Biol. Chem. 2013, 288(48):34680-34698); enzyme-form row 'Y272A'; donor CMP-NeuAc block: column 'Km (uM)' = 220; column 'kcat (min^-1)' = 3.0; column 'kcat/Km (mM^-1 min^-1)' = 14. The GFP fluorescence cell and the last three cells of the same printed row belong to the expression readout and to the acceptor Gal-beta-1,4-GlcNAc block.

raw_value_unit_evidence: Table 2, enzyme-form row 'Y272A', donor CMP-Neu5Ac columns: Km = 220 uM; kcat = 3.0 min^-1; kcat/Km = 14 mM^-1 min^-1.

row_label: Table 2, enzyme-form row 'Y272A', the three donor CMP-Neu5Ac cells (Km, kcat, kcat/Km)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13721 canonical sequence direct REST check on 2026-06-16; Q232A reconstructed from selected source mutation label after residue-coordinate check. and applied mutation signature Q232A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13721 and applied mutation signature K355A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters for wild type rat ST6GAL1 and mutants using CMP-Neu5Ac as donor and N-acetyllactosamine as acceptor substrate (J. Biol. Chem. 2013, 288(48):34680-34698); enzyme-form row 'K355A'; donor CMP-NeuAc block: column 'Km (uM)' = 95; column 'kcat (min^-1)' = 41.6; column 'kcat/Km (mM^-1 min^-1)' = 438. The GFP fluorescence cell and the last three cells of the same printed row belong to the expression readout and to the acceptor Gal-beta-1,4-GlcNAc block.

raw_value_unit_evidence: Table 2, enzyme-form row 'K355A', donor CMP-Neu5Ac columns: Km = 95 uM; kcat = 41.6 min^-1; kcat/Km = 438 mM^-1 min^-1.

row_label: Table 2, enzyme-form row 'K355A', the three donor CMP-Neu5Ac cells (Km, kcat, kcat/Km)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13721 canonical sequence direct REST check on 2026-06-16; Y119F reconstructed from selected source mutation label after residue-coordinate check. and applied mutation signature Y119F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13721 and applied mutation signature Q354A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters for wild type rat ST6GAL1 and mutants using CMP-Neu5Ac as donor and N-acetyllactosamine as acceptor substrate (J. Biol. Chem. 2013, 288(48):34680-34698); enzyme-form row 'Q354A'; donor CMP-NeuAc block: column 'Km (uM)' = 100; column 'kcat (min^-1)' = 25.0; column 'kcat/Km (mM^-1 min^-1)' = 250. The GFP fluorescence cell and the last three cells of the same printed row belong to the expression readout and to the acceptor Gal-beta-1,4-GlcNAc block.

raw_value_unit_evidence: Table 2, enzyme-form row 'Q354A', donor CMP-Neu5Ac columns: Km = 100 uM; kcat = 25.0 min^-1; kcat/Km = 250 mM^-1 min^-1.

row_label: Table 2, enzyme-form row 'Q354A', the three donor CMP-Neu5Ac cells (Km, kcat, kcat/Km)


sequence_variant_note: Resolved canonical sequence from UniProt REST P13721 canonical sequence checked 2026-06-16 and applied mutation signature F208A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P13721 canonical sequence checked 2026-06-16 and applied mutation signature K355A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P13721 canonical sequence checked 2026-06-16 and applied mutation signature Y272A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P13721 canonical sequence checked 2026-06-16 and applied mutation signature Q354A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13721 and applied mutation signature F208A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters for wild type rat ST6GAL1 and mutants using CMP-Neu5Ac as donor and N-acetyllactosamine as acceptor substrate (J. Biol. Chem. 2013, 288(48):34680-34698); enzyme-form row 'F208A'; donor CMP-NeuAc block: column 'Km (uM)' = 400; column 'kcat (min^-1)' = 11.3; column 'kcat/Km (mM^-1 min^-1)' = 28. The GFP fluorescence cell and the last three cells of the same printed row belong to the expression readout and to the acceptor Gal-beta-1,4-GlcNAc block.

raw_value_unit_evidence: Table 2, enzyme-form row 'F208A', donor CMP-Neu5Ac columns: Km = 400 uM; kcat = 11.3 min^-1; kcat/Km = 28 mM^-1 min^-1.

row_label: Table 2, enzyme-form row 'F208A', the three donor CMP-Neu5Ac cells (Km, kcat, kcat/Km)


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from UniProt REST P13721 canonical sequence checked 2026-06-16 and applied mutation signature V220A to reconstruct the assayed variant sequence.

substrate: Unknown


enzyme_display_name: protein O-GlcNAcase

organism: Bacteroides thetaiotaomicron

sequence_source: UniProt REST Q89ZI2 canonical sequence checked 2026-06-16

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +3, so it is treated as a source-provided variant sequence.

enzyme: protein O-GlcNAcase


sequence_variant_note: Mutation signature Y282F matches the mutant residue at offset +4 and the reference residue at offset -1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


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


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: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +2, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -7, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +12, so it is treated as a source-provided variant sequence.


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.

proof_lines: D242N mutant, at a pH value of 8.5 the apparent Km is 12fold reduced (1 mM to 0.08 mM)


organism: Clostridium perfringens

sequence_variant_note: Resolved canonical sequence from UniProt REST Q0TR53 canonical sequence checked 2026-06-16 and applied mutation signature N396A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: protein O-GlcNAcase(Enzyme) mutant N396A


sequence_variant_note: Resolved canonical sequence from https://rest.uniprot.org/uniprotkb/Q0TR53 FASTA/JSON direct check, 2026-06-16 and applied mutation signature D401A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: protein O-GlcNAcase(Enzyme) mutant D401A


sequence_variant_note: Resolved canonical sequence from https://rest.uniprot.org/uniprotkb/Q0TR53 FASTA/JSON direct check, 2026-06-16 and applied mutation signature D298N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: protein O-GlcNAcase(Enzyme) mutant D298N


sequence_variant_note: Resolved canonical sequence from https://rest.uniprot.org/uniprotkb/Q0TR53 FASTA/JSON direct check, 2026-06-16 and applied mutation signature W490A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: protein O-GlcNAcase(Enzyme) mutant W490A


sequence_variant_note: Resolved canonical sequence from https://rest.uniprot.org/uniprotkb/Q0TR53 FASTA/JSON direct check, 2026-06-16 and applied mutation signature N390A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: protein O-GlcNAcase(Enzyme) mutant N390A


sequence_variant_note: Resolved canonical sequence from https://rest.uniprot.org/uniprotkb/Q0TR53 FASTA/JSON direct check, 2026-06-16 and applied mutation signature D297N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: protein O-GlcNAcase(Enzyme) mutant D297N


sequence_source: https://rest.uniprot.org/uniprotkb/Q0TR53 FASTA/JSON direct check, 2026-06-16


sequence_variant_note: Resolved canonical sequence from https://rest.uniprot.org/uniprotkb/Q0TR53 FASTA/JSON direct check, 2026-06-16 and applied mutation signature Y335F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: protein O-GlcNAcase(Enzyme) mutant Y335F


sequence_variant_note: Resolved canonical sequence from https://rest.uniprot.org/uniprotkb/Q0TR53 FASTA/JSON direct check, 2026-06-16 and applied mutation signature V331C to reconstruct the assayed variant sequence.


sequence_source: https://rest.uniprot.org/uniprotkb/O60502 FASTA/JSON direct check, 2026-06-16

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

proof_lines: full-length enzyme, pH and temperature not specified in the publication


mutation_signature: truncated enzyme OGA1-662

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

mutation_type: truncation

proof_lines: truncated enzyme OGA1-662, pH and temperature not specified in the publication


mutation_signature: truncated enzyme OGA57-400/544-705

proof_lines: truncated enzyme OGA57-400/544-705, pH and temperature not specified in the publication


mutation_signature: truncated enzyme OGA14-400

proof_lines: truncated enzyme OGA14-400, pH and temperature not specified in the publication


mutation_signature: truncated enzyme OGA14-341

proof_lines: truncated enzyme OGA14-341, pH and temperature not specified in the publication


mutation_signature: truncated enzyme OGA14-400/554-705

proof_lines: truncated enzyme OGA14-400/554-705, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt REST accession O60502; variant reconstructed from canonical residues on 2026-06-16 and applied mutation signature E602A/E605A to reconstruct the assayed variant sequence.


organism: Mus musculus

sequence_variant_note: Resolved canonical sequence from UniProt REST accession Q9EQQ9; variant reconstructed from canonical residues on 2026-06-16 and applied mutation signature D175A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST accession Q9EQQ9; variant reconstructed from canonical residues on 2026-06-16 and applied mutation signature C166S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST accession Q9EQQ9; variant reconstructed from canonical residues on 2026-06-16 and applied mutation signature D174N to reconstruct the assayed variant sequence.


sequence_source: UniProt REST accession Q9EQQ9; canonical sequence checked on 2026-06-16

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 UniProt REST accession Q9EQQ9; variant reconstructed from canonical residues on 2026-06-16 and applied mutation signature D177N to reconstruct the assayed variant sequence.


enzyme_display_name: cellulose 1,4-beta-cellobiosidase (reducing end)

organism: Acetivibrio thermocellus

substrate_name: cellopentaose

sequence_source: UniProt REST accession A3DH67; canonical sequence checked on 2026-06-16

proof_lines: pH 5.7, temperature not specified in the publication

substrate: cellopentaose


organism: Dictyostelium discoideum

substrate_name: 4-nitrophenyl beta-D-lactoside

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

proof_lines: pH 5.0, 45°C, recombinant protein carrying Hypocrea jecorina carbohydrate-binding module and linker

enzyme: cellulose 1,4-beta-cellobiosidase (reducing end)

substrate: 4-nitrophenyl beta-D-lactoside


organism: Dictyostelium purpureum


organism: Geotrichum candidum


substrate_name: 4-nitrophenyl beta-D-cellobioside

substrate: 4-nitrophenyl beta-D-cellobioside


proof_lines:
catalyticdomain, pH 5.0, 37°C
Raw SKiD Env: Temp=37°C, pH=5


organism: Limnoria quadripunctata

proof_lines:
pH 4.5, 30°C
at pH 4.5 and 30°C


organism: Melanocarpus albomyces

substrate_name: 2-chloro-4-nitrophenyl beta-D-lactoside

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

substrate: 2-chloro-4-nitrophenyl beta-D-lactoside


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


organism: Phialemonium thermophilum

assay_conditions_summary: pH 5.7; 295.15 K; buffer 50 mM sodium phosphate

proof_lines: in 50 mM sodium phosphate buffer, pH 5.7, at 22°C

proof_lines: in 50 mM sodium acetate buffer, pH 5.0, at 22°C


organism: Rasamsonia emersonii

substrate_name: 4-methylumbelliferyl beta-D-lactoside

substrate: 4-methylumbelliferyl beta-D-lactoside


proof_lines:
pH 5.0, 60°C, wild-type
pH 5.0, 45°C, wild-type
pH 5.0, 22°C, wild-type


proof_lines: pH 5.0, 22°C, fusion protein with CBM1 from Hypocrea jecorina Cel7A containing an additional S-S bridge in the catalytic module

proof_lines: pH 5.0, 45°C, fusion protein with CBM1 from Hypocrea jecorina Cel7A containing an additional S-S bridge in the catalytic module


organism: Talaromyces funiculosus

substrate_name: 4-nitrophenyl beta-D-lactopyranoside

proof_lines:
at pH 4.0 and 60°C
Raw SKiD Env: Temp=60°C, pH=4

substrate: 4-nitrophenyl beta-D-lactopyranoside


organism: Unknown


organism: Thermoascus aurantiacus

assay_conditions_summary: pH 5; 295.15 K; buffer 50 mM sodium acetate

proof_lines: pH 5.0, 50°C, presence of 1 mM mannobiose


organism: Thermochaetoides thermophila


organism: Thermothelomyces thermophilus

proof_lines: at 50°C in 50 mM sodium acetate (pH 5.0)


organism: Thermothielavioides terrestris


organism: Trichoderma harzianum

proof_lines:
pH 5.0, 50°C
Raw SKiD Env: Temp=50°C, pH=5


organism: Trichoderma reesei


proof_lines: pH 5.0, 27°C, recombinant mutant W40A enzyme catalytic domain


proof_lines: pH 5.0, 27°C, recombinant wild-type enzyme catalytic domain


substrate_name: Avicel

substrate: Avicel


substrate_name: 4-nitrophenyl lactopyranoside

proof_lines:
pH 5.0, 25°C, wild-type enzyme
25°C, pH 7, wild-type
25°C, pH 5, wild-type

substrate: 4-nitrophenyl lactopyranoside


proof_lines: pH 5.0, 25°C, substrate: 4-nitrophenyl lactopyranoside, mutant enzyme R251A


proof_lines: pH 5.0, 25°C, substrate: 4-nitrophenyl lactopyranoside, mutant enzyme R394A


proof_lines:
Raw SKiD Env: Temp=25°C, pH=7
Raw SKiD Env: Temp=25°C, pH=5


substrate_name: CoASH

substrate: CoASH


substrate_name: xanthine

substrate: xanthine


organism: Canis lupus familiaris

substrate_name: glyoxylate

proof_lines: pH 8.2, 37°C, isoenzyme 1, alanine as amino donor

proof_lines: pH 8.2, 37°C, isoenzyme 1, glyoxylate as amino acceptor

substrate: glyoxylate


organism: Felis catus


organism: Mus musculus

substrate_name: L-alanine

proof_lines: pH 8.2, 37°C, isoenzyme 2, glyoxylate as amino acceptor

substrate: L-alanine


organism: Rattus norvegicus

proof_lines: pH 8.0, 37°C, pyruvate as amino acceptor


organism: Saccharomyces cerevisiae

proof_lines: pH 8.2, 37°C, glyoxylate as amino acceptor

proof_lines: pH 8.2, 37°C, isoenzyme 2, alanine as amino donor


organism: Suncus murinus

proof_lines: GPT 1, alanine:2-oxoglutarate aminotransferase AGT activity


substrate_name: UMP

substrate: UMP


organism: Homo sapiens

substrate_name: Cidofovir monophosphate; ATP

assay_conditions_summary: 298.15 K; cofactor ATP

proof_lines:
isozyme B6, 25°C
cosubstrate ADP
isozyme A6, 25°C

substrate: Cidofovir monophosphate; ATP


organism: Oryza sativa

substrate_name: GTP

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ADP

proof_lines: isozyme NDPK2, in 4 mM Tris-HCl, pH 7.5, 100 mM KCl, 25 mM MgCl2, at 25°C

proof_lines: isozyme NDPK3, in 4 mM Tris-HCl, pH 7.5, 100 mM KCl, 25 mM MgCl2, at 25°C

proof_lines: isozyme NDPK1, in 4 mM Tris-HCl, pH 7.5, 100 mM KCl, 25 mM MgCl2, at 25°C

substrate: GTP


substrate_name: acetyl-CoA

source_db: uniprot

assay_conditions_summary: cofactor CoA

substrate: acetyl-CoA

source: uniprot


organism: Caenorhabditis elegans

substrate_name: beta-xylose nitrophenyl (at 17 degrees Celsius)


organism: Bacillus subtilis (strain 168)


organism: Enterococcus faecalis (strain ATCC 700802 / V583)


substrate_name: CMP-NeuAc

substrate: CMP-NeuAc


organism: Arabidopsis thaliana

substrate_name: glutamate

substrate: glutamate


substrate_name: L-alanine (with the His-AGXT construct)

substrate: L-alanine (with the His-AGXT construct)


substrate_name: D-beta-aminoisobutyrate

substrate: D-beta-aminoisobutyrate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Bos taurus

substrate_name: ATP

substrate: ATP


organism: Gallus gallus


substrate_name: IDP

substrate: IDP


substrate_name: AMP with ATP as phosphate donor

substrate: AMP with ATP as phosphate donor


substrate_name: AMP

substrate: AMP


substrate_name: AMP (with ATP as phosphate donor)

substrate: AMP (with ATP as phosphate donor)


substrate_name: CMP

substrate: CMP


substrate_name: ADP

substrate: ADP


enzyme_display_name: coagulation factor VIIa

substrate_name: H-D-Ile-Pro-Arg-p-nitroanilide; H2O

proof_lines: SABIO-RK modifier species: coagulation factor VIIa(Enzyme) mutant C164V/V299C-FVIIa

enzyme: coagulation factor VIIa

substrate: H-D-Ile-Pro-Arg-p-nitroanilide; H2O


substrate_name: H2O; H-D-Ile-Pro-Arg-p-nitroanilide

proof_lines: presence of 200 mM NaCl, pH 7.4, temperature not specified in the publication

proof_lines: presence of 5 mM Ca2+, pH 7.4, temperature not specified in the publication

substrate: H2O; H-D-Ile-Pro-Arg-p-nitroanilide


proof_lines: SABIO-RK modifier species: coagulation factor VIIa(Enzyme) mutant L280I/V299M-FVIIa


proof_lines: SABIO-RK modifier species: coagulation factor VIIa(Enzyme) mutant V299M-FVIIa


substrate_name: Unknown

proof_lines: mutant G372 + soluble tissue factor for induced allosteric activation of factor VIIa

substrate: Unknown


substrate_name: Factor X

proof_lines: mutant G372A + lipidated tissue factor for induced allosteric activation of factor VIIa, pH 7.4

proof_lines: mutant G372A + soluble tissue factor for induced allosteric activation of factor VIIa, pH 7.4

substrate: Factor X


sequence_source: UniProtKB:P08709 direct REST lookup 2026-06-16


proof_lines: wild type enzyme, in the absence of soluble tissue factor (1-219), at pH 7.4 and 25°C

proof_lines: wild-type FVIIa + lipidated tissue factor for induced allosteric activation of factor VIIa, pH 7.4

proof_lines: wild type enzyme, in the presence of soluble tissue factor (1-219), at pH 7.4 and 25°C


enzyme_display_name: coagulation factor XIa

enzyme: coagulation factor XIa


sequence_source: UniProtKB:P03951 direct REST lookup 2026-06-16

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


enzyme_display_name: dihydropyrimidinase

organism: Geobacillus stearothermophilus

substrate_name: DL-p-hydroxyphenylhydantoin

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q45515 canonical sequence with row-specific mutation reconstruction (M63H/F159N) and applied mutation signature M63H/F159N to reconstruct the assayed variant sequence.

enzyme: dihydropyrimidinase

substrate: DL-p-hydroxyphenylhydantoin


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14117 canonical sequence with row-specific mutation reconstruction (T418I) and applied mutation signature T418I to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme T418I


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14117 canonical sequence with row-specific mutation reconstruction (R118Q) and applied mutation signature R118Q to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme R118Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14117 canonical sequence with row-specific mutation reconstruction (H365Y) and applied mutation signature H365Y to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme H365Y


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14117 canonical sequence with row-specific mutation reconstruction (T513A) and applied mutation signature T513A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme T513A


sequence_source: UniProtKB:Q14117 canonical accession sequence from direct lookup

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14117 canonical sequence with row-specific mutation reconstruction (Y448H) and applied mutation signature Y448H to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme Y448H


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14117 canonical sequence with row-specific mutation reconstruction (G410S) and applied mutation signature G410S to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme G410S


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14117 canonical sequence with row-specific mutation reconstruction (H295R) and applied mutation signature H295R to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme H295R


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q14117 canonical sequence with row-specific mutation reconstruction (A189V) and applied mutation signature A189V to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme A189V


organism: Jannaschia sp. CCS1

sequence_source: UniProtKB:Q28SA7 direct lookup returned Inactive/deleted; no live replacement accession was present in the selected evidence.


organism: Lachancea kluyveri

sequence_source: UniProtKB:Q9P903 canonical sequence found, but selected source notes a C-terminal Strep-Tag construct.

proof_lines: pH 7.0, 25°C, dihydropyrimidinase with a C-terminal Strep-Tag


organism: Pseudomonas aeruginosa

substrate_name: 5,6-Dihydrouracil; H2O

sequence_source: UniProtKB:Q9I676 canonical accession sequence from direct lookup

substrate: 5,6-Dihydrouracil; H2O


organism: Pseudomonas fluorescens

substrate_name: isobutylhydantoin

sequence_source: UniProtKB:S5MPT0 canonical accession sequence from direct lookup

substrate: isobutylhydantoin


substrate_name: indolmethylhydantoin

substrate: indolmethylhydantoin


substrate_name: isopropylhydantoin

substrate: isopropylhydantoin


sequence_source: UniProtKB REST direct lookup for S5MPT0 on 2026-06-16


substrate_name: phenylmethylhydantoin

substrate: phenylmethylhydantoin


organism: Rattus norvegicus

substrate_name: H2O; 5,6-Dihydrouracil

sequence_source: UniProtKB REST direct lookup for Q63150 on 2026-06-16

substrate: H2O; 5,6-Dihydrouracil


organism: Saccharomyces kluyveri

sequence_source: UniProtKB REST direct lookup for Q9P903 on 2026-06-16


organism: Aspergillus niger

substrate_name: CoASH

proof_lines:
mitochondrial enzyme
cytosolic enzyme

substrate: CoASH


substrate_name: O-acetyl-L-carnitine

proof_lines:
heart enzyme
sperm enzyme

substrate: O-acetyl-L-carnitine


organism: Camelus dromedarius

substrate_name: butyryl-CoA

substrate: butyryl-CoA


organism: Candida albicans

substrate_name: acetyl-CoA

proof_lines:
mitochondrial enzyme
peroxisomal enzyme

substrate: acetyl-CoA


organism: Candida tropicalis

substrate_name: propionyl-CoA

proof_lines: peroxisomal enzyme, second substrate propionyl-CoA

substrate: propionyl-CoA


organism: Cavia porcellus

substrate_name: L-carnitine

substrate: L-carnitine


organism: Columba livia

substrate_name: carnitine

substrate: carnitine


organism: Columba sp.


organism: Homo sapiens

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines:
cosubstrate propionyl-CoA
peroxisomal enzyme, at pH 7.4 and 37°C
cosubstrate hexanoyl-CoA


organism: Mus musculus

substrate_name: hexanoyl-CoA

proof_lines:
cosubstrate butanoyl-CoA
cosubstrate decanoyl-CoA
cosubstrate hexanoyl-CoA

substrate: hexanoyl-CoA


organism: Oryctolagus cuniculus

substrate_name: choline

proof_lines:
brain enzyme
heart enzyme

substrate: choline


proof_lines: above, mutant enzyme A106M/T465V/T467N/R518N


proof_lines: presence of 25 microM of inhibitor 3_4_21-27_2-1, pH 7.4, 37°C

proof_lines: presence of 100 microM of inhibitor 3_4_21-27_2-1, pH 7.4, 37°C


enzyme_display_name: cathepsin H

organism: Capra hircus

substrate_name: Unknown

proof_lines: pH 6.0, 37°C, 1 mM, 25.40% activity remaining

enzyme: cathepsin H

substrate: Unknown


organism: Sus scrofa


organism: Bacillus sp. (in: firmicutes)

substrate_name: dihydrouracil

substrate: dihydrouracil


organism: Geobacillus stearothermophilus

substrate_name: DL-p-hydroxyphenylhydantoin

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q45515 FASTA direct lookup plus reconstructed substitutions M63I/F159S and applied mutation signature M63I/F159S to reconstruct the assayed variant sequence.

substrate: DL-p-hydroxyphenylhydantoin


substrate_name: hydantoin

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q45515 FASTA direct lookup plus reconstructed substitutions M63H/F159N and applied mutation signature M63H/F159N to reconstruct the assayed variant sequence.

substrate: hydantoin


sequence_source: UniProtKB:Q45515 FASTA direct lookup 2026-06-16


sequence_source: UniProtKB:Q45515 FASTA direct lookup plus reconstructed substitutions M63H/F159N


sequence_source: UniProtKB:Q45515 FASTA direct lookup plus reconstructed substitutions M63I/F159S


substrate_name: 3',5'-Cyclic AMP

sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed D811A variant during review. and applied mutation signature D811A to reconstruct the assayed variant sequence.

substrate: 3',5'-Cyclic AMP


substrate_name: 3',5'-Cyclic AMP; H2O

sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed D812A variant during review. and applied mutation signature D812A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant D812A

substrate: 3',5'-Cyclic AMP; H2O


sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed T810A variant during review. and applied mutation signature T810A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant T810A


sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed H796A variant during review. and applied mutation signature H796A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed S804A variant during review. and applied mutation signature S804A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant S804A


sequence_source: UniProt Q14432 canonical sequence version 3; reconstructed S804A variant during review.


sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed H798A variant during review. and applied mutation signature H798A to reconstruct the assayed variant sequence.


sequence_source: UniProt Q14432 canonical sequence version 3; reconstructed D811A variant during review.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant D811A


sequence_source: UniProt Q14432 canonical sequence version 3, direct REST/FASTA check during review.

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 UniProt Q14432 canonical sequence version 3; reconstructed H782A variant during review. and applied mutation signature H782A to reconstruct the assayed variant sequence.


substrate_name: H2O; 3',5'-Cyclic AMP

sequence_source: UniProt Q14432 canonical sequence version 3; reconstructed H782A variant during review.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant H782A

substrate: H2O; 3',5'-Cyclic AMP


sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed C816S variant during review. and applied mutation signature C816S to reconstruct the assayed variant sequence.


sequence_source: UniProt Q14432 canonical sequence version 3; reconstructed T810A variant during review.


sequence_variant_note: Resolved canonical sequence from UniProt Q14432 canonical sequence version 3; reconstructed Y807A variant during review. and applied mutation signature Y807A to reconstruct the assayed variant sequence.


sequence_source: UniProt Q14432 canonical sequence version 3; reconstructed Y807A variant during review.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant Y807A


enzyme_display_name: ubiquitinyl hydrolase 1

substrate_name: ubiquitin 7-amido-4-methylcoumarin

sequence_source: UniProt Q9Y5K5 sequence, direct UniProt REST lookup on 2026-06-16

enzyme: ubiquitinyl hydrolase 1

substrate: ubiquitin 7-amido-4-methylcoumarin


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 Reconstructed from UniProt P15374 canonical sequence, direct UniProt REST lookup on 2026-06-16 and applied mutation signature Q89A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt P09936 canonical sequence, direct UniProt REST lookup on 2026-06-16 and applied mutation signature Q84A to reconstruct the assayed variant sequence.


sequence_source: UniProt P09936 sequence, direct UniProt REST lookup on 2026-06-16

proof_lines: recombinant wild-type isozyme L1, pH 7.8, room temperature


substrate_name: Ubiquitin-AMC; H2O

sequence_source: UniProt Q6R6M4 sequence, direct UniProt REST lookup on 2026-06-16

substrate: Ubiquitin-AMC; H2O


substrate_name: H2O; Ubiquitin-AMC

sequence_source: UniProt Q93009 sequence, direct UniProt REST lookup on 2026-06-16

substrate: H2O; Ubiquitin-AMC


sequence_source: UniProt Q96RU2 sequence, direct UniProt REST lookup on 2026-06-16


substrate_name: Arg-Leu-Arg-Gly-Gly-AMC; H2O

sequence_source: UniProt Q96AP4 sequence, direct UniProt REST lookup on 2026-06-16

substrate: Arg-Leu-Arg-Gly-Gly-AMC; H2O


organism: Middle East respiratory syndrome-related coronavirus

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: SABIO-RK modifier species: ubiquitinyl hydrolase 1(Enzyme) mutant PLpro-deltaUbl2-domain (aa 1545-1801)


substrate_name: H2O; Ubiquitin-AFC

substrate: H2O; Ubiquitin-AFC


sequence_source: UniProt Q9R0P9 sequence, direct UniProt REST lookup on 2026-06-16


organism: Porcine epidemic diarrhea virus

substrate_name: Ubiquitin-AFC; H2O

substrate: Ubiquitin-AFC; H2O


organism: porcine epidemic diarrhea virus

substrate_name: Dabcyl-FKKKGGGDVKE-Edans

substrate: Dabcyl-FKKKGGGDVKE-Edans


organism: Rattus norvegicus

substrate_name: 3',5'-Cyclic AMP; H2O; 3',5'-Cyclic AMP; H2O; AMP


substrate_name: H2O; 3',5'-Cyclic AMP; H2O; 3',5'-Cyclic AMP; AMP


sequence_source: UniProtKB:Q01062 direct REST lookup on 2026-06-16

substrate: 3',5'-Cyclic AMP; H2O; 3',5'-Cyclic AMP; H2O; AMP


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:P22434 direct REST lookup on 2026-06-16


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

proof_lines:
pH 7.5, 22°C
pH 7.5, 22°C, presence of 10 mM MgCl2
pH 7.5, 22°C, presence of 10 mM MnCl2


organism: Thermotoga maritima

substrate_name: 5'-pApG; 5'-pApA

sequence_source: UniProtKB:Q9X1T1 direct REST lookup on 2026-06-16

proof_lines:
pH 8.5, 23°C
Raw SKiD Env: Temp=23°C, pH=8.5

substrate: 5'-pApG; 5'-pApA


organism: Thermus thermophilus


substrate_name: 3',5'-Cyclic GMP

substrate: 3',5'-Cyclic GMP


substrate_name: H2O; 3',5'-Cyclic AMP; H2O; 3',5'-Cyclic AMP; AMP; H2O; 3',5'-Cyclic GMP; 3',5'-Cyclic GMP; GMP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P09936 direct REST lookup on 2026-06-16 plus selected mutation signature and applied mutation signature S18Y to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant S18Y isozyme L1, pH 7.8, room temperature


sequence_variant_note: Resolved canonical sequence from UniProtKB:P09936 direct REST lookup on 2026-06-16 plus selected mutation signature and applied mutation signature I93M to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant I93M isozyme L1, pH 7.8, room temperature


substrate_name: H2O; Ubiquitin fused C-terminal to tryptophan; H2O; Ubiquitin fused C-terminal to tryptophan; Ubiquitin; Tryptophan; Ubiquitin fused C-terminal to tryptophan; H2O; H2O; Ubiquitin fused C-terminal to alanine-tryptophan; Ubiquitin fused C-terminal to alanine-tryptophan; Ala-Trp; H2O; Ubiquitin fused C-terminal to tryptophan-alanine; Ubiquitin fused C-terminal to tryptophan-alanine; Trp-Ala


substrate_name: Ubiquitin fused C-terminal to tryptophan; H2O; Ubiquitin fused C-terminal to tryptophan; H2O; Tryptophan; Ubiquitin; H2O; Ubiquitin fused C-terminal to tryptophan; H2O; Ubiquitin fused C-terminal to alanine-tryptophan; Ubiquitin fused C-terminal to alanine-tryptophan; Ala-Trp; Ubiquitin fused C-terminal to tryptophan-alanine; H2O; Ubiquitin fused C-terminal to tryptophan-alanine; Trp-Ala

sequence_source: UniProtKB:P09936 direct REST lookup on 2026-06-16


sequence_source: UniProtKB:P15374 direct REST lookup on 2026-06-16


enzyme_display_name: pyridoxal kinase

organism: Bacillus subtilis

substrate_name: Pyridoxal

sequence_source: UniProtKB reviewed accession P39610 / PDXK_BACSU, REST check 2026-06-16

enzyme: pyridoxal kinase

substrate: Pyridoxal


substrate_name: ATP; Pyridoxal

substrate: ATP; Pyridoxal


organism: Bombyx mori

substrate_name: pyridoxal

sequence_source: UniProtKB reviewed accession Q1PCB1 / PDXK_BOMMO, REST check 2026-06-16

substrate: pyridoxal


substrate_name: ATP

assay_conditions_summary: pH 5.5; 310.15 K; cofactor ATP

substrate: ATP


proof_lines: in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C


organism: Dictyostelium discoideum

sequence_source: UniProtKB reviewed accession Q55EK9 / PDXK_DICDI, REST check 2026-06-16


organism: Homo sapiens

sequence_source: UniProtKB reviewed accession O00764 / PDXK_HUMAN, REST check 2026-06-16


proof_lines: SABIO-RK modifier species: pyridoxal kinase(Enzyme) mutant D235A


proof_lines: SABIO-RK modifier species: pyridoxal kinase(Enzyme) mutant D235N


assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP


substrate_name: 3',5'-Cyclic AMP

sequence_variant_note: Resolved canonical sequence from UniProtKB Q14432 canonical sequence with selected-batch mutation D812A applied after residue check and applied mutation signature D812A to reconstruct the assayed variant sequence.

substrate: 3',5'-Cyclic AMP


sequence_variant_note: Resolved canonical sequence from UniProtKB Q14432 canonical sequence with selected-batch mutation G815A applied after residue check and applied mutation signature G815A to reconstruct the assayed variant sequence.


substrate_name: 3',5'-Cyclic AMP; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB Q14432 canonical sequence with selected-batch mutation Y807C applied after residue check and applied mutation signature Y807C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant Y807C

substrate: 3',5'-Cyclic AMP; H2O


substrate_name: H2O; 3',5'-Cyclic AMP

sequence_variant_note: Resolved canonical sequence from UniProtKB Q14432 canonical sequence with selected-batch mutation C816S applied after residue check and applied mutation signature C816S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant C816S

substrate: H2O; 3',5'-Cyclic AMP


sequence_source: UniProtKB Q14432 canonical sequence with selected-batch mutation G815A applied after residue check

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant G815A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q14432 canonical sequence with selected-batch mutation K805A applied after residue check and applied mutation signature K805A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q14432 canonical sequence with selected-batch mutation H798A applied after residue check and applied mutation signature H798A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant H798A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q14432 canonical sequence with selected-batch mutation Y814A applied after residue check and applied mutation signature Y814A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q14432 canonical sequence with selected-batch mutation Y807C applied after residue check


sequence_source: UniProtKB Q9Y233 canonical sequence context only; selected row describes a tagged/truncated construct

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) wildtype PDE10A2 truncated (aa 449-789), His-tagged


sequence_source: UniProtKB Q9Y233 canonical sequence from direct REST lookup on 2026-06-16

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


organism: Mus musculus

sequence_source: UniProtKB Q8CA95 canonical sequence from direct REST lookup on 2026-06-16


sequence_source: UniProtKB Q9Z0X4 canonical sequence context only; selected row describes a tagged/truncated construct

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant N-term truncation (del346), HA-tagged (C-term)


sequence_source: UniProtKB Q9Z0X4 canonical sequence from direct REST lookup on 2026-06-16


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB P9WP65 canonical sequence from direct REST lookup on 2026-06-16

proof_lines: pH and temperature not specified in the publication


sequence_source: UniProtKB Q9QYJ6 canonical sequence from direct REST lookup on 2026-06-16


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: pyridoxamine

sequence_source: UniProt REST accession A0A0F7J8S0; checked 2026-06-16

substrate: pyridoxamine


organism: Staphylococcus aureus

sequence_variant_note: Resolved canonical sequence from UniProt REST accession A0A0H3JTP0; checked 2026-06-16 and applied mutation signature C214D to reconstruct the assayed variant sequence.

proof_lines: mutant C214D, pH not specified in the publication, temperature not specified in the publication


substrate_name: pyridoxine

sequence_source: UniProt REST accession A0A0H3JTP0; checked 2026-06-16

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

substrate: pyridoxine


sequence_variant_note: Resolved canonical sequence from UniProt REST accession A0A0H3JTP0; checked 2026-06-16 and applied mutation signature C110A to reconstruct the assayed variant sequence.

proof_lines: mutant C110A, pH not specified in the publication, temperature not specified in the publication


organism: Trypanosoma cruzi

sequence_source: UniProt REST accession Q4D946; checked 2026-06-16

proof_lines: in the presence of K+, at pH 7.0 and 30°C


organism: Arthrobacter sp.

sequence_source: UniProt REST accession M9W6G9; checked 2026-06-16


organism: Bos taurus


organism: Helicobacter pylori

sequence_source: UniProt REST accession O25683; checked 2026-06-16


substrate_name: Bis-4-nitrophenyl phosphate; H2O

substrate: Bis-4-nitrophenyl phosphate; H2O


substrate_name: Bis-4-nitrophenyl phosphate

substrate: Bis-4-nitrophenyl phosphate


sequence_source: UniProt REST accession Q9Y233; checked 2026-06-16


substrate_name: cAMP

substrate: cAMP


sequence_variant_note: Resolved canonical sequence from UniProt REST accession Q14432; checked 2026-06-16 and applied mutation signature K805A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant K805A


sequence_variant_note: Resolved canonical sequence from UniProt REST accession Q14432; checked 2026-06-16 and applied mutation signature Y814A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant Y814A


sequence_variant_note: Resolved canonical sequence from UniProt REST accession Q14432; checked 2026-06-16 and applied mutation signature H796A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-nucleotide phosphodiesterase(Enzyme) mutant H796A


sequence_variant_note: Resolved canonical sequence from UniProtKB O00764 FASTA; reconstructed variant sequence from selected mutation signature and applied mutation signature D87H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O00764 FASTA; reconstructed H246Q sequence from selected mutation signature and applied mutation signature H246Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB O00764 FASTA direct check

proof_lines: pH 7.3, 37°C recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB O00764 FASTA; reconstructed variant sequence from selected mutation signature and applied mutation signature H246Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB O00764 FASTA; reconstructed variant sequence from selected mutation signature


sequence_variant_note: Resolved canonical sequence from UniProtKB O00764 FASTA; reconstructed A243G sequence from selected mutation signature and applied mutation signature A243G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O00764 FASTA; reconstructed V128I sequence from selected mutation signature and applied mutation signature V128I to reconstruct the assayed variant sequence.


substrate_name: ATP; Pyridoxine

assay_conditions_summary: pH 6.2; 310.15 K; buffer 70 mM potassium phosphate; cofactor ATP

proof_lines: in 70 mM potassium phosphate buffer, pH 6.2

substrate: ATP; Pyridoxine


organism: Leishmania donovani

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

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP


proof_lines: recombinant wild-type enzyme, pH 7.2, 37°C


substrate_name: ginkgotoxin

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

substrate: ginkgotoxin


organism: Plasmodium vivax

sequence_source: UniProtKB A5K1Z8 FASTA direct check

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


sequence_source: UniProtKB A0A0F7J8S0 FASTA direct check

assay_conditions_summary: pH 6.6; 310.15 K; cofactor ATP

proof_lines:
with pyridoxal, pH 6.6, 37°C
pH 6.6, 37°C
with pyridoxamine, pH 8.5, 37°C


organism: porcine epidemic diarrhea virus

substrate_name: Dabcyl-FRLKGGAPIKGV-Edans

sequence_source: UniProtKB:A0A075ECV2 canonical sequence with D195-N196 deletion reconstructed from UniProt PDB 7F0U chain A/B=1686-1922 mapping

sequence_variant_note: Mutation signature N196del could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: Dabcyl-FRLKGGAPIKGV-Edans


substrate_name: Dabcyl-FKKKGGGDVKE-Edans

sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A075ECV2 canonical sequence with N138A reconstructed from UniProt PDB 7F0U chain A/B=1686-1922 mapping and applied mutation signature N138A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

substrate: Dabcyl-FKKKGGGDVKE-Edans


sequence_source: UniProtKB:A0A075ECV2 canonical sequence retrieved by direct accession lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A075ECV2 canonical sequence with E99A reconstructed from UniProt PDB 7F0U chain A/B=1686-1922 mapping and applied mutation signature E99A to reconstruct the assayed variant sequence.


organism: SARS coronavirus

substrate_name: Ubiquitin-AMC; H2O

substrate: Ubiquitin-AMC; H2O


organism: Schizosaccharomyces pombe

substrate_name: H2O; Arg-Leu-Arg-Gly-Gly-AMC

sequence_source: UniProtKB:O13979 canonical reviewed sequence

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

substrate: H2O; Arg-Leu-Arg-Gly-Gly-AMC


substrate_name: 3',5'-cyclic AMP

substrate: 3',5'-cyclic AMP


substrate_name: 3',5'-cyclic AMP (isoform 1)

substrate: 3',5'-cyclic AMP (isoform 1)


organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)


organism: Rattus norvegicus


substrate_name: 3',5'-cyclic AMP (at pH 7.5)

substrate: 3',5'-cyclic AMP (at pH 7.5)


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

substrate_name: p-nitrophenyl-O-GlcNAc (pNP-O-GlcNAc) (at pH 7.4)


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


organism: Homo sapiens

substrate_name: pNP-GlcNAc

substrate: pNP-GlcNAc


organism: Mus musculus


organism: Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516)

substrate_name: p-nitrophenyl-GlcNAc

substrate: p-nitrophenyl-GlcNAc


substrate_name: pNP-O-GlcNAc

substrate: pNP-O-GlcNAc


organism: Crimean-Congo hemorrhagic fever virus (strain Nigeria/IbAr10200/1970)

substrate_name: Ub-AMC

substrate: Ub-AMC


substrate_name: cGMP

proof_lines:
stimulation with Mg2+ or Mn2+
two forms of phosphodiesterase
30 C, pH 8.0, PDE3A

substrate: cGMP


substrate_name: wild-type di-ubiquitin

proof_lines:
pH 8.0, 37 C
pH 8.0, 37 C, isozyme L2
pH 8.0, 37 C, isozyme H2

substrate: wild-type di-ubiquitin


proof_lines: below, pH 7.5, 25 C, inhibition kinectis


sequence_source: UniProtKB:Q9R0P9 direct accession check; UniProt references PMID 12913066

proof_lines: recombinant wild-type isozyme L1, pH 7.5, 25 C

proof_lines: pH 7.5, 25 C, recombinant wild-type isozyme L1


organism: Arabidopsis thaliana

substrate_name: ATP

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

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Bacillus subtilis (strain 168)

substrate_name: HMP

substrate: HMP


organism: Dictyostelium discoideum

substrate_name: pyridoxal (at 37 degrees Celsius)

substrate: pyridoxal (at 37 degrees Celsius)


organism: Spinacia oleracea

substrate_name: GDP

assay_conditions_summary: cofactor ADP

substrate: GDP


organism: Sus scrofa

substrate_name: ThDP

substrate: ThDP


organism: Bos taurus

substrate_name: Unknown

substrate: Unknown


organism: Drosophila melanogaster

substrate_name: 3',5'-cyclic GMP

substrate: 3',5'-cyclic GMP


substrate_name: cAMP

substrate: cAMP


substrate_name: 3',5'-cyclic AMP

substrate: 3',5'-cyclic AMP


organism: Dugbe virus (isolate ArD44313)


substrate_name: ubiquitin vinyl sulfone (in presence of WDR48)


substrate_name: ubiquitin-rhodamine

substrate: ubiquitin-rhodamine


organism: Turnip yellow mosaic virus


organism: Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543 / NRRL Y-12651)

substrate_name: dihydrouracil

substrate: dihydrouracil


organism: Escherichia coli (strain K12)

substrate_name: guanine (at pH 8.5)

proof_lines: kcat is 112.0 sec(-1) with guanine as substrate. kcat is 150.1 sec(-1) with xanthine as substrate. kcat is 54.8 sec(-1) with hypoxanthine as substrate (at pH 8.5).

substrate: guanine (at pH 8.5)


organism: Rattus norvegicus

proof_lines: kcat is 35.6 min(-1) for the donor CMP-Neu5Ac (at pH 6.5 and 37 degrees Celsius). kcat is 40.3 min(-1) for the acceptor beta-Gal1,4-GlcNAc (at pH 6.5 and 37 degrees Celsius).


organism: Aedes aegypti

substrate_name: 3-hydroxykynurenine (at 50 degrees Celsius and pH 7.0)

assay_conditions_summary: pH 7

proof_lines: kcat is 2424 min(-1) for 3-hydroxykynurenine (at 50 degrees Celsius and pH 7) (PubMed:11880382). kcat is 1640 min(-1) for L-alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate) (PubMed:11880382). kcat is 1200 min(-1) f


proof_lines: kcat is 117 sec(-1) for alanine (at 45 degrees Celsius, pH 7.5 and with glyoxylate as cosubstrate).


organism: Anopheles gambiae

proof_lines: kcat is 988.5 min(-1) for D,L-3-hydroxykynurenine (at 50 degrees Celsius, pH 7 and with glyoxylate as cosubstrate) (PubMed:16262702). kcat is 1077.2 min(-1) for D,L-kynurenine (at 50 degrees Celsius, pH 7 and with glyoxylate as cosubstrate)


substrate_name: alanine (with recombinant enzyme, in the presence of 20 mM glyoxylate)

proof_lines: kcat is 6.4 sec(-1) for L-serine. kcat is 2.86 sec(-1) for L-alanine.


proof_lines: kcat is 6800 min(-1) for glyoxylate (at 50 degrees Celsius, pH 7 and with alanine as cosubstrate) (PubMed:12220660). kcat is 7880 min(-1) for alanine (at 50 degrees Celsius, pH 7 and with glyoxylate as cosubstrate) (PubMed:12220660).


organism: Bombyx mori

substrate_name: ATP (in the presence of 0.5 mM ZnCl(2), at pH 5.5 and 37 degrees Celsius)

assay_conditions_summary: pH 5.5; cofactor ATP

proof_lines: kcat is 1.23 sec(-1) for ATP. kcat is 1.35 sec(-1) for PL.


substrate_name: pyridoxal (in the presence of MgATP, at pH 7.3 and 37 degrees Celsius)

proof_lines: kcat is 140 min(-1) for the phosphorylation of PL with MgATP. kcat is 120 min(-1) for the phosphorylation of PL with ZnATP. kcat is 20 min(-1) for the phosphorylation of PN with MgATP. kcat is 40 min(-1) for the phosphorylation of PM with M


organism: Homo sapiens

substrate_name: pyridoxal (in the presence of K(+))

proof_lines: KM is <10 uM for pyridoxal (in the presence of K(+)) (PubMed:17766369). KM is <25 uM for MgATP (in the presence of K(+)) (PubMed:17766369). kcat is 200 min(-1) for phosphorylase activity using PL as substrate in the presence of Na(+). kcat

substrate: pyridoxal (in the presence of K(+))


organism: Acanthamoeba polyphaga mimivirus

substrate_name: dGDP

proof_lines: KM values are below 10 uM for dCDP, dCTP and dUTP.

substrate: dGDP


organism: Schistosoma mansoni

substrate_name: GDP (at pH 7.6)

proof_lines: kcat is 0.68 sec(-1) with GDP as substrate.

substrate: GDP (at pH 7.6)


proof_lines: kcat is 10 min(-1) for cleavage after 'Arg-191' in F9 (in the presence of 5 mM CaCl(2), from initial velocities). kcat is 7.1 min(-1) for cleavage after 'Arg-226' in F9 cleaved at 'Arg-191' (in the presence of 5 mM CaCl(2), from initial vel


enzyme_display_name: ADP-specific glucose/glucosamine kinase

organism: Methanohalobium evestigatum

substrate_name: ADP

sequence_source: UniProtKB REST exact accession lookup: D7E8P3

assay_conditions_summary: pH 7.8; 313.15 K; cofactor ADP

enzyme: ADP-specific glucose/glucosamine kinase

substrate: ADP


proof_lines:
MgADP, pH 7.8, 40°C
pH 7.8, 40°C


organism: Methanosarcina mazei

substrate_name: D-glucose

sequence_source: UniProtKB REST exact accession lookup: Q8PZL9

substrate: D-glucose


proof_lines:
pH 7.8, 40°C
MgADP, pH 7.8, 40°C


organism: Mus musculus

substrate_name: D-Glucose; ADP

sequence_source: UniProtKB REST exact accession lookup: Q8VDL4

assay_conditions_summary: pH 7; 310.15 K; cofactor ADP

proof_lines: at 0.8 mM and an ADP:Mg2+ ratio of 1:1, pH 7.0, 37°C

substrate: D-Glucose; ADP


organism: Pyrococcus furiosus

substrate_name: ADP; D-Glucose

sequence_source: UniProtKB REST exact accession lookup: Q9V2Z6

proof_lines:
versus ADP
Raw SKiD Env: Temp=40°C, pH=7.8

substrate: ADP; D-Glucose


organism: Pyrococcus horikoshii

sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession lookup: O58328 and applied mutation signature F272A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: ADP-specific glucokinase(Enzyme) mutant F272A N-terminal His6-tag


sequence_source: UniProtKB REST exact accession lookup: O58328

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ADP

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


organism: Thermococcus kodakarensis

substrate_name: D-glucosamine

sequence_source: UniProtKB REST exact accession lookup: Q5JE39

assay_conditions_summary: pH 7.5; 343.15 K; cofactor ADP

substrate: D-glucosamine


assay_conditions_summary: pH 7.5; 353.15 K; cofactor ADP


substrate_name: D-Glucosamine

substrate: D-Glucosamine


organism: Thermococcus litoralis

sequence_source: UniProtKB REST exact accession lookup: Q7M537


sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession lookup: Q7M537 and applied mutation signature E279D to reconstruct the assayed variant sequence.


organism: Caldanaerobacter subterraneus subsp. tengcongensis

assay_conditions_summary: pH 8; 348.15 K; cofactor ADP


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 REST direct accession lookup Q9BRR6, accessed 2026-06-16


organism: Methanocaldococcus jannaschii

sequence_source: UniProtKB REST direct accession lookup Q58999, accessed 2026-06-16


organism: Methanococcoides burtonii

sequence_source: UniProtKB REST direct accession lookup Q12WB9, accessed 2026-06-16

assay_conditions_summary: pH 7.8; 298.15 K; cofactor ADP


organism: Methanococcus maripaludis

sequence_source: UniProtKB REST direct accession lookup Q6LXQ3, accessed 2026-06-16

assay_conditions_summary: pH 6.5; 303.15 K; cofactor ADP

proof_lines: pH 6.5, 30°C, phosphopfructokinase activity

proof_lines: pH 7.8, 30°C, reverse glucokinase reaction


substrate_name: D-Fructose 6-phosphate

substrate: D-Fructose 6-phosphate


assay_conditions_summary: pH 7; 303.15 K; cofactor ADP


substrate_name: D-glucose 6-phosphate

substrate: D-glucose 6-phosphate


sequence_source: UniProtKB REST direct accession lookup D7E8P3, accessed 2026-06-16


enzyme_display_name: non-specific protein-tyrosine kinase

substrate_name: ATP

enzyme: non-specific protein-tyrosine kinase

substrate: ATP


substrate_name: phosphoenolpyruvate (at 32 degrees Celsius, pH 8.0)

assay_conditions_summary: pH 8; cofactor ADP


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


substrate_name: D-glucose (at 37 degrees Celsius)

substrate: D-glucose (at 37 degrees Celsius)


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


organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

substrate_name: glucose

substrate: glucose


organism: Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)


organism: Rattus norvegicus

substrate_name: carnitine

substrate: carnitine


substrate_name: choline

substrate: choline


substrate_name: palmitoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: palmitoyl-CoA


substrate_name: CoASH

proof_lines: supplementation with R-alpha-lipoic acid

proof_lines: substrate hexanoylcarnitine, enzyme from liver homogenate

substrate: CoASH


organism: Saccharomyces cerevisiae

substrate_name: L-(-)-carnitine

substrate: L-(-)-carnitine


organism: Sus scrofa

substrate_name: (-)carnitine

substrate: (-)carnitine


organism: Drosophila melanogaster

substrate_name: UDPgalactose

substrate: UDPgalactose


organism: Gallus gallus