sequence_source: UniProtKB G4XDR8 plus RCSB 6IH2 SIFTS mapping.

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

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


enzyme_display_name: phosphite dehydrogenase

organism: Ralstonia sp. 4506

substrate_name: NAD+

source_db: brenda

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB G4XDR8 plus RCSB 6IH2 SIFTS mapping; variant reconstructed from selected mutation signature after residue check. and applied mutation signature C174H/D175A/P176R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 310.15 K; cofactor NADP+

proof_lines: pH 7.3, 37°C, recombinant His-tagged mutant C174H/D175A/P176R

enzyme: phosphite dehydrogenase

substrate: NAD+

source: brenda


organism: Stutzerimonas stutzeri

substrate_name: NADP+

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

mutation_type: substitution

assay_conditions_summary: pH 7.25; 298.15 K; cofactor NADP+

substrate: NADP+


proof_lines: cosubstrate NADP+, mutant E175A, pH 7.3, 25°C


proof_lines: 25°C, pH 7.25, E175A/A176R mutant enzyme


substrate_name: phosphonate

mutation_signature: Unknown

sequence_source: UniProtKB reviewed O69054/PTXD_STUST direct EC+organism lookup.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

proof_lines:
pH 7.5, 25°C, wild type enzyme
wild-type, pH 7.3, 25°C
wild-type

substrate: phosphonate


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical PTDH sequence with selected-record mutation reconstruction and applied mutation signature K330* to reconstruct the assayed variant sequence.

mutation_type: truncation

assay_conditions_summary: pH 7.3; 298.15 K; cofactor NAD+

proof_lines: cosubstrate NAD+, mutant K330*, pH 7.3, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical PTDH sequence with selected-record mutation reconstruction and applied mutation signature D13E/M26I/E175A/E332N/C336D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 298.15 K; cofactor NADP+

proof_lines: cosubstrate NADP+, mutant D13E/M26I/E175A/E332N/C336D, pH 7.3, 25°C

proof_lines: cosubstrate NAD+, mutant D13E/M26I/E175A/E332N/C336D, pH 7.3, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical PTDH sequence with selected-record mutation reconstruction and applied mutation signature M26I/E332N/C336D to reconstruct the assayed variant sequence.

proof_lines: cosubstrate NAD+, mutant M26I/E332N/C336D, pH 7.3, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical PTDH sequence with selected-record mutation reconstruction and applied mutation signature D13E/M26I/E332N/C336D to reconstruct the assayed variant sequence.

proof_lines: cosubstrate NAD+, mutant D13E/M26I/E332N/C336D, pH 7.3, 25°C

proof_lines: cosubstrate NADP+, mutant D13E/M26I/E332N/C336D, pH 7.3, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical PTDH sequence with selected-record mutation reconstruction and applied mutation signature D13E/M26I/E175A/T181S/E332N/C336D to reconstruct the assayed variant sequence.

proof_lines: cosubstrate NADP+, mutant D13E/M26I/E175A/T181S/E332N/C336D, pH 7.3, 25°C

proof_lines: cosubstrate NAD+, mutant D13E/M26I/E175A/T181S/E332N/C336D, pH 7.3, 25°C


substrate_name: phosphite

sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical PTDH sequence with selected-record mutation reconstruction and applied mutation signature D79N to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NAD+

substrate: phosphite


sequence_variant_note: Resolved canonical sequence from UniProtKB O69054 canonical PTDH sequence with selected-record mutation reconstruction and applied mutation signature D79A to reconstruct the assayed variant sequence.


km_display: Not reported

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

proof_lines:
mutant NADP-12X NAD
thermostable mutant 12X-PTDH


enzyme_display_name: 1-deoxy-D-xylulose-5-phosphate synthase

organism: Vitis vinifera

substrate_name: D-glyceraldehyde 3-phosphate

kcat_display: Not reported

enzyme: 1-deoxy-D-xylulose-5-phosphate synthase

substrate: D-glyceraldehyde 3-phosphate


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


organism: Badhamia polycephala

substrate_name: putrescine

substrate: putrescine


organism: Zea mays

source_db: uniprot

proof_lines: kcat is 0.249 sec(-1) for TRIBOA-glucoside.

source: uniprot


enzyme_display_name: D-histidine 2-aminobutanoyltransferase

organism: Staphylococcus aureus (strain Mu50 / ATCC 700699)

substrate_name: D-histidine

enzyme: D-histidine 2-aminobutanoyltransferase

substrate: D-histidine


enzyme_display_name: polynucleotide adenylyltransferase

organism: Homo sapiens

substrate_name: UTP

assay_conditions_summary: cofactor ATP

proof_lines: kcat is 0.059 sec(-1) with UTP as substrate. kcat is 0.002 sec(-1) with ATP as substrate. kcat is 0.061 sec(-1) with U6 snRNA-u4 as substrate.

enzyme: polynucleotide adenylyltransferase

substrate: UTP


enzyme_display_name: protein-serine/threonine phosphatase

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

substrate_name: pNPP

proof_lines: kcat is 0.0076 sec(-1) with pNPP as substrate.

enzyme: protein-serine/threonine phosphatase

substrate: pNPP


organism: Pseudomonas aeruginosa (strain UCBPP-PA14)

proof_lines: kcat is 0.00162 sec(-1) with pNPP as substrate.


enzyme_display_name: nicotinamidase

organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)

substrate_name: nicotinamide

enzyme: nicotinamidase

substrate: nicotinamide


organism: Arabidopsis thaliana

proof_lines: kcat is 0.93 sec(-1) with nicotinamide as substrate.


organism: Saccharomyces cerevisiae

substrate_name: CTP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P29468 canonical FASTA fetched 2026-06-16 plus selected mutation_signature Y224F and applied mutation signature Y224F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

substrate: CTP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29468 canonical FASTA fetched 2026-06-16 plus selected mutation_signature N226A and applied mutation signature N226A to reconstruct the assayed variant sequence.


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P29468 canonical FASTA fetched 2026-06-16 plus selected mutation_signature K215A and applied mutation signature K215A to reconstruct the assayed variant sequence.

substrate: ATP


substrate_name: GTP

sequence_source: UniProtKB:P29468 canonical FASTA fetched 2026-06-16

substrate: GTP


enzyme_display_name: cruzipain

organism: Trypanosoma cruzi

sequence_source: UniProtKB:Q598P5 canonical FASTA fetched 2026-06-16

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

proof_lines: recombinant form without C-terminal extension

enzyme: cruzipain


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

sequence_source: UniProtKB:P25779 canonical FASTA fetched 2026-06-16

proof_lines: 37°C, pH 5.5, recombinant cruzain, consisting of the catalytic domain of cruzipain but excluding the carboxy-terminal extension

proof_lines: pH and temperature not specified in the publication


substrate_name: Benzoyl-Pro-Phe-Arg-p-nitroanilide

source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

data_origin: experimental

substrate: Benzoyl-Pro-Phe-Arg-p-nitroanilide

status: unverified

source: oed


proof_lines:
pH 8.5, 25°C, wild-type enzyme
pH 5.5, 25°C, wild-type enzyme
pH 3.5, 25°C, wild-type enzyme


organism: Pagrus major

substrate_name: CBz-Gln-Ser

substrate: CBz-Gln-Ser


organism: Patinopecten sp.

substrate_name: Monodansylcadaverine

proof_lines:
pH 7.5, 10°C, hemocyte enzyme
pH 7.5, 10°C, muscle enzyme

substrate: Monodansylcadaverine


organism: Rattus norvegicus

substrate_name: methylamine

proof_lines:
chondrosarcoma transglutaminase B
soluble liver transglutaminase
brain transglutaminase NI

substrate: methylamine


organism: Streptomyces hygroscopicus

substrate_name: N-carboxybenzoyl-L-glutaminyl-glycine

proof_lines:
recombinant enzyme, at pH 8.0 and 37°C
pH 6.0, 37°C
native enzyme, at pH 8.0 and 37°C

substrate: N-carboxybenzoyl-L-glutaminyl-glycine


organism: Streptomyces mobaraensis

substrate_name: Propylamine

assay_conditions_summary: pH 8; 310.15 K; buffer 250 mM Tris acetate

proof_lines: 1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5-N,N-dimethylamino-1-naphthalenesulfonyl)diamidopentane as glutamine donor

proof_lines: 1-N-(carbobenzoxy-L-glutaminylglycyl)-5-N-(5-N-N-dimethylamino-1naphthalenesulfonyl)diamidopentane as glutamine donor

proof_lines: in 250 mM Tris acetate buffer (pH 8.0), at 37°C

substrate: Propylamine


organism: Streptomyces sp. TYQ1024

substrate_name: CBz-Gln-Gly

substrate: CBz-Gln-Gly


substrate_name: UDPglucose

substrate: UDPglucose


organism: Brassica napus

substrate_name: phenylacetothiohydroximate

substrate: phenylacetothiohydroximate


organism: Tropaeolum majus

proof_lines: pH 7.4, 30°C, phenylacetothiohydroximate

proof_lines: pH 7.4, 30°C, 4-methylthiobutyrothiohydroximate


enzyme_display_name: hyaluronan synthase

organism: Candidatus Mycoplasma liparidae

substrate_name: UDP-D-glucosamine

enzyme: hyaluronan synthase

substrate: UDP-D-glucosamine


organism: Mus musculus

substrate_name: UDP-D-glucuronate

substrate: UDP-D-glucuronate


organism: Bos taurus

substrate_name: putrescine

proof_lines: tissue transglutaminase from endothelial cells

substrate: putrescine


organism: Cavia porcellus

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


organism: Gallus gallus

substrate_name: casein

proof_lines:
gizzard transglutaminase
plasma factor XII, actin

substrate: casein


organism: Glycine max


organism: Homo sapiens

substrate_name: NQENVSPLTLLRLGN

proof_lines:
37°C, pH 7.4
recombinant transglutaminase 5
factor XIIIa

substrate: NQENVSPLTLLRLGN


substrate_name: Nalpha-benzyloxycarbonyl-L-Gln-Gly

proof_lines: Km above 0.03 mM, mutant enzyme C371A, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37°C

substrate: Nalpha-benzyloxycarbonyl-L-Gln-Gly


proof_lines: Km above 0.03 mM, mutant enzyme C370A, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37°C


proof_lines: wild type enzyme, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37°C


proof_lines: mutant enzyme C230A, in 1 M MOPS, 5 mM EDTA, and 50 mM 2-oxoglutarate (pH 7.2), 100 mM CaCl2, at 37°C


organism: Lathyrus oleraceus


proof_lines: enzyme induced by 12-O-tetradecanoylphorbol-13-acetate or Ca2+


organism: Mythimna separata

substrate_name: N-Cbz-Gln-Gly

substrate: N-Cbz-Gln-Gly


organism: Streptococcus dysgalactiae subsp. equisimilis

substrate_name: UDP-N-acetyl-D-glucosamine

proof_lines: pH 7.0, 30°C, recombinant mutant C262A/C367A

substrate: UDP-N-acetyl-D-glucosamine


proof_lines: pH 7.0, 30°C, recombinant mutant C226A/C367A


organism: Streptococcus equisimilis

substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate

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

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C262A, C281A


proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C226A, C367A

substrate: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate


substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C281S


proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C226A, C262A

substrate: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine


proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C367A


proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant (3C)C226

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant (3C)C262

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant (3C)C281


proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C367S


organism: Pasteurella multocida


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C226A/C262A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, recombinant mutant C226A/C262A


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C262A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:O50201 / NCBI Protein:AAB87874.1

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

proof_lines: pH 7.0, 30°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C281A/C367A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, recombinant mutant C281A/C367A


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C226A/C281A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, recombinant mutant C226A/C281A


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C226S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C262S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C367A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C281S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C367S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O50201 / NCBI Protein:AAB87874.1 and applied mutation signature C262A/C281A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, recombinant mutant C262A/C281A


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature A319R to reconstruct the assayed variant sequence.

substrate: ATP


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature Y237A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature G203H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature R199A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature K232A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature V247R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature D167N/T317G to reconstruct the assayed variant sequence.


sequence_source: RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500

assay_conditions_summary: 310.15 K; buffer formamide; cofactor ATP

proof_lines: wild-type, reactions are started with the addition of PAP and incubated at 37 °C for 15 minutes. Reactions are stopped by the addition of 8 microL of stop buffer (formamide with trace amount of bromophenol blue dye)


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature K158A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature T317G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature N239A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB PDB 1Q78/1Q79 entity 1 sequence linked to UniProt P25500 and applied mutation signature K228A to reconstruct the assayed variant sequence.


organism: Xenopus laevis

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


proof_lines: pH 7.5, 30°C, recombinant mutant C337S at higher UDP-glucuronate concentration


proof_lines: pH 7.5, 30°C, recombinant mutant C239S/C337S


proof_lines: pH 7.5, 30°C, recombinant mutant C304S/C337S


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

proof_lines: pH 7.5, 30°C, recombinant wild-type enzyme at low UDP-glucuronate concentration

proof_lines: pH 7.5, 30°C, recombinant wild-type enzyme at low UDP-N-acetyl-D-glucosamine concentration, and mutant C239S

proof_lines: pH 7.5, 30°C, recombinant wild-type enzyme and mutants C210S, C337S at low UDP-glucuronate concentration


enzyme_display_name: thymidine phosphorylase

organism: Escherichia coli

assay_conditions_summary: pH 6.5; 298.15 K; buffer 0.1 M potassium phosphate

proof_lines: in 0.1 M potassium phosphate buffer (pH 7.4), at 25°C

enzyme: thymidine phosphorylase


substrate_name: thymidine

proof_lines:
normal tissue
37°C, pH 7.4
tumor tissue

substrate: thymidine


organism: Lacticaseibacillus casei

substrate_name: phosphate

substrate: phosphate


substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine

sequence_variant_note: Resolved canonical sequence from UniProt REST O50201 canonical sequence plus selected SABIO-RK mutation note; checked 2026-06-16. and applied mutation signature C226A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C226A


substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDP-N-acetyl-D-glucosamine; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n UDPglucuronate

sequence_source: UniProt REST O50201 canonical sequence; checked 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 O50201 canonical sequence plus selected SABIO-RK mutation note; checked 2026-06-16. and applied mutation signature C262A/C367A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C262A, C367A


sequence_variant_note: Resolved canonical sequence from UniProt REST O50201 canonical sequence plus selected SABIO-RK mutation note; checked 2026-06-16. and applied mutation signature C281A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C281A


sequence_variant_note: Resolved canonical sequence from UniProt REST O50201 canonical sequence plus selected SABIO-RK mutation note; checked 2026-06-16. and applied mutation signature C262A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C262A


sequence_variant_note: Resolved canonical sequence from UniProt REST O50201 canonical sequence plus selected SABIO-RK mutation note; checked 2026-06-16. and applied mutation signature C262S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C262S


sequence_variant_note: Resolved canonical sequence from UniProt REST O50201 canonical sequence plus selected SABIO-RK mutation note; checked 2026-06-16. and applied mutation signature C281A/C367A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C281A, C367A


sequence_variant_note: Resolved canonical sequence from UniProt REST O50201 canonical sequence plus selected SABIO-RK mutation note; checked 2026-06-16. and applied mutation signature C226S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C226S


sequence_variant_note: Resolved canonical sequence from UniProt REST O50201 canonical sequence plus selected SABIO-RK mutation note; checked 2026-06-16. and applied mutation signature C226A/C281A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hyaluronan synthase(Enzyme) mutant C226A, C281A


organism: Streptococcus pyogenes


proof_lines: pH 7.5, 30°C, recombinant mutants C117S and C210S


enzyme_display_name: tRNA uracil 4-sulfurtransferase

organism: Bacillus subtilis

substrate_name: L-cysteine

enzyme: tRNA uracil 4-sulfurtransferase

substrate: L-cysteine


proof_lines:
pH 7.5, 37°C
pH 7.5, 37°C, sulfur deficient tRNA
pH 7.8, 37°C


enzyme_display_name: keratan sulfotransferase

substrate_name: Keratan sulfate

enzyme: keratan sulfotransferase

substrate: Keratan sulfate


enzyme_display_name: hydroxyacylglutathione hydrolase

organism: Aloe vera

substrate_name: S-acetylglutathione

enzyme: hydroxyacylglutathione hydrolase

substrate: S-acetylglutathione


organism: Candida albicans

substrate_name: S-D-lactoylglutathione

substrate: S-D-lactoylglutathione


organism: Cyberlindnera mrakii

substrate_name: S-Lactoylglutathione

substrate: S-Lactoylglutathione


proof_lines: recombinant wild-type enzyme, pH 7.1, 37°C


organism: Leishmania infantum

substrate_name: mono-(lactoyl)trypanothione

substrate: mono-(lactoyl)trypanothione


organism: Mus musculus


organism: Oryza sativa

proof_lines: pH and temperature not specified in the publication, Vmax: 1 mmol/min/mg


organism: Bos taurus

substrate_name: RNA (A)15

sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 residues 1-513 plus PMID 15328606 Table 3 mutation label and applied mutation signature D167N/N202A to reconstruct the assayed variant sequence.

substrate: RNA (A)15


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 residues 1-513 plus PMID 15328606 Table 3 mutation label and applied mutation signature F153A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 residues 1-513 plus PMID 15328606 Table 3 mutation label and applied mutation signature V206A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 residues 1-513 plus PMID 15328606 Table 3 mutation label and applied mutation signature D167N/V247R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 residues 1-513 plus PMID 15328606 Table 3 mutation label and applied mutation signature N202A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 residues 1-513 plus PMID 15328606 Table 3 mutation label and applied mutation signature F100D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P25500 residues 1-513 plus PMID 15328606 Table 3 mutation label and applied mutation signature V247A to reconstruct the assayed variant sequence.


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

assay_conditions_summary: pH 9; 308.15 K; cofactor ATP

proof_lines: p(A)3 primer, Mn2+-activated calf thymus enzyme


organism: Cricetulus griseus


substrate_name: CTP

assay_conditions_summary: 303.15 K; cofactor ATP

substrate: CTP


organism: Lathyrus oleraceus

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP


organism: Mesocricetus auratus

assay_conditions_summary: 310.15 K; cofactor ATP

proof_lines:
polymerase IIb, 37°C
polymerase IIa, 37°C


organism: Rattus norvegicus

substrate_name: thymine

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

proof_lines: enzyme from SD-lymphoma, pH 6.4, 37°C, substrate: phosphate

proof_lines: enzyme from SD-lymphoma, pH 6.4, 37°C, substrate: 2-deoxythymidine

substrate: thymine


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: arsenate

substrate: arsenate


enzyme_display_name: sym-norspermidine synthase

organism: Saccharolobus solfataricus

substrate_name: putrescine

enzyme: sym-norspermidine synthase

substrate: putrescine


enzyme_display_name: thermospermine synthase

organism: Thalassiosira pseudonana

substrate_name: spermidine

enzyme: thermospermine synthase

substrate: spermidine


organism: Yersinia pseudotuberculosis


enzyme_display_name: anhydro-N-acetylmuramic acid kinase

organism: Escherichia coli

substrate_name: ATP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: in 100 mM Tris-HCl (pH 7.5), 20 mM MgCl2, at 37°C

enzyme: anhydro-N-acetylmuramic acid kinase


organism: Artemia sp.

substrate_name: dATP

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP

substrate: dATP


organism: Bacillus subtilis

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


organism: Pseudomonas putida

substrate_name: Unknown

ki_unit: mM

substrate: Unknown


substrate: ATP


organism: Saccharomyces cerevisiae

proof_lines: incubation at 30 °C for 15 min in the presence of MgATP2-


proof_lines:
wild-type PAP, incubation at 30 °C
wild-type PAP


organism: Triticum aestivum


organism: Vigna radiata


organism: Zea mays

substrate_name: Nucleotide

substrate: Nucleotide


enzyme_display_name: alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase

substrate_name: GTP

proof_lines: PhnI, PhnG, PhnH and PhnL, GST tags in situ removed, proteins begin to precipitate after removal of the GST tags, therefore kinetic constants are not definitive, pH not specified in the publication, temperature not specified in the publicat

proof_lines: PhnI, nucleosidase activity, pH not specified in the publication, temperature not specified in the publication

substrate: GTP


organism: Plasmodium falciparum

proof_lines: mutant R154M, at 25°C, in 100 mM MOPS/NaOH, pH 6.8


proof_lines: mutant R154K, at 25°C, in 100 mM MOPS/NaOH, pH 6.8


proof_lines: wild-type, at 25°C, in 100 mM MOPS/NaOH, pH 6.8


proof_lines: mutant R257Q, at 25°C, in 100 mM MOPS/NaOH, pH 7.4


proof_lines: mutant K260D, at 25°C, in 100 mM MOPS/NaOH, pH 6.8


proof_lines: mutant K260Q, at 25°C, in 100 mM MOPS/NaOH, pH 6.8


proof_lines: mutant R257D, at 25°C, in 100 mM MOPS/NaOH, pH 6.8


proof_lines: inhibitor binding to the free enzyme, at 25°C, pH 6.8

proof_lines: inhibitor binding to the occupied enzyme, at 25°C, pH 6.8


proof_lines:
mitochondrial enzyme
enzyme from erythrocytes
matrix enzyme


substrate_name: S-D-mandeloylglutathione

substrate: S-D-mandeloylglutathione


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


assay_conditions_summary: pH 7.2; 298.15 K; buffer 10 mM MOPS

proof_lines: in 10 mM MOPS buffer at pH 7.2, at 25 °C


organism: Bacillus anthracis

substrate_name: 4-nitrophenyl phosphate

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication

substrate: 4-nitrophenyl phosphate


substrate_name: H2O; SpoIIAA-phosphorylated

substrate: H2O; SpoIIAA-phosphorylated


organism: Bos taurus

substrate_name: FYDEEVDEMY(P)REAPIDKKGNFNY(P)VEFTR

proof_lines:
30°C, AC dimer
30°C, C-subunit
30°C, AC-R2

substrate: FYDEEVDEMY(P)REAPIDKKGNFNY(P)VEFTR


organism: chicken anemia virus

substrate_name: RRApTVA

substrate: RRApTVA


organism: Enterococcus faecium

proof_lines: mutant enzyme T101R, with 2 mM Mn2+, in 50 mM Tris-HCl (pH 8.0), at 37°C


proof_lines: mutant enzyme D136Y, with 2 mM Mn2+, in 50 mM Tris-HCl (pH 8.0), at 37°C

proof_lines: mutant enzyme D136Y, with 0.05 mM Mn2+, in 50 mM Tris-HCl (pH 8.0), at 37°C


proof_lines: mutant enzyme S120R, with 2 mM Mn2+, in 50 mM Tris-HCl (pH 8.0), at 37°C

proof_lines: mutant enzyme S120R, with 0.05 mM Mn2+, in 50 mM Tris-HCl (pH 8.0), at 37°C


proof_lines: wild type enzyme, with 0.05 mM Mn2+, in 50 mM Tris-HCl (pH 8.0), at 37°C

proof_lines: wild type enzyme, with 2 mM Mn2+, in 50 mM Tris-HCl (pH 8.0), at 37°C


substrate_name: 4-Nitrophenyl phosphate; H2O

substrate: 4-Nitrophenyl phosphate; H2O


organism: Glycine max

substrate_name: phosphohistone H1

substrate: phosphohistone H1


organism: Homo sapiens


proof_lines: pH 7.5, 30°C, recombinant His-tagged Wip1 catalytic subunit


organism: Hymenolepis diminuta

substrate_name: DLDVPIPGRFDRRVSVAAE

substrate: DLDVPIPGRFDRRVSVAAE


organism: Hymenolepis microstoma


organism: Lambdavirus lambda

substrate_name: p-nitrophenyl phosphate

substrate: p-nitrophenyl phosphate


proof_lines:
pH 7.8, wild-type Prep 2
pH 7.8, wild-type Prep 1


enzyme_display_name: oleoyl-[acyl-carrier-protein] hydrolase

organism: Arabidopsis thaliana

substrate_name: stearoyl-[acyl-carrier protein]

proof_lines:
isozyme FatB, pH 8.0, 22°C
isozyme FatA, pH 8.0, 22°C

enzyme: oleoyl-[acyl-carrier-protein] hydrolase

substrate: stearoyl-[acyl-carrier protein]


substrate_name: myristoyl-ACP (14:0-ACP)

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

proof_lines: The catalytic efficiency for 18:1 is at least 20-fold higher than for other substrates.

substrate: myristoyl-ACP (14:0-ACP)


organism: Escherichia coli (strain K12)

assay_conditions_summary: cofactor CoA

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


organism: Lathyrus oleraceus


organism: Meleagris gallopavo

substrate_name: heavy meromyosin

substrate: heavy meromyosin


organism: Oryctolagus cuniculus

substrate_name: phosphorylase a

proof_lines:
presence of Mn2+
absence of Mn2+

substrate: phosphorylase a


organism: Rattus norvegicus

substrate_name: Phosphoprotein; H2O

proof_lines: SABIO-RK modifier species: phosphoprotein phosphatase(Enzyme) mutant a/CaNA

substrate: Phosphoprotein; H2O


substrate_name: phosphohistone

substrate: phosphohistone


organism: Saccharomyces cerevisiae

proof_lines: purified, catalytically active 40 kDa-subunit, in 300 mM Tris pH 7.8, 150 mM potassium chloride, 25 mM magnesium chloride, 5 mM dithiothreitol, at 30°C

proof_lines: full-length Ppt1, in 300 mM Tris pH 7.8, 150 mM potassium chloride, 25 mM magnesium chloride, 5 mM dithiothreitol, at 30°C


organism: Salmonella enterica

substrate_name: serine/threonine-phosphorylated myelin basic protein

proof_lines:
pH 8.0, recombinant His-tagged enzyme
pH 9.5, recombinant His-tagged enzyme


organism: Synechocystis sp.

substrate_name: phosphoserine-myelin basic protein

proof_lines:
pH 7.5, 37°, recombinant SynPPP1
pH 7.5, 37°, recombinant SynPPM3

substrate: phosphoserine-myelin basic protein


organism: Triticum aestivum

substrate_name: phosphocasein

substrate: phosphocasein


organism: Trypanosoma brucei


enzyme_display_name: dGTPase

organism: Escherichia coli

substrate_name: dGTP

enzyme: dGTPase

substrate: dGTP


enzyme_display_name: glutamyl aminopeptidase

organism: Aspergillus oryzae

substrate_name: L-Leu-beta-naphthylamide

enzyme: glutamyl aminopeptidase

substrate: L-Leu-beta-naphthylamide


organism: Ricinus communis

substrate_name: oleoyl-[acyl-carrier protein]

smiles: CCCCCCCCC=CCCCCCCCC(=O)S

substrate: oleoyl-[acyl-carrier protein]


substrate_name: palmitoyl-[acyl-carrier protein]

sequence_source: UniProtKB:A9XK92 REST/FASTA direct lookup on 2026-06-16

assay_conditions_summary: pH 8; 295.15 K; buffer 50 mM Tris-HCl

proof_lines: in 50 mM Tris-HCl buffer, pH 8.0, 5 mM DTT, at 22°C

substrate: palmitoyl-[acyl-carrier protein]


substrate_name: palmitoleoyl-[acyl-carrier protein]

smiles: *SC(=O)CCCCCCC/C=C\CCCCCC

substrate: palmitoleoyl-[acyl-carrier protein]


sequence_source: UniProtKB:A9XUG5 REST/FASTA direct lookup on 2026-06-16


smiles: *SC(=O)CCCCCCCCCCCCCCC


smiles: *SC(=O)CCCCCCCCCCCCCCCCC


organism: Homo sapiens

substrate_name: acetyl-CoA

assay_conditions_summary: cofactor NADPH

substrate: acetyl-CoA


organism: Mus musculus

substrate_name: malonyl-CoA

substrate: malonyl-CoA


substrate_name: Unknown

substrate: Unknown


substrate_name: UDP-xylose

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

assay_conditions_summary: pH 7; 310.15 K; buffer the batch. Source notes: in 100 mM cacodylate

proof_lines: in 100 mM cacodylate buffer, pH 7.0 containing 10 mM MnCl2 and 0.2-6 microM purified fusion-beta1,4-GalT7

proof_lines: recombinant maltose-binding protein-beta1,4-GalT7 fusion protein

source_databases_merged: brenda skid

substrate: UDP-xylose


substrate_name: UDP-galactose

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 7; 310.15 K; buffer 100 mM sodium cacodylate

proof_lines: pH 7.0, 37°C, mutant D230A, protein expressed in HeLa cells

proof_lines: mutant enzyme D230A, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C

substrate: UDP-galactose


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature G223A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant G223A, protein expressed in HeLa cells

proof_lines: mutant enzyme G223A, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature W224H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature D165E to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant D165E, protein expressed in HeLa cells

proof_lines: mutant enzyme D165E, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature W222A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant W222A, protein expressed in HeLa cells

proof_lines: mutant enzyme W222A, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature E227D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature F221Y to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant F221Y, protein expressed in HeLa cells

proof_lines: mutant enzyme F221Y, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature W222F to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant W222F, protein expressed in HeLa cells

proof_lines: mutant enzyme W222F, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature D228E to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant D228E, protein expressed in HeLa cells

proof_lines: mutant enzyme D228E, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


proof_lines: pH 7.0, 37°C, mutant W224H, protein expressed in Escherichia coli

proof_lines: pH 7.0, 37°C, mutant W224H, protein expressed in HeLa cells

proof_lines: mutant enzyme W224H, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature F221A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant F221A, protein expressed in HeLa cells

proof_lines: mutant enzyme F221A, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


proof_lines: pH 7.0, 37°C, mutant E227D, protein expressed in Escherichia coli

proof_lines: pH 7.0, 37°C, mutant E227D, protein expressed in HeLa cells

proof_lines: mutant enzyme E227D, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UBV7 and applied mutation signature V164A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant V164A, protein expressed in HeLa cells

proof_lines: mutant enzyme V164A, in 100 mM sodium cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C


organism: Cuphea hookeriana

substrate_name: decanoyl-[acyl-carrier protein]

sequence_source: UniProtKB REST lookup for Q39514 on 2026-06-16

smiles: *SC(=O)CCCCCCCCC

substrate: decanoyl-[acyl-carrier protein]


sequence_variant_note: Resolved canonical sequence from UniProtKB REST lookup for Q39514 on 2026-06-16 and applied mutation signature I198E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST lookup for Q39514 on 2026-06-16 and applied mutation signature K287E to reconstruct the assayed variant sequence.


substrate_name: dodecanoyl-[acyl-carrier protein]; octanoyl-[acyl-carrier protein]

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

proof_lines: acyl carrier protein of Escherichia coli, pH 8, temperature not specified in the publication

proof_lines: acyl carrier protein2 of Cuphea hookeriana, pH 8, temperature not specified in the publication


organism: Cuphea palustris

substrate_name: octanoyl-[acyl-carrier protein]

sequence_source: UniProtKB REST lookup for Q39554 on 2026-06-16

proof_lines: at pH 7.4, temperature not specified in the publication

substrate: octanoyl-[acyl-carrier protein]


organism: Koelreuteria paniculata

substrate_name: palmitoyl-[acyl-carrier protein]; stearoyl-[acyl-carrier protein]; oleoyl-[acyl-carrier protein]

sequence_source: UniProtKB REST lookup for A0A678PVH0 on 2026-06-16


sequence_source: UniProtKB REST lookup for A0A7S5LEX2 on 2026-06-16

substrate: palmitoyl-[acyl-carrier protein]; stearoyl-[acyl-carrier protein]; oleoyl-[acyl-carrier protein]


organism: Macadamia tetraphylla

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


substrate_name: palmitoleoyl-[acyl-carrier protein]; oleoyl-[acyl-carrier protein]; palmitoyl-[acyl-carrier protein]; stearoyl-[acyl-carrier protein]

sequence_source: UniProtKB REST lookup for D5FFZ2 on 2026-06-16


substrate_name: palmitoleoyl-[acyl-carrier protein]; palmitoyl-[acyl-carrier protein]; stearoyl-[acyl-carrier protein]; oleoyl-[acyl-carrier protein]

sequence_source: UniProtKB REST lookup for D2E6T0 on 2026-06-16


substrate_name: stearoyl-[acyl-carrier protein]

substrate: stearoyl-[acyl-carrier protein]


substrate_name: UDP-alpha-D-galactose

sequence_variant_note: Resolved canonical sequence from UniProt REST/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence and applied mutation signature H195R to reconstruct the assayed variant sequence.

substrate: UDP-alpha-D-galactose


sequence_source: UniProt REST/FASTA direct accession check

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

proof_lines: pH 7.0, 37°C, recombinant wild-type enzyme

proof_lines: pH 7.0, 37°C, wild-type, protein expressed in Escherichia coli

proof_lines: pH 7.0, 37°C, wild-type, protein expressed in HeLa cells


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.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UBV7 and applied mutation signature R270K to reconstruct the assayed variant sequence.

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 R270K; shared kcat column cell = 48.7 min^-1; 4-MUX Km column cell = 0.54 mm; 4-MUX kcat/Km column cell = 85 min^-1 mm^-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 48.7 under the column head kcat (min-1); one min^-1 is 1/60 s^-1, so 48.7 / 60 = 0.8116666666666668 s^-1; the exported value is 0.81 s^(-1). Km: printed Table 1 cell 0.54 under the 4-MUX column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.54 mM; the exported value is 0.54 mM. kcat/Km: printed Table 1 cell 85 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 85 / 60 = 1.4166666666666667 s^-1 mM^-1; the exported value is 1.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R270K, 4-MUX columns: kcat = 48.7 min^-1 (printed with its tolerance +/- 1.5); Km = 0.54 mm (printed with its tolerance +/- 0.07); kcat/Km = 85 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.

status: corrected


column_label: Table 1: Kinetic parameters of wild-type and mutant GST-b4GalT7 (J. Biol. Chem. 2015, 290(12):7658). Enzyme row R270K; shared kcat column cell = 48.7 min^-1; UDP-Gal Km column cell = 0.37 mm; UDP-Gal kcat/Km column cell = 139 min^-1 mm^-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 48.7 under the column head kcat (min-1); one min^-1 is 1/60 s^-1, so 48.7 / 60 = 0.8116666666666668 s^-1; the exported value is 0.81 s^(-1). Km: printed Table 1 cell 0.37 under the UDP-Gal column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.37 mM; the exported value is 0.37 mM. kcat/Km: printed Table 1 cell 139 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 139 / 60 = 2.316666666666667 s^-1 mM^-1; the exported value is 2.1891891891891895 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R270K, UDP-Gal columns: kcat = 48.7 min^-1 (printed with its tolerance +/- 1.5); Km = 0.37 mm (printed with its tolerance +/- 0.02); kcat/Km = 139 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/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence and applied mutation signature R226K to reconstruct the assayed variant sequence.


sequence_source: UniProt REST/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UBV7 and applied mutation signature R270A 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 R270A; shared kcat column cell = 46.4 min^-1; UDP-Gal Km column cell = 0.27 mm; UDP-Gal kcat/Km column cell = 184 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 0.27 under the UDP-Gal column head Km (mm); the printed millimolar column needs no conversion, so the canonical value is 0.27 mM; the exported value is 0.27 mM. kcat/Km: printed Table 1 cell 184 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 184 / 60 = 3.066666666666667 s^-1 mM^-1; the exported value is 2.8518518518518516 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R270A, UDP-Gal columns: kcat = 46.4 min^-1 (printed with its tolerance +/- 0.2); Km = 0.27 mm (printed with its tolerance +/- 0.01); kcat/Km = 184 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/FASTA direct accession check; variant sequence reconstructed from canonical accession sequence and applied mutation signature Y196F 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 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.


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.


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.


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.


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

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

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


enzyme_display_name: xanthine phosphoribosyltransferase

organism: Bacillus subtilis

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

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

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

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

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


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

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

proof_lines: pH 7.4, temperature not specified in the publication


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


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


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


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

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


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

substrate: Unknown


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_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


organism: Homo sapiens

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

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

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


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.


organism: Homo sapiens

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.

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.