sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:F6BL85 and applied mutation signature R786H to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters of TxGH116 and Its Mutants for Hydrolysis of 4NP-Glycosides and Oligosaccharides), protein row 'R786H', substrate column value '4NP β-D-glucoside'; column 'KM (mM)' = 15.7 ± 0.50; column 'kcat (s^-1)' = 193 ± 2.4; column 'kcat/KM (mM^-1 s^-1)' = 12.3; column 'temperature optimum' = 70 °C; column 'Tm' = 73.9 °C.

normalized_value_unit_evidence: Km: printed Table 2 cell 15.7 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 15.7 mM. kcat: printed Table 2 cell 193 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 193.0 s^(-1). kcat/Km: printed Table 2 cell 12.3 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell normalizes to 12.3 s^(-1)*mM^(-1). The exported kcat_over_km 12.29299363057325 s^(-1)*mM^(-1) is the exact quotient 193 / 15.7 of the same Table 2 cells, and the printed cell is that quotient carried to the precision the paper prints.

raw_value_unit_evidence: Table 2, protein row 'R786H', substrate '4NP β-D-glucoside': KM = 15.7 mM; kcat = 193 s^-1; printed kcat/KM = 12.3 mM^-1 s^-1.

row_label: Table 2, protein row 'R786H' with substrate '4NP β-D-glucoside'


enzyme_display_name: adenine phosphoribosyltransferase

organism: Escherichia coli

substrate_name: adenine

source_db: brenda

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

enzyme: adenine phosphoribosyltransferase

substrate: adenine

source: brenda


organism: Hevea brasiliensis

kcat_display: Not reported


organism: Homo sapiens

proof_lines:
in (HPRT+)
in Propositus (HPRT-)


organism: Leishmania donovani

substrate_name: diphosphate

protein_accession_database: UniProt

sequence_source: UniProtKB:Q27679 via RCSB 1QB7/1QB8/1QCC/1QCD SIFTS alignment

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

proof_lines: pH 7.4, temperature not specified in the publication

substrate: diphosphate


organism: Mus musculus

substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


organism: Plasmodium chabaudi


enzyme_display_name: deoxyguanosine kinase

substrate_name: Deoxyguanosine; ATP

km_display: Not reported

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

sequence_source: UniProtKB direct accession lookup: Q9QX60

assay_conditions_summary: cofactor ATP

enzyme: deoxyguanosine kinase

substrate: Deoxyguanosine; ATP


organism: Mycoplasma mycoides

substrate_name: Deoxyguanosine

source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

sequence_source: UniProtKB direct accession lookup: Q93IG4

data_origin: experimental

substrate: Deoxyguanosine

status: unverified

source: oed


organism: Staphylococcus aureus

substrate_name: ATP; Deoxyguanosine

sequence_source: UniProtKB direct accession lookup: Q0H0G8

substrate: ATP; Deoxyguanosine


organism: Xenopus laevis

substrate_name: deoxyadenosine

sequence_source: UniProtKB direct accession lookup: Q6GPW6

assay_conditions_summary: pH 8

proof_lines: at pH 8.0, temperature not specified in the publication

substrate: deoxyadenosine


enzyme_display_name: glucosylceramidase

organism: Arabidopsis thaliana

sequence_source: UniProtKB direct accession lookup: F4JLJ2

enzyme: glucosylceramidase


organism: Thermoanaerobacterium xylanolyticum

substrate_name: laminaribiose

sequence_source: UniProtKB direct accession lookup: F6BL85

proof_lines: wild type enzyme without N-terminal tag, at pH 5.5 and 60°C

proof_lines: wild type enzyme with N-terminal tag, at pH 5.5 and 60°C

substrate: laminaribiose


substrate_name: 4-nitrophenyl beta-D-glucoside

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup: F6BL85 and applied mutation signature D508N to reconstruct the assayed variant sequence.

mutation_type: substitution

substrate: 4-nitrophenyl beta-D-glucoside


organism: Unknown

substrate_name: DNA adenine

substrate: DNA adenine


organism: Bacillus subtilis

substrate_name: UTP; Deoxyguanosine

sequence_source: UniProtKB:P37530 direct REST lookup 2026-06-06

substrate: UTP; Deoxyguanosine


substrate_name: CTP

substrate: CTP


substrate_name: GTP

substrate: GTP


substrate_name: ATP

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: UTP

substrate: UTP


organism: Bos taurus

sequence_source: UniProtKB:Q2KIN2 direct REST lookup 2026-06-06


organism: Dictyostelium discoideum

substrate_name: ATP; Deoxyadenosine

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

sequence_source: UniProtKB:Q54UT2 direct REST lookup 2026-06-06

substrate: ATP; Deoxyadenosine


organism: Escherichia phage P1

substrate_name: ssDNA

source_db: uniprot

substrate: ssDNA

source: uniprot


organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

substrate_name: S-adenosyl-L-methionine

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

substrate: S-adenosyl-L-methionine


substrate_name: U2 snRNA

substrate: U2 snRNA


organism: Thermus aquaticus

substrate_name: DNA

substrate: DNA


sequence_source: UniProtKB:Q54UT2 direct lookup


substrate_name: D-2'-Deoxycarbocyclic guanosine; ATP

sequence_source: UniProtKB:Q16854 direct lookup

substrate: D-2'-Deoxycarbocyclic guanosine; ATP


organism: Lactobacillus johnsonii

substrate_name: deoxyguanosine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q74HC2 direct lookup plus D84N reconstruction from selected mutation_signature and applied mutation signature D84N to reconstruct the assayed variant sequence.

substrate: deoxyguanosine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q74HC2 direct lookup plus D84A reconstruction from selected mutation_signature and applied mutation signature D84A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q74HC2 direct lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q74HC2 direct lookup plus D84E reconstruction from selected mutation_signature and applied mutation signature D84E to reconstruct the assayed variant sequence.


substrate_name: ATP; Deoxyguanosine

ki_unit: mM

substrate: ATP; Deoxyguanosine


enzyme_display_name: S-formylglutathione hydrolase

organism: Escherichia coli

substrate_name: p-Nitrophenyl acetate

sequence_source: UniProtKB P33018 canonical sequence from direct REST/FASTA check

enzyme: S-formylglutathione hydrolase

substrate: p-Nitrophenyl acetate


substrate_name: H2O; 1-Naphthylacetic acid

sequence_variant_note: Resolved canonical sequence from UniProtKB P33018 canonical sequence; D199A reconstructed by replacing canonical residue 199 D with A and applied mutation signature D199A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: S-formylglutathione hydrolase(Enzyme) mutant YeiG D199A

substrate: H2O; 1-Naphthylacetic acid


substrate_name: p-Nitrophenyl acetate; H2O

sequence_source: UniProtKB P51025 canonical sequence from direct REST/FASTA check

substrate: p-Nitrophenyl acetate; H2O


substrate_name: 1-Naphthylacetic acid

sequence_variant_note: Resolved canonical sequence from UniProtKB P33018 canonical sequence; C26A reconstructed by replacing canonical residue 26 C with A and applied mutation signature C26A to reconstruct the assayed variant sequence.

substrate: 1-Naphthylacetic acid


sequence_source: UniProtKB P33018 canonical sequence; C26A reconstructed by replacing canonical residue 26 C with A

proof_lines: SABIO-RK modifier species: S-formylglutathione hydrolase(Enzyme) mutant YeiG C26A


substrate_name: p-Nitrophenyl propionate

substrate: p-Nitrophenyl propionate


substrate_name: 1-Naphthylacetic acid; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB P33018 canonical sequence; D255A reconstructed by replacing canonical residue 255 D with A and applied mutation signature D255A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: S-formylglutathione hydrolase(Enzyme) mutant YeiG D255A

substrate: 1-Naphthylacetic acid; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P33018 direct FASTA/JSON lookup on 2026-06-06 and applied mutation signature D255A to reconstruct the assayed variant sequence.


substrate_name: S-Lactoylglutathione

sequence_source: UniProtKB reviewed accession P33018 direct FASTA/JSON lookup on 2026-06-06

substrate: S-Lactoylglutathione


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P33018 direct FASTA/JSON lookup on 2026-06-06 and applied mutation signature D80A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P33018 direct FASTA/JSON lookup on 2026-06-06 and applied mutation signature D199A to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: S-formylglutathione hydrolase(Enzyme) mutant YeiG D80A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P33018 direct FASTA/JSON lookup on 2026-06-06 and applied mutation signature C54A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P51025 direct FASTA/JSON lookup on 2026-06-06


substrate_name: S-Formylglutathione

substrate: S-Formylglutathione


sequence_source: UniProtKB reviewed accession P33018


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P33018 plus SABIO-RK source mutation note D218A and applied mutation signature D218A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: S-formylglutathione hydrolase(Enzyme) mutant YeiG D218A


organism: Saccharomyces cerevisiae

substrate_name: 4-nitrophenyl acetate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P40363 plus BRENDA source mutation note C60R/W197I and applied mutation signature C60R/W197I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C

substrate: 4-nitrophenyl acetate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P40363 plus BRENDA source mutation note L58H/W197I and applied mutation signature L58H/W197I to reconstruct the assayed variant sequence.

proof_lines: kcat less than 0.0165 s-1, mutant enzyme L58H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C

proof_lines: Km less than 0.2 mM, mutant enzyme L58H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C


substrate_name: 4-nitrophenyl butyrate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P40363 plus BRENDA source mutation note W197I and applied mutation signature W197I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C

substrate: 4-nitrophenyl butyrate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P40363 plus BRENDA source mutation note C60H/W197I and applied mutation signature C60H/W197I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C60H/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C


sequence_source: UniProtKB reviewed accession P40363

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

proof_lines: Km above 1.25 mM, wild type enzyme, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P40363 plus BRENDA source mutation note M162H and applied mutation signature M162H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M162H, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C


sequence_source: UniProtKB REST lookup: Q8LAS8


substrate_name: p-Nitrophenyl caproate

sequence_source: UniProtKB REST lookup: P33018

substrate: p-Nitrophenyl caproate


sequence_source: UniProtKB REST lookup: P51025


sequence_variant_note: Resolved canonical sequence from UniProtKB REST lookup P33018 plus C54A reconstruction from selected mutation signature and applied mutation signature C54A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: S-formylglutathione hydrolase(Enzyme) mutant YeiG C54A


sequence_variant_note: Resolved canonical sequence from UniProtKB REST lookup P33018 plus D218A reconstruction from selected mutation signature and applied mutation signature D218A to reconstruct the assayed variant sequence.


substrate_name: S-Lactoylglutathione; H2O

substrate: S-Lactoylglutathione; H2O


substrate_name: p-Nitrophenyl butyrate

substrate: p-Nitrophenyl butyrate


organism: Bacillus subtilis (strain 168)

substrate_name: deoxyguanosine (with UTP at pH 7.8 and at 37 degrees Celsius)

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


organism: Homo sapiens

substrate_name: deoxycytidine (dC)

substrate: deoxycytidine (dC)


organism: Mus musculus

substrate_name: deoxycytidine

substrate: deoxycytidine


substrate_name: S-formylglutathione

substrate: S-formylglutathione


organism: Escherichia coli (strain K12)


sequence_variant_note: Resolved canonical sequence from UniProtKB P40363 direct REST lookup; variant reconstructed from checked canonical residues C60 and W197. and applied mutation signature C60Q/W197I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C60Q/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P40363 direct REST lookup; variant reconstructed from checked canonical residue C60. and applied mutation signature C60S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C60S, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P40363 direct REST lookup; variant reconstructed from checked canonical residues C60 and W197. and applied mutation signature C60S/W197I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P40363 direct REST lookup; variant reconstructed from checked canonical residues M162, C60, and W197. and applied mutation signature M162H/C60S/W197I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M162H/C60S/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P40363 direct REST lookup; variant reconstructed from checked canonical residues C60 and W197. and applied mutation signature C60K/W197I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C60K/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB P40363 direct REST lookup.

source: skid


organism: Shewanella frigidimarina

sequence_source: UniProtKB Q07XK4 direct REST lookup.

proof_lines: wild-type, pH 8, temperature not specified in the publication


substrate_name: 4-nitrophenyl butanoate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q07XK4 direct REST lookup; variant reconstructed from checked canonical residue W182. and applied mutation signature W182A to reconstruct the assayed variant sequence.

proof_lines: mutant W182A, pH 8, temperature not specified in the publication

substrate: 4-nitrophenyl butanoate


organism: Helicobacter pylori

substrate_name: DNA adenine

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

proof_lines: in 10 mM Tris/HCl, pH 8.0, 5 mM 2-mercaptoethanol, at 37°C

substrate: DNA adenine


organism: Klebsiella pneumoniae

substrate_name: adenine in DNA

proof_lines: substrate hemimethylated duplex DNA, recombinant enzyme, pH 8.0, 37°C

proof_lines: substrate unmethylated duplex DNA, recombinant enzyme, pH 8.0, 37°C

proof_lines: substrate plasmid DNA, recombinant enzyme, pH 8.0, 37°C

substrate: adenine in DNA


organism: Tequatrovirus T4

proof_lines: 20mer duplex, unligated, single-site, pH 8.0, 25°C

proof_lines: nonglucosylated unmethylated T4 gt- dam- DNA


substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

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

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


organism: Gallus gallus

proof_lines: kcat is 0.05 sec(-1) with deoxycytodine as substrate. kcat is 4.07 sec(-1) with deoxyadenosine as substrate. kcat is 1.23 sec(-1) with deoxyguanosine as substrate. kcat is 1.05 sec(-1) with deoxyuridine as substrate. kcat is 1.08 sec(-1) wi


substrate_name: deoxyguanosine

proof_lines: kcat is 0.67 sec(-1) with deoxyguanosine as substrate. kcat is 0.52 sec(-1) with deoxycytidine as substrate. kcat is 2.56 sec(-1) with deoxyadenosine as substrate. kcat is 0.53 sec(-1) with deoxyuridine as substrate. kcat is 0.26 sec(-1) wi

substrate: deoxyguanosine


organism: Xenopus laevis

proof_lines: kcat is 0.09 sec(-1) with deoxycytodine as substrate. kcat is 3.40 sec(-1) with deoxyguanosine as substrate. kcat is 2.73 sec(-1) with deoxyadenosine as substrate. kcat is 0.29 sec(-1) with deoxythymidine as substrate. kcat is 1.27 sec(-1)


proof_lines: kcat is 0.11 sec(-1) with deoxyguanosine as substrate. kcat is 0.30 sec(-1) with deoxyadenosine as substrate. kcat is 0.51 sec(-1) with deoxycytidine as substrate. kcat is 0.02 sec(-1) with deoxyuridine as substrate. kcat is 0.07 sec(-1) wi


proof_lines: kcat is 1.26 sec(-1) with deoxyguanosine as substrate. kcat is 4.87 sec(-1) with deoxyadenosine as substrate. kcat is 0.42 sec(-1) with deoxycytidine as substrate. kcat is 0.36 sec(-1) with deoxyuridine as substrate. kcat is 0.14 sec(-1) wi


enzyme_display_name: sterol esterase

substrate_name: p-nitrophenyl acetate

proof_lines: kcat is 59 min(-1), 29 min(-1), 90 min(-1) with 2-arachidonoylglycerol, prostaglandin F2alpha 1-glyceryl ester and prostaglandin E2 1-glyceryl ester as substrates, respectively.

enzyme: sterol esterase

substrate: p-nitrophenyl acetate


sequence_variant_note: Resolved canonical sequence from UniProt P49435 plus PMID 11535055 mutagenesis feature and applied mutation signature E106L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P49435 plus PMID 11535055 mutagenesis feature and applied mutation signature E106Q to reconstruct the assayed variant sequence.


sequence_source: UniProt P49435 with RCSB 1G2Q/SIFTS support

proof_lines:
wild-type enzyme, mutant G108A
wild-type


sequence_variant_note: Resolved canonical sequence from UniProt P49435 plus PMID 11535055 mutagenesis feature and applied mutation signature R89A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P49435 plus PMID 11535055 mutagenesis feature and applied mutation signature Y107F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P49435 plus PMID 11535055 mutagenesis feature and applied mutation signature Y107D to reconstruct the assayed variant sequence.


organism: Schizosaccharomyces pombe

sequence_source: UniProtKB reviewed O42842 (APT_SCHPO)

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


organism: Triticum aestivum


enzyme_display_name: aromatic-amino-acid transaminase

organism: Aspergillus fumigatus

substrate_name: L-tryptophan

proof_lines: pH 7.4, 25°C, recombinant enzyme, with cosubstrate 2-oxoglutarate

proof_lines: pH 7.4, 25°C, recombinant enzyme, with cosubstrate L-glutamate

proof_lines: pH 7.4, 25°C, recombinant enzyme, with cosubstrate L-tryptophan

enzyme: aromatic-amino-acid transaminase

substrate: L-tryptophan


organism: Azospirillum brasilense

substrate_name: L-tyrosine

proof_lines:
cosubstrate L-tyrosine
cosubstrate L-tryptophan

substrate: L-tyrosine


organism: Bacillus brevis

substrate_name: 2-Oxoglutarate; L-Phenylalanine

substrate: 2-Oxoglutarate; L-Phenylalanine


enzyme_display_name: N-acylneuraminate cytidylyltransferase

organism: Unknown

substrate_name: CTP

enzyme: N-acylneuraminate cytidylyltransferase

substrate: CTP


organism: Escherichia coli O18:K1:H7 (strain RS218 / NMEC)

substrate_name: NeuNAc (at pH 9.0)

assay_conditions_summary: pH 9

substrate: NeuNAc (at pH 9.0)


organism: Neisseria meningitidis

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A0Z8 and applied mutation signature R173A to reconstruct the assayed variant sequence.

column_label: Table 1 (True kinetic parameters determined for wild-type and mutant CNS), row 'R173A'; column 'kcat (min^-1)' = 420; column 'Km(CTP) (uM)' = 48; column 'kcat/Km (uM^-1 min^-1) CTP' = 8.6; column 'Km(Neu5Ac) (uM)' = 290; column 'ka0 (uM)' = 320; column 'kcat/Km (uM^-1 min^-1) Neu5Ac' = 1.4.

raw_value_unit_evidence: Table 1, row R173A, substrate CTP: kcat = 420 min^-1; Km(CTP) = 48 uM; printed kcat/Km(CTP) = 8.6 uM^-1 min^-1.

row_label: Table 1, row R173A, substrate CTP (the kcat, Km(CTP) and kcat/Km(CTP) cells of that printed row)

table_label: Table 1: True kinetic parameters determined for wild-type and mutant CNS (FEBS Journal 277 (2010) 2779-2790)

status: corrected


substrate_name: N-glycolylneuraminate

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

sequence_source: UniProtKB REST accession P0A0Z8

proof_lines:
pH 8.5, 37°C
Raw SKiD Env: Temp=37°C, pH=8.5
Raw SKiD Env: Temp=22°C, pH=7.5

source_databases_merged: brenda skid

substrate: N-glycolylneuraminate


organism: Oncorhynchus mykiss

substrate_name: CTP; Deaminoneuraminate

sequence_source: UniProtKB REST accession Q90WG6

substrate: CTP; Deaminoneuraminate


organism: Rattus norvegicus

substrate_name: CTP; N-Acetylneuraminate

sequence_source: UniProtKB REST accession P69060

substrate: CTP; N-Acetylneuraminate


organism: Streptococcus agalactiae

sequence_source: UniProtKB REST accession Q9AFG9


organism: Thermoanaerobacterium xylanolyticum

substrate_name: 4-nitrophenyl beta-D-galactoside

verification_status: verified

sequence_source: UniProtKB REST accession F6BL85

column_label: Table 2 (Kinetic Parameters of TxGH116 and Its Mutants for Hydrolysis of 4NP-Glycosides and Oligosaccharides), protein row 'TxGH116 WT without N-term tag', substrate column value '4NP β-D-galactoside'; column 'KM (mM)' = 16.3 ± 0.94; column 'kcat (s^-1)' = 255 ± 5; column 'kcat/KM (mM^-1 s^-1)' = 15.6.

normalized_value_unit_evidence: Km: printed Table 2 cell 16.3 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 16.3 mM. kcat: printed Table 2 cell 255 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 255.0 s^(-1). kcat/Km: printed Table 2 cell 15.6 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell normalizes to 15.6 s^(-1)*mM^(-1). The exported kcat_over_km 15.644171779141104 s^(-1)*mM^(-1) is the exact quotient 255 / 16.3 of the same Table 2 cells, and the printed cell is that quotient carried to the precision the paper prints.

raw_value_unit_evidence: Table 2, protein row 'TxGH116 WT without N-term tag', substrate '4NP β-D-galactoside': KM = 16.3 mM; kcat = 255 s^-1; printed kcat/KM = 15.6 mM^-1 s^-1.

row_label: Table 2, protein row 'TxGH116 WT without N-term tag' with substrate '4NP β-D-galactoside'

table_label: Table 2: Kinetic Parameters of TxGH116 and Its Mutants for Hydrolysis of 4NP-Glycosides and Oligosaccharides (ACS Chem. Biol. 2016, 11, 1891-1900)

substrate: 4-nitrophenyl beta-D-galactoside

status: verified


substrate_name: cellobiose

column_label: Table 2 (Kinetic Parameters of TxGH116 and Its Mutants for Hydrolysis of 4NP-Glycosides and Oligosaccharides), protein row 'TxGH116 WT without N-term tag', substrate column value 'cellobiose'; column 'KM (mM)' = 0.25 ± 0.016; column 'kcat (s^-1)' = 44.4 ± 0.7; column 'kcat/KM (mM^-1 s^-1)' = 178.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.25 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 0.25 mM. kcat: printed Table 2 cell 44.4 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 44.4 s^(-1). kcat/Km: printed Table 2 cell 178 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell normalizes to 178.0 s^(-1)*mM^(-1). The exported kcat_over_km 177.6 s^(-1)*mM^(-1) is the exact quotient 44.4 / 0.25 of the same Table 2 cells, and the printed cell is that quotient carried to the precision the paper prints.

raw_value_unit_evidence: Table 2, protein row 'TxGH116 WT without N-term tag', substrate 'cellobiose': KM = 0.25 mM; kcat = 44.4 s^-1; printed kcat/KM = 178 mM^-1 s^-1.

row_label: Table 2, protein row 'TxGH116 WT without N-term tag' with substrate 'cellobiose'

substrate: cellobiose


substrate_name: 4-nitrophenyl beta-D-glucoside

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession F6BL85 and applied mutation signature R786H to reconstruct the assayed variant sequence.

substrate: 4-nitrophenyl beta-D-glucoside


sequence_variant_note: Resolved canonical sequence from UniProtKB:F6BL85 REST check on 2026-06-06; sequence version 1 and applied mutation signature D508H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:F6BL85 REST check on 2026-06-06; sequence version 1 and applied mutation signature R544W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:F6BL85 REST check on 2026-06-06; sequence version 1 and applied mutation signature D508N to reconstruct the assayed variant sequence.


substrate_name: laminaribiose

sequence_source: UniProtKB:F6BL85 REST check on 2026-06-06; sequence version 1

substrate: laminaribiose


sequence_source: UniProtKB:P0A0Z8 reviewed canonical FASTA fetched directly on 2026-06-06


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P0A0Z8 reviewed canonical FASTA using row mutation Y179A and applied mutation signature Y179A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P0A0Z8 reviewed canonical FASTA using row mutation F192A and applied mutation signature F192A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P0A0Z8 reviewed canonical FASTA using row mutation D211A and applied mutation signature D211A to reconstruct the assayed variant sequence.


sequence_source: Reconstructed from UniProtKB:P0A0Z8 reviewed canonical FASTA using row mutation Y179A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A0Z8 and applied mutation signature F193A to reconstruct the assayed variant sequence.

column_label: Table 1 (True kinetic parameters determined for wild-type and mutant CNS), row 'F193A'; column 'kcat (min^-1)' = 300; column 'Km(CTP) (uM)' = 52; column 'kcat/Km (uM^-1 min^-1) CTP' = 5.8; column 'Km(Neu5Ac) (uM)' = 780; column 'ka0 (uM)' = 310; column 'kcat/Km (uM^-1 min^-1) Neu5Ac' = 0.38.

raw_value_unit_evidence: Table 1, row F193A, substrate CTP: kcat = 300 min^-1; Km(CTP) = 52 uM; printed kcat/Km(CTP) = 5.8 uM^-1 min^-1.

row_label: Table 1, row F193A, substrate CTP (the kcat, Km(CTP) and kcat/Km(CTP) cells of that printed row)


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P0A0Z8 reviewed canonical FASTA using row mutation Q104A and applied mutation signature Q104A to reconstruct the assayed variant sequence.


sequence_source: Reconstructed from UniProtKB:P0A0Z8 reviewed canonical FASTA using row mutation Q104A


organism: Drosophila melanogaster

substrate_name: N-acetylneuraminic acid

sequence_source: UniProtKB:Q8IQV0 REST lookup on 2026-06-06

substrate: N-acetylneuraminic acid


organism: Mus musculus

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:Q99KK2 REST lookup on 2026-06-06

proof_lines: N-terminal domain and C-terminal domain of CMP-sialic acid synthetase, substrate N-acetylneuraminic acid

proof_lines: N-terminal domain of CMP-sialic acid synthetase, substrate N-acetylneuraminic acid

source_databases_merged: sabio_rk brenda skid


sequence_source: UniProtKB:P0A0Z8 REST lookup on 2026-06-06


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A0Z8 REST lookup on 2026-06-06 plus direct F193A substitution reconstruction and applied mutation signature F193A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A0Z8 and applied mutation signature N175A to reconstruct the assayed variant sequence.

column_label: Table 1 (True kinetic parameters determined for wild-type and mutant CNS), row 'N175A'; column 'kcat (min^-1)' = 1500; column 'Km(CTP) (uM)' = 270; column 'kcat/Km (uM^-1 min^-1) CTP' = 5.4; column 'Km(Neu5Ac) (uM)' = 1600; column 'ka0 (uM)' = 550; column 'kcat/Km (uM^-1 min^-1) Neu5Ac' = 0.93.

raw_value_unit_evidence: Table 1, row N175A, substrate CTP: kcat = 1500 min^-1; Km(CTP) = 270 uM; printed kcat/Km(CTP) = 5.4 uM^-1 min^-1.

row_label: Table 1, row N175A, substrate CTP (the kcat, Km(CTP) and kcat/Km(CTP) cells of that printed row)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A0Z8 REST lookup on 2026-06-06 plus direct N175A substitution reconstruction and applied mutation signature N175A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A0Z8 and applied mutation signature F192A to reconstruct the assayed variant sequence.

column_label: Table 1 (True kinetic parameters determined for wild-type and mutant CNS), row 'F192A'; column 'kcat (min^-1)' = 1200; column 'Km(CTP) (uM)' = 150; column 'kcat/Km (uM^-1 min^-1) CTP' = 7.9; column 'Km(Neu5Ac) (uM)' = 380; column 'ka0 (uM)' = 2400; column 'kcat/Km (uM^-1 min^-1) Neu5Ac' = 3.1.

raw_value_unit_evidence: Table 1, row F192A, substrate CTP: kcat = 1200 min^-1; Km(CTP) = 150 uM; printed kcat/Km(CTP) = 7.9 uM^-1 min^-1.

row_label: Table 1, row F192A, substrate CTP (the kcat, Km(CTP) and kcat/Km(CTP) cells of that printed row)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A0Z8 REST lookup on 2026-06-06 plus direct R173A substitution reconstruction and applied mutation signature R173A to reconstruct the assayed variant sequence.


organism: Brevibacillus brevis

substrate_name: L-phenylalanine

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

substrate: L-phenylalanine


organism: Brevibacterium linens


organism: Candida albicans


organism: Candida maltosa

proof_lines:
pH 8.6, 37°C, AAT I
AAT I, substrate inhibition
AAT I and III, substrate inhibition


organism: Escherichia coli

substrate_name: oxaloacetate

proof_lines: pH 8.0, 25°C, cosubstrate 2-oxoglutarate

substrate: oxaloacetate


proof_lines: pH 8.0, 25°C, single-turnover, wild-type enzyme


organism: Flavobacterium sp.

proof_lines: aromatic amino acid transferase from strain CB 60


organism: Klebsiella aerogenes

proof_lines:
cosubstrate 2-oxoglutarate
cosubstrate glutamate
cosubstrate tryptophan


organism: Methanococcus aeolicus

substrate_name: L-Tyrosine; 2-Oxoglutarate

proof_lines: pH 7.5, 37°C, cosubstrate: L-tyrosine, aromatic aminotransferase II

proof_lines: pH 7.5, 37°C, cosubstrate: L-phenylalanine, aromatic aminotransferase II

substrate: L-Tyrosine; 2-Oxoglutarate


organism: Pyrococcus furiosus

proof_lines: pH 7.6, 80°C, cosubstrate 2-oxoglutarate


proof_lines:
cosubstrate phenylalanine
pH 8.0. 37°C


organism: Trypanosoma brucei

substrate_name: alpha-ketomethiobutyrate

substrate: alpha-ketomethiobutyrate


organism: Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828)

substrate_name: Unknown

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

substrate: Unknown


enzyme_display_name: alpha,alpha-trehalase

organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

substrate_name: trehalose

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

enzyme: alpha,alpha-trehalase

substrate: trehalose


organism: Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)


organism: Homo sapiens

substrate_name: glucosylceramide (at 37 degrees Celsius and pH 6.0)

proof_lines: kcat is 0.43 min(-1) for the hydrolysis of glucosylceramide (PubMed:17595169). kcat<0.01 min(-1) for the hydrolysis of galactosylceramide (PubMed:17595169). kcat is 7.26 min(-1) for the hydrolysis of C6-NBD-glucosylceramide (PubMed:17595169


proof_lines: kcat is 2500 min(-1) for the hydrolysis of beta-D-glucosyl-(1->3)-O-lithocholate (PubMed:9111029). kcat is 1300 min(-1) for the hydrolysis of beta-D-glucosyl-(1->3)-O-chenodeoxycholate (PubMed:9111029). kcat is 4700 min(-1) for the hydrolys


enzyme_display_name: aromatic-L-amino-acid decarboxylase

organism: Bacillus atrophaeus

substrate_name: L-tryptophan

proof_lines: kcat is 6.7 sec(-1) with L-tryptophan as substrate (at 37 degrees Celsius) (PubMed:33713143). kcat is 7.0 sec(-1) with L-phenylalanine as substrate (at 30 degrees Celsius) (PubMed:33713143). kcat is 7.4 sec(-1) with L-phenylalanine as subst

enzyme: aromatic-L-amino-acid decarboxylase

substrate: L-tryptophan


organism: Vigna radiata


organism: Bacillus subtilis

substrate_name: GTP

proof_lines: pH 8.5, 37°C, recombinant enzyme, with 2-deoxyguanosine as acceptor substrate

proof_lines: pH 8.5, 37°C, recombinant enzyme, with GTP as donor substrate

substrate: GTP


organism: Bos taurus

substrate_name: deoxyinosine

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines: pH 7.4, 37°C, mitochondrial deoxyguanosine kinase

proof_lines: pH 7.5, 37°C, mitochondrial deoxyguanosine kinase

proof_lines: pH 7.4, 37°C, vs. deoxyguanosine, mitochondrial deoxyguanosine kinase

substrate: deoxyinosine


substrate_name: ATP

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

assay_conditions_summary: pH 7.6; cofactor ATP

proof_lines: pH 7.6, recombinant mutant E227K, with 2-deoxyguanosine

proof_lines: pH 7.6, recombinant mutant E227K, with 2-deoxyadenosine

substrate: ATP


proof_lines: pH 7.6, recombinant mutant R142K, with 2-deoxyguanosine


substrate_name: dioxolane guanosine

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines: pH 7.6, 37°C, recombinant deoxguanosine kinase, cosubstrate ATP

substrate: dioxolane guanosine


organism: Caulobacter vibrioides

substrate_name: DNA adenine

substrate: DNA adenine


organism: Cereibacter sphaeroides

sequence_source: UniProtKB:P14751; PMID:16464821 paper context


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14751 canonical sequence with PMID:16464821 S124D reconstruction and applied mutation signature S124D to reconstruct the assayed variant sequence.


organism: Enterobacter cloacae


organism: Escherichia coli

proof_lines: with specific sequence AAGCTT, at pH 7.0 and 37°C

proof_lines: in 100 mM Tris (pH 8.0), 1 mM EDTA, 1 mM dithiothreitol, and 0.2 mg/ml bovine serum albumin, at 22°C

proof_lines: with specific sequence AAGCTT/TTCGAA, at pH 7.0 and 37°C


organism: Geobacillus stearothermophilus

substrate_name: T7 DNA adenine

proof_lines: in 33 mM Tris-acetate, pH 7.9, 10 mM magnesium acetate, 66 mM potassium acetate, 1 mM dithiothreitol, at 55°C

substrate: T7 DNA adenine


enzyme_display_name: (R)-mandelonitrile lyase

organism: Granulicella tundricola (strain ATCC BAA-1859 / DSM 23138 / MP5ACTX9)

substrate_name: (R)-mandelonitrile (at pH 4.5 and at 25 degrees Celsius)

proof_lines: kcat is 0.03 sec(-1) with (R)-mandelonitrile as substrate (at pH 4.5 and at 25 degrees Celsius). kcat is 0.0075 sec(-1) with (R)-mandelonitrile as substrate (at pH 5.5 and at 5 degrees Celsius).

enzyme: (R)-mandelonitrile lyase


substrate_name: 2',3'-Cyclic GMP

substrate: 2',3'-Cyclic GMP


substrate_name: 2',3'-Cyclic AMP; H2O

substrate: 2',3'-Cyclic AMP; H2O


substrate_name: 2',3'-Cyclic AMP

substrate: 2',3'-Cyclic AMP


organism: Mus musculus

sequence_variant_note: Resolved canonical sequence from uniprot_accession_with_paper_mutation_reconstruction and applied mutation signature H230Q with inferred residue-numbering offset +20 to reconstruct the assayed variant sequence.

proof_lines: mutant H230Q, pH and temperature not specified in the publication

proof_lines: mutant enzyme H230Q, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession_with_paper_mutation_reconstruction and applied mutation signature V321A with inferred residue-numbering offset +20 to reconstruct the assayed variant sequence.

proof_lines: mutant V321A, pH and temperature not specified in the publication

proof_lines: mutant enzyme V321A, pH and temperature not specified in the publication


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

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession_with_paper_mutation_reconstruction and applied mutation signature H230S with inferred residue-numbering offset +20 to reconstruct the assayed variant sequence.

proof_lines: mutant H230S, pH and temperature not specified in the publication

proof_lines: mutant enzyme H230S, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession_with_paper_mutation_reconstruction and applied mutation signature H309S with inferred residue-numbering offset +20 to reconstruct the assayed variant sequence.

proof_lines: mutant H309S, pH and temperature not specified in the publication

proof_lines: mutant enzyme H309S, pH and temperature not specified in the publication


organism: Arabidopsis thaliana

substrate_name: Appr>p

substrate: Appr>p


substrate_name: AMP

substrate: AMP


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: adenosine 1',2'-cyclic phosphate

assay_conditions_summary: cofactor ADP

substrate: adenosine 1',2'-cyclic phosphate


assay_conditions_summary: pH 5.2; 310.15 K; cofactor ATP

proof_lines: pH 5.2, 37°C, at concentrations below 0.5 mM


organism: Rattus norvegicus

substrate_name: ATP; Deoxyguanosine

substrate: ATP; Deoxyguanosine


organism: Sus scrofa

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines:
pH 8.0, 37°C
ATP in form of MgATP2-


enzyme_display_name: riboflavin kinase

assay_conditions_summary: cofactor FMN

enzyme: riboflavin kinase


substrate_name: roseoflavin

substrate: roseoflavin


substrate_name: riboflavin

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

substrate: riboflavin


sequence_source: UniProtKB REST direct lookup for P16330


organism: Saccharomyces cerevisiae

substrate_name: 2',3'-Cyclic GMP; H2O

sequence_source: UniProtKB REST direct lookup for P53314; matches reusable canonical sequence cache

substrate: 2',3'-Cyclic GMP; H2O


organism: Triticum aestivum

sequence_source: UniProtKB REST direct lookup for P62809


organism: Nicotiana tabacum


proof_lines:
pH 8, 37°C
pH 8.0, 37°C
pH 8.0, 37°C, against riboflavin


enzyme_display_name: choline kinase

organism: Caenorhabditis elegans

substrate_name: choline

assay_conditions_summary: pH 10; 310.15 K; cofactor ATP

enzyme: choline kinase

substrate: choline


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P16330-2; reconstructed_variant_from PMID:26563764 and applied mutation signature Y168A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y168A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P16330-2; reconstructed_variant_from PMID:26563764 and applied mutation signature R307Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R307Q, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P16330-2; reconstructed_variant_from PMID:26563764 and applied mutation signature P296G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme P296G, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P16330-2; reconstructed_variant_from PMID:26563764 and applied mutation signature F235A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F235A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P16330-2; reconstructed_variant_from PMID:26563764 and applied mutation signature T232A to reconstruct the assayed variant sequence.

proof_lines: Kcat_Km less than 10 1/sec*mM, mutant enzyme T232A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P16330-2; reconstructed_variant_from PMID:26563764 and applied mutation signature P225G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme P225G, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P16330-2; reconstructed_variant_from PMID:26563764 and applied mutation signature F235L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F235L, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P16330-2; reconstructed_variant_from PMID:26563764 and applied mutation signature Y168S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y168S, pH and temperature not specified in the publication


organism: Corynebacterium ammoniagenes

sequence_variant_note: Resolved canonical sequence from RCSB 3ZUG entity 1 sequence mapped to UniProt Q59263 by SIFTS and applied mutation signature E268D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 310.15 K; cofactor FAD

proof_lines: apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q59263 using PMID 22892871 N210D source note and same-paper RCSB 3ZUG/Q59263 CaFADS anchor and applied mutation signature N210D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines: apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2


sequence_source: UniProt Q59263, supported by same-paper RCSB 3ZUG/Q59263 CaFADS mapping for PMID 22892871

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

assay_conditions_summary: pH 7; 310.15 K; cofactor FMN

proof_lines: apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2


sequence_source: UniProt Q59263 reference to PMID 3023344 for catalytic activity/function

assay_conditions_summary: cofactor FAD


organism: Megasphaera elsdenii

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


organism: Neurospora crassa

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

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP

proof_lines:
pH 8.5, 30°C
ATP in form of MgATP2-


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from UniProt Q16854 FASTA with UniProt natural variant VAR_023789 and PubMed 15639197 support and applied mutation signature L250S to reconstruct the assayed variant sequence.

proof_lines: pH 7.6, mutant L250S, with 2-deoxyadenosine

proof_lines: pH 7.6, mutant L250S, with 2-deoxyguanosine


sequence_source: UniProt Q16854 FASTA; DGUOK_HUMAN paper references include PubMed 15639197

proof_lines: pH 7.6, recombinant wild-type enzyme, with 2-deoxyguanosine


sequence_variant_note: Resolved canonical sequence from UniProt Q16854 FASTA with UniProt natural variant VAR_076983 and PubMed 17073823 support and applied mutation signature L266R to reconstruct the assayed variant sequence.


sequence_source: UniProt Q16854 FASTA and UniProt natural variant VAR_076980 were checked, but row-specific variant sequence was not accepted because the selected source contexts are mixed.

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

proof_lines: patient with double mutation N46S/L266, pH 7.4, 37°C


organism: Lactobacillus acidophilus

substrate_name: Deoxyguanosine; ATP

assay_conditions_summary: pH 8; 293.15 K; cofactor ATP

proof_lines:
pH 8.0, 20°C
pH 8.0, 20°C, vs. ATP
pH 8.0, 20°C, vs. deoxyguanosine

substrate: Deoxyguanosine; ATP


proof_lines: SABIO-RK modifier species: deoxyguanosine kinase(Enzyme) mutant R79K:dGK


enzyme_display_name: beta-mannosidase

organism: Phlebia radiata

substrate_name: p-nitrophenyl-beta-D-mannoside

proof_lines:
isozyme GM-1
isozyme OT-1
isozyme GM-2

enzyme: beta-mannosidase

substrate: p-nitrophenyl-beta-D-mannoside


organism: Aspergillus niger


organism: Bacteroides thetaiotaomicron

substrate_name: Unknown

substrate: Unknown


organism: Hordeum vulgare

substrate_name: Cellotetraose

substrate: Cellotetraose


substrate_name: Cellopentaose

substrate: Cellopentaose


substrate_name: cellotriose

substrate: cellotriose


substrate_name: Laminaritriose

substrate: Laminaritriose


substrate_name: laminaribiose

substrate: laminaribiose


organism: Pyrococcus horikoshii

substrate_name: 4-nitrophenyl beta-D-mannopyranoside / beta-D-glucopyranoside / beta-D-galactopyranoside

sequence_source: UniProtKB O58237 direct lookup; source accession maps to P. horikoshii PH0501.


substrate_name: 4-nitrophenyl beta-D-galactopyranoside

substrate: 4-nitrophenyl beta-D-galactopyranoside


substrate_name: 4-nitrophenyl beta-D-glucopyranoside

substrate: 4-nitrophenyl beta-D-glucopyranoside


substrate_name: 4-nitrophenyl beta-D-mannopyranoside

substrate: 4-nitrophenyl beta-D-mannopyranoside


substrate_name: p-Nitrophenyl-beta-D-mannoside; H2O

sequence_source: UniProtKB Q4FZV0 direct lookup; reviewed MANBA_RAT EC 3.2.1.25 entry.

substrate: p-Nitrophenyl-beta-D-mannoside; H2O


organism: Thermobifida fusca

sequence_source: UniProtKB Q8KLI9 direct lookup; EC 3.2.1.25 beta-mannosidase/manB entry.


organism: Thermococcus kodakarensis

substrate_name: 4-nitrophenyl beta-D-mannopyranoside / beta-D-glucopyranoside / beta-D-fucopyranoside

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9YGB8 direct lookup with direct D206N substitution. and applied mutation signature D206N to reconstruct the assayed variant sequence.

proof_lines: 80°C, pH is not specified in the publication, mutant enzyme D206N


sequence_source: UniProtKB:Q9YGB8 direct REST lookup on 2026-06-06

proof_lines: 80°C, pH is not specified in the publication, wild-type


organism: Thermotoga maritima

sequence_source: UniProtKB:Q9X1V9 direct REST lookup on 2026-06-06


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt Q22942 canonical sequence after direct residue check and applied mutation signature R149K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt Q22942 canonical sequence after direct residue check and applied mutation signature N308A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt Q22942 canonical sequence after direct residue check and applied mutation signature E151A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt Q22942 canonical sequence after direct residue check and applied mutation signature S86A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt Q22942 canonical sequence after direct residue check and applied mutation signature N260A to reconstruct the assayed variant sequence.


substrate_name: H2O; p-Nitrophenyl-beta-D-glucoside

sequence_source: UniProtKB:B5A496 REST FASTA, checked 2026-06-06

substrate: H2O; p-Nitrophenyl-beta-D-glucoside


substrate_name: cellohexaose

substrate: cellohexaose


substrate_name: Cellobiose

substrate: Cellobiose


substrate_name: p-nitrophenyl-beta-mannopyranoside

proof_lines: kcat is 4048 min(-1) with p-nitrophenyl-beta-mannopyranoside as substrate.

substrate: p-nitrophenyl-beta-mannopyranoside


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

assay_conditions_summary: pH 7

proof_lines: kcat is 79.2 min(-1) with p-nitrophenyl-beta-mannopyranoside as substrate.


organism: Thermothelomyces thermophilus

proof_lines: kcat is 15 sec(-1) with p-nitrophenyl-beta-mannopyranoside as substrate.


sequence_source: UniProtKB O58237 FASTA direct accession check supplies only the canonical PH0501 sequence; row-specific variant sequence remains unresolved.


sequence_source: UniProtKB O58237 FASTA direct accession check on 2026-06-06; PH0501 from Pyrococcus horikoshii OT-3.


substrate_name: choline

substrate: choline


organism: Culex quinquefasciatus

substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Lathyrus oleraceus


organism: Mus musculus

mutation_signature: N-terminal truncated enzyme version of CK-beta N-terminal truncated enzyme version of CK-beta

mutation_type: truncation


organism: Oryctolagus cuniculus


organism: Plasmodium falciparum

assay_conditions_summary: pH 8.8; 310.15 K; cofactor ATP

proof_lines: in 100 mM Tris/HCl, 6 mM MgCl2, 5 mM ATP, pH 8.8, at 37°C


organism: Rattus norvegicus

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

proof_lines:
kidney enzyme
liver enzyme
pH 8.5, 37°C


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 9.5; 303.15 K; cofactor ATP

proof_lines:
per subunit
pH 9.5, 30°C
pH 8.5, 25°C


organism: Secale cereale

substrate_name: ATP; Choline

substrate: ATP; Choline


organism: Toxoplasma gondii


organism: Caenorhabditis elegans

sequence_variant_note: Resolved canonical sequence from UniProt:Q22942; PMID:14960577; RCSB:1NW1 and applied mutation signature N308D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:Q22942; PMID:14960577; RCSB:1NW1 and applied mutation signature E125Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:Q22942; PMID:14960577; RCSB:1NW1 and applied mutation signature E303A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:Q22942; PMID:14960577; RCSB:1NW1 and applied mutation signature E303Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:Q22942; PMID:14960577; RCSB:1NW1 and applied mutation signature N87A to reconstruct the assayed variant sequence.


organism: Trypanosoma brucei

assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP

proof_lines: pH 7.8, 37°C, assay with recombinantly expressed enzyme


organism: Acetivibrio thermocellus

substrate_name: CTP

proof_lines: at 50°C, 10 mM MnCl2, 50 mM Tris buffer (pH 9.5)

substrate: CTP


organism: Bos taurus

substrate_name: N-acetylneuraminate

substrate: N-acetylneuraminate


organism: Cricetulus griseus


organism: Equus caballus

substrate_name: N-glycolylneuraminate

proof_lines:
37°C, crude enzyme extract
pH 7, 37°C
pH 9, 37°C

substrate: N-glycolylneuraminate


organism: Escherichia coli

proof_lines:
pH 9.0, 37°C
at 37°C


organism: [Haemophilus] ducreyi

proof_lines:
pH 7.1, 25°C
at pH 7.1 and 37°C
pH 7.1, 37°C


organism: Homo sapiens


organism: Mannheimia haemolytica

substrate_name: N-acetylneuraminate methyl ester

proof_lines:
pH 9.0, 37°C, reaction with CTP
pH 9.0, 37°C, reaction with CDP
pH 9.0, 37°C, reaction with UTP

substrate: N-acetylneuraminate methyl ester


organism: Neisseria meningitidis

substrate_name: N-acylneuraminate

substrate: N-acylneuraminate


sequence_variant_note: Resolved canonical sequence from uniprot_q22942_direct_lookup and applied mutation signature E134A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_q22942_direct_lookup and applied mutation signature E125D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_q22942_direct_lookup and applied mutation signature H253A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_q22942_direct_lookup and applied mutation signature C252S to reconstruct the assayed variant sequence.


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

proof_lines: wild type enzyme including His-tag, pH 10, 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_q22942_direct_lookup and applied mutation signature W387A to reconstruct the assayed variant sequence.


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


organism: Oncorhynchus mykiss

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


organism: Pasteurella multocida


organism: Pelophylax lessonae


organism: Photobacterium leiognathi


organism: Rattus norvegicus


substrate_name: p-nitrophenyl octanoate

substrate: p-nitrophenyl octanoate


substrate_name: p-nitrophenyl caproate

proof_lines: presence of 0.05 mM/l resveratrol, pH 7.4, 30°C

substrate: p-nitrophenyl caproate


organism: Rattus sp.

substrate_name: cholesteryl oleate

proof_lines:
native cholesterol esterase
parenchymal cells
non-parenchymal cells

substrate: cholesteryl oleate


substrate_name: lipoyl 4-aminobenzoate

substrate: lipoyl 4-aminobenzoate


organism: Saccharomyces cerevisiae

proof_lines:
at pH 6.6
at pH 4.4


substrate_name: 4-nitrophenyl acetate

sequence_source: UniProtKB:P51025 direct lookup from PMID 16567800 FrmB context

substrate: 4-nitrophenyl acetate


substrate_name: Alpha-naphthyl acetate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P33018 direct lookup plus D218A reconstruction and applied mutation signature D218A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 37°C, recombinant YeiG mutant D218A

substrate: Alpha-naphthyl acetate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P33018 direct lookup plus C54A reconstruction and applied mutation signature C54A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 37°C, recombinant YeiG mutant C54A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P33018 direct lookup plus D199A reconstruction and applied mutation signature D199A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 37°C, recombinant YeiG mutant D199A


sequence_source: UniProtKB:P33018 direct lookup from PMID 16567800 YeiG context

proof_lines: pH 8.0, 37°C, recombinant wild-type YeiG


sequence_variant_note: Resolved canonical sequence from UniProtKB:P33018 direct lookup plus D80A reconstruction and applied mutation signature D80A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 37°C, recombinant YeiG mutant D80A


enzyme_display_name: arginine decarboxylase

substrate_name: L-arginine

sequence_source: UniProtKB:A3DGQ8 direct REST lookup on 2026-06-06

enzyme: arginine decarboxylase

substrate: L-arginine


organism: Avena sativa

substrate_name: L-Arginine

sequence_source: UniProtKB:P22220 direct REST lookup on 2026-06-06

substrate: L-Arginine


proof_lines:
untagged ADC
His-tagged ADC


organism: Chlamydophila pneumoniae

sequence_source: UniProtKB:Q9Z6M7 direct REST lookup on 2026-06-06


sequence_source: UniProtKB:P28629 direct REST lookup on 2026-06-06

proof_lines:
pH 5.2, 37°C, inducible ArgDC
pH 8.4, 37°C, constitutive ArgDC


sequence_source: UniProtKB:P21170 direct REST lookup on 2026-06-06


organism: Glycine max

substrate_name: S-Adenosyl-L-methionine

sequence_source: UniProtKB:Q8S3F8 direct REST lookup on 2026-06-06

substrate: S-Adenosyl-L-methionine


organism: Streptococcus sp.


organism: Sus scrofa

substrate_name: CTP; N-Acylneuraminate

proof_lines:
37°C, crude enzyme extract
pH 9.0, 37°C

substrate: CTP; N-Acylneuraminate


organism: Vibrio cholerae

sequence_source: NCBI Protein WP_000064388.1 from PMID 31205019; RCSB PDB 6IFI/6IFD confirm Vibrio cholerae CMP-N-acetylneuraminate synthetase structures. Native NCBI sequence used, not the N-terminal His-tagged PDB construct sequence.


organism: Acinetobacter sp.

substrate_name: cholesteryl linoleate

substrate: cholesteryl linoleate


organism: Bos taurus

proof_lines: in mixed emulsion of cholesteryl oleate, phosphatidylcholine and taurocholic acid


organism: Homo sapiens


organism: Limtongozyma cylindracea

substrate_name: 4-nitrophenyl butyrate

proof_lines: CRL3, pH 7.4, 25°C, in presence of taurocholate

substrate: 4-nitrophenyl butyrate


organism: Mus musculus


organism: Ophiostoma piceae

substrate_name: cholesteryl palmitate

substrate: cholesteryl palmitate


organism: Oryctolagus cuniculus

substrate_name: 4-methylumbelliferyl oleate

proof_lines:
for neutral CEase
for CEase-ISF II

substrate: 4-methylumbelliferyl oleate


organism: Streptomyces griseus

substrate_name: 4-nitrophenyl palmitate

substrate: 4-nitrophenyl palmitate


organism: Streptomyces sp.

substrate_name: p-nitrophenyl laurate

substrate: p-nitrophenyl laurate


assay_conditions_summary: pH 7.4; 298.15 K; buffer sodium phosphate

proof_lines: pH 7.4, 25°C, in presence of taurocholate

proof_lines: in sodium phosphate buffer (0.1 M, pH 7.0), at 25°C


organism: Agrobacterium tumefaciens

substrate_name: naphthalen-1-yl n-butanoate

sequence_source: RCSB 3E4D entity 1 / UniProtKB A9CJ11 paper-linked sequence

assay_conditions_summary: pH 8; buffer Tris-HCl

substrate: naphthalen-1-yl n-butanoate


organism: Arabidopsis thaliana

substrate_name: fluorescein diacetate

sequence_source: UniProtKB Q8LAS8 linked to PMID 11888210

proof_lines:
recombinant enzyme, pH 7.2, 37°C
recombinant enzyme, pH 7.5, 37°C
pH 7.0, 25°C

substrate: fluorescein diacetate


organism: [Candida] boidinii

substrate_name: S-formylglutathione

substrate: S-formylglutathione


organism: Helicobacter pylori


organism: Methanocaldococcus jannaschii


organism: Paramecium bursaria chlorella virus 1


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q84527 plus E296D reconstruction and applied mutation signature E296D to reconstruct the assayed variant sequence.


organism: Unknown

substrate_name: L-Arg

substrate: L-Arg


organism: Saccharomyces cerevisiae

substrate_name: S-Lactoylglutathione

substrate: S-Lactoylglutathione


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


proof_lines: mutant H160I oxidized form with catalase, pH 7.4, 22°C

proof_lines: mutant H160I oxidized form, pH 7.4, 22°C


organism: Acinetobacter baumannii

sequence_source: UniProtKB REST direct lookup accession A0A0R0VXX6


organism: Enterobacter cloacae

sequence_source: UniProtKB REST direct lookup accession P33038

proof_lines: pH and temperature not specified in the publication


organism: Escherichia coli

sequence_source: UniProtKB REST direct lookup accession P0A749


organism: Fusobacterium nucleatum subsp. nucleatum

substrate_name: UDP-N-acetyl-alpha-D-glucosamine

sequence_source: UniProtKB REST direct lookup accession Q8RIQ1

substrate: UDP-N-acetyl-alpha-D-glucosamine


organism: Haemophilus influenzae

sequence_source: UniProtKB REST direct lookup accession P45025


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB REST direct lookup accession P9WJM1


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB REST direct lookup accession Q9HVW7


organism: Staphylococcus aureus

sequence_source: UniProtKB REST direct lookup accession P65456


substrate_name: L-Lysine

substrate: L-Lysine


substrate_name: L-Arginine

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

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

substrate: L-Arginine


organism: Persea americana

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


organism: Saccharolobus solfataricus


substrate_name: L-arginine

substrate: L-arginine


organism: Selenomonas ruminantium

substrate_name: L-lysine

substrate: L-lysine


organism: Streptococcus pneumoniae

substrate_name: L-ornithine

substrate: L-ornithine


organism: Sulfolobus solfataricus


sequence_source: UniProtKB reviewed accession Q9UWU1 live lookup on 2026-06-06; sequence version 1; same sequence was present in accession_5fe787b4974d4582.


organism: Trypanosoma brucei

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


organism: Vibrio vulnificus


substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


substrate_name: phosphoenolpyruvate

substrate: phosphoenolpyruvate


assay_conditions_summary: pH 7.5; cofactor ADP

proof_lines: the calculated value for UDP is 40 times higher than that of ADP


assay_conditions_summary: pH 6

proof_lines:
mutant C115D, pH 6.0
mutant C115D, pH 8.0
mutant C115D


organism: Escherichia coli (strain K12)

substrate_name: UDP-N-acetylglucosamine

substrate: UDP-N-acetylglucosamine


organism: Chlamydia pneumoniae


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)


enzyme_display_name: dihydroorotase

organism: Aquifex aeolicus

substrate_name: L-Dihydroorotate

enzyme: dihydroorotase

substrate: L-Dihydroorotate


substrate_name: N-carbamoyl-L-aspartate

proof_lines: pH 8.0, 74°C, recombinant isolated DHO mutant DHO E179V

proof_lines: pH 8.0, 74°C, recombinant DHO-ATC complex with mutant DHO E179V

substrate: N-carbamoyl-L-aspartate


proof_lines: pH 8.0, 74°C, recombinant DHO-ATC complex with mutant DHO E183V

proof_lines: pH 8.0, 74°C, recombinant isolated DHO mutant DHO E183V


sequence_variant_note: Resolved canonical sequence from uniprot_accession:O66990 and applied mutation signature C181A to reconstruct the assayed variant sequence.


proof_lines: pH 8.0, 74°C, recombinant wild-type DHO-ATC complex


proof_lines: pH 8.0, 74°C, recombinant DHO-ATC complex with mutant DHO C181A


substrate_name: Phosphoenolpyruvate

substrate: Phosphoenolpyruvate


substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


substrate_name: L-Dihydroorotate; H2O

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

substrate: L-Dihydroorotate; H2O


organism: Escherichia coli

substrate_name: N-(aminocarbonyl)-L-aspartic acid; carbamoyl aspartate

sequence_source: UniProtKB P05020 direct FASTA/REST lookup on 2026-06-06

proof_lines:
wild type enzyme, at pH 5.8
wild type, Zn/Zn-dihydroorotase, pH 5.8


substrate_name: N-Carbamoyl-L-aspartate; H2O; L-Dihydroorotate; N-(aminocarbonyl)-L-aspartic acid

sequence_variant_note: Resolved canonical sequence from UniProtKB P05020 direct lookup plus RCSB 1XGE/PubMed 17711307 mature-chain offset reconstruction on 2026-06-06 and applied mutation signature T110V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: dihydroorotase(Enzyme) mutant T110V


substrate_name: N-Carbamoyl-L-aspartate; L-Dihydroorotate; H2O; N-(aminocarbonyl)-L-aspartic acid

sequence_variant_note: Resolved canonical sequence from UniProtKB P05020 direct lookup plus RCSB 1XGE/PubMed 17711307 mature-chain offset reconstruction on 2026-06-06 and applied mutation signature T110S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: dihydroorotase(Enzyme) mutant T110S


sequence_source: UniProtKB P05020 direct lookup plus RCSB 1XGE/PubMed 17711307 mature-chain offset reconstruction on 2026-06-06

sequence_variant_note: Mutation signature T109S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: dihydroorotase(Enzyme) mutant T109S

substrate: N-Carbamoyl-L-aspartate; H2O; L-Dihydroorotate; N-(aminocarbonyl)-L-aspartic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB P05020 direct lookup plus RCSB 1XGE/PubMed 17711307 mature-chain offset reconstruction on 2026-06-06 and applied mutation signature T110A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: dihydroorotase(Enzyme) mutant T110A


organism: Homo sapiens

sequence_source: UniProtKB P27708 direct REST lookup and listed reuse cache on 2026-06-06


substrate_name: N-Carbamoyl-L-aspartate

substrate: N-Carbamoyl-L-aspartate


substrate_name: H2O; L-Dihydroorotate; H2O; L-Dihydroorotate; N-Carbamoyl-L-aspartate


sequence_source: UniProtKB:P65907 direct FASTA/JSON lookup on 2026-06-06


substrate_name: (S)-dihydroorotate

proof_lines: pH 8.3, 25°C, recombinant detagged enzyme

substrate: (S)-dihydroorotate


organism: Toxoplasma gondii

substrate_name: dihydroorotate

sequence_source: UniProtKB:Q8MXA5 direct FASTA/JSON lookup on 2026-06-06

proof_lines:
purified recombinant enzyme, at 37°C
purified recombinant protein

substrate: dihydroorotate


organism: Klebsiella pneumoniae


organism: Leishmania donovani


proof_lines:
pH 6.0, 25°C, recombinant enzyme
pH 8.0, 25°C, recombinant enzyme


organism: Mesocricetus auratus


organism: Mus musculus


sequence_source: UniProtKB direct accession lookup, fetched 2026-06-06


organism: Bacillus anthracis

proof_lines: pH 8.3, temperature not specified in the publication, recombinant wild-type enzyme

proof_lines: pH 5.8, temperature not specified in the publication, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup, fetched 2026-06-06 and applied mutation signature N93A to reconstruct the assayed variant sequence.

proof_lines: pH 5.8, temperature not specified in the publication, recombinant mutant N93A


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

proof_lines:
Raw SKiD Env: Temp=-----, pH=8.3
Raw SKiD Env: Temp=-----, pH=5.8


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup, fetched 2026-06-06 and applied mutation signature D250E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: dihydroorotase(Enzyme) mutant D250E


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup, fetched 2026-06-06 and applied mutation signature D250S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: dihydroorotase(Enzyme) mutant D250S


assay_conditions_summary: pH 8

proof_lines:
Zn/Zn-dihydroorotase, pH 8.0
Cd/Cd-dihydroorotase, pH 8.0
Co/Co-dihydroorotase, pH 8.0


sequence_variant_note: Mutation signature R20K could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: dihydroorotase(Enzyme) mutant R20K


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


organism: Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)

assay_conditions_summary: buffer not captured in selected packet


enzyme_display_name: diamine N-acetyltransferase

organism: Pseudomonas aeruginosa

substrate_name: spermidine

sequence_source: UniProtKB:Q9I1K2 REST direct accession lookup; sequence version from live record checked 2026-06-06

enzyme: diamine N-acetyltransferase

substrate: spermidine


organism: Staphylococcus aureus

sequence_source: UniProtKB:A0A0H2XGJ0 REST direct accession lookup; sequence version from live record checked 2026-06-06


substrate_name: spermine

smiles: NCCCNCCCCNCCCN

substrate: spermine


smiles: NCCCCNCCCN


sequence_source: UniProtKB:U5NVV0 REST direct accession lookup; sequence version from live record checked 2026-06-06

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines: no pre-incubation with spermidine, at pH 8.0 and 37°C

proof_lines: assayed after pre-incubation with spermidine, at pH 8.0 and 37°C

proof_lines: no pre-incubation with spermine, at pH 8.0 and 37°C


organism: Streptomyces sp.

substrate_name: acetyl-CoA

sequence_source: UniProtKB:D2CFQ9 REST direct accession lookup; sequence version from live record checked 2026-06-06

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

substrate: acetyl-CoA


substrate_name: D-glucosamine 6-phosphate

substrate: D-glucosamine 6-phosphate


organism: Bacillus subtilis (strain 168)

substrate_name: AcCoA (at pH 9 and 37 degrees Celsius)

assay_conditions_summary: pH 9

proof_lines: kcat is 21.9 min(-1) for acetyltransferase activity with AcCoA as substrate (at pH 9 and 37 degrees Celsius). kcat is 19.1 min(-1) for acetyltransferase activity with spermine as substrate (at pH 9 and 37 degrees Celsius). kcat is 7.1 min(-

substrate: AcCoA (at pH 9 and 37 degrees Celsius)


substrate_name: putrescine

proof_lines: kcat is 0.0023 sec(-1) with putrescine as substrate (PubMed:15283699). kcat is 0.0072 sec(-1) with spermidine as substrate (PubMed:15283699). kcat is 0.0020 sec(-1) with spermine as substrate (PubMed:15283699). kcat is 0.0137 sec(-1) with 1

substrate: putrescine


substrate_name: acetyl-coenzyme A

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 8.7 sec(-1) with spermidine as substrate (PubMed:15283699). kcat is 5 sec(-1) with spermine as substrate (PubMed:15283699).

substrate: acetyl-coenzyme A


organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

substrate_name: Unknown

proof_lines: kcat is 42 min(-1) for acetyltransferase activity with acetylspermidine as substrate (at pH 8.3). kcat is 31 min(-1) for acetyltransferase activity with AcCoA as substrate (at pH 8.3).

substrate: Unknown


organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)

substrate_name: spermine (in the presence of 100 uM AcCoA at pH 9 and 37 degrees Celsius)

proof_lines: kcat is 16.8 sec(-1) for acetyltransferase activity with AcCoA as substrate (in the presence of 500 uM spermine at pH 9 and 37 degrees Celsius). kcat is 6.79 sec(-1) for acetyltransferase activity with spermine as substrate (in the presence


proof_lines: kcat is 1.9 sec(-1) with dihydroorotate as substrate. kcat is 2.1 sec(-1) with carbamoyl aspartate as substrate.


organism: Cryptosporidium parvum (strain Iowa II)


organism: Escherichia coli (strain K12)

substrate_name: AcCoA (in the presence of 3 mM spermidine at pH 7.5 and 37 degrees Celsius)


organism: Paramecium bursaria Chlorella virus 1


substrate_name: poly-L-lysine

substrate: poly-L-lysine


organism: Vibrio cholerae serotype O1

sequence_source: UniProtKB:Q9KL03 plus source mutation note F149A

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.


sequence_source: UniProtKB:Q9KL03 plus source mutation note F149G

sequence_variant_note: Mutation signature F149G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9KL03 plus source mutation note N152L and applied mutation signature N152L to reconstruct the assayed variant sequence.


organism: Bacillus thuringiensis

sequence_source: UniProt REST direct accession lookup for A0A437SL45

proof_lines: at pH 7.8 and 37°C, enzyme is preincubated with polyamine prior to performing kinetics


organism: Cryptosporidium parvum

substrate_name: Acetyl-CoA; Spermine

sequence_source: UniProt REST direct accession lookup for Q5CPU3

substrate: Acetyl-CoA; Spermine


substrate_name: Spermine

substrate: Spermine


substrate_name: Acetyl-CoA

substrate: Acetyl-CoA


organism: Danio rerio

sequence_source: UniProt REST direct accession lookup for Q6GQM2

proof_lines: isozyme ssat1b, pH and temperature not specified in the publication

proof_lines: isozyme ssat1a, pH and temperature not specified in the publication


organism: Homo sapiens

sequence_source: UniProt REST direct accession lookup for P21673

proof_lines: pH and temperature not specified in the publication

proof_lines: measured at fixed saturating concentrations of acetyl-CoA


organism: Mus musculus

substrate_name: Spermine; Acetyl-CoA

sequence_source: UniProt REST direct accession lookup for P48026

substrate: Spermine; Acetyl-CoA


organism: Physcomitrium patens

substrate_name: L-lysine

sequence_source: UniProt REST direct accession lookup for A0A2K1KKM6

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

proof_lines: with 1,3-diaminopropane as cosubstrate, at pH 7.5 and 30°C

substrate: L-lysine


organism: Enterococcus faecalis

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


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


organism: Mammalia


organism: Ascaris suum


organism: Bacillus subtilis

substrate_name: aminopropylcadaverine

sequence_source: UniProtKB P21340 from direct lit_pubmed:16210326 + ec:2.3.1.57 + Bacillus subtilis lookup

assay_conditions_summary: pH 9; cofactor CoA

proof_lines:
pH 9
pH 9, cosubstrate: spermine

substrate: aminopropylcadaverine


organism: [Candida] boidinii

substrate_name: sym-norspermidine

substrate: sym-norspermidine


organism: Cricetulus griseus

substrate_name: spermidine

proof_lines: pH 7.8, 30°C, recombinant wild-type enzyme


proof_lines: pH 7.8, 30°C, recombinant mutant L156F enzyme


substrate_name: spermine

sequence_source: UniProtKB Q5CPU3 from direct lit_pubmed:17289169 + ec:2.3.1.57 + Cryptosporidium parvum lookup


substrate_name: dihydroorotate

proof_lines: kcat is 127 sec(-1) with dihydroorotate as substrate and 195 sec(-1) with N-carbamoyl-DL-aspartate as substrate (PubMed:6142052). kcat is 100 sec(-1) with dihydroorotate as substrate and 160 sec(-1) with carbamoyl aspartate as substrate in

substrate: dihydroorotate


enzyme_display_name: 3',5'-cyclic-GMP phosphodiesterase

proof_lines: recombinant human cone PDE6C, pH and temperature not specified in the publication

enzyme: 3',5'-cyclic-GMP phosphodiesterase


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


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

sequence_source: UniProtKB O70628 direct lookup on 2026-06-06; reviewed PDE9A_MOUSE canonical sequence.


organism: Plasmodium falciparum

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


sequence_source: UniProtKB Q2V2M6 direct lookup on 2026-06-06 resolved to primary Q8I5V4/PDEA_PLAF7 canonical sequence.


organism: Rattus norvegicus

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-GMP phosphodiesterase(Enzyme) wildtype His-tagged splice variant PDE11A4

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-GMP phosphodiesterase(Enzyme) wildtype His-tagged splice variant PDE11A3

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-GMP phosphodiesterase(Enzyme) wildtype His-tagged splice variant PDE11A2

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


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

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-GMP phosphodiesterase(Enzyme) mutant His-tagged truncated PDE11At


sequence_source: UniProtKB O54735 direct lookup on 2026-06-06; reviewed PDE5A_RAT canonical sequence.

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


substrate_name: cGMP

sequence_variant_note: Resolved canonical sequence from UniProt O76074 FASTA fetched 2026-06-06; PMID 17979301 and selected source records provide the row context. and applied mutation signature Q817A to reconstruct the assayed variant sequence.

substrate: cGMP


sequence_variant_note: Resolved canonical sequence from UniProt O76074 FASTA fetched 2026-06-06; PMID 17979301 and selected source records provide the row context. and applied mutation signature Y612F to reconstruct the assayed variant sequence.


sequence_source: UniProt O76074 FASTA fetched 2026-06-06; PMID 17979301 and selected source records provide the row context.


sequence_variant_note: Resolved canonical sequence from UniProt O76074 FASTA fetched 2026-06-06; PMID 17979301 and selected source records provide the row context. and applied mutation signature L765A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O76074 FASTA fetched 2026-06-06; PMID 17979301 and selected source records provide the row context. and applied mutation signature F820A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O76074 FASTA fetched 2026-06-06; PMID 17979301 and selected source records provide the row context. and applied mutation signature H613A to reconstruct the assayed variant sequence.


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

sequence_variant_note: Resolved canonical sequence from UniProt O76083-2 FASTA fetched 2026-06-06; PMID 21483814 and selected source records provide the row context. and applied mutation signature Q453E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-GMP phosphodiesterase(Enzyme) mutant Q453E

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


substrate_name: 3',5'-Cyclic AMP

sequence_variant_note: Resolved canonical sequence from UniProt O76083-2 FASTA fetched 2026-06-06; PMID 21483814 and selected source records provide the row context. and applied mutation signature E406A to reconstruct the assayed variant sequence.

substrate: 3',5'-Cyclic AMP


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

sequence_source: UniProtKB Q9HCR9 direct accession lookup

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


proof_lines: SABIO-RK modifier species: 3',5'-cyclic-GMP phosphodiesterase(Enzyme) wildtype His-tagged splice variant PDE11A1


proof_lines:
splice variant PDE9A1
splice variant PDE9A5


substrate_name: 3',5'-Cyclic GMP

substrate: 3',5'-Cyclic GMP


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


sequence_variant_note: Resolved canonical sequence from UniProtKB O76074 direct accession lookup; Y612A reconstructed during review and applied mutation signature Y612A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O76074 direct accession lookup; F786A reconstructed during review and applied mutation signature F786A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O76074 direct accession lookup; V782A reconstructed during review and applied mutation signature V782A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB O76083 reviewed canonical sequence fetched by exact accession lookup on 2026-06-06.

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 RCSB PDB 3QI4 entity 1 FASTA/source sequence for PDE9A(Q453E), linked to PMID 21483814. and applied mutation signature Q453E to reconstruct the assayed variant sequence.


sequence_source: RCSB PDB 3N3Z entity 1 FASTA/source sequence for the PDE9A E406A catalytic domain.

sequence_variant_note: Mutation signature E406A references residue 406, which is outside the resolved sequence length.

proof_lines: SABIO-RK modifier species: 3',5'-cyclic-GMP phosphodiesterase(Enzyme) mutant E406A


sequence_source: RCSB PDB 3QI4 entity 1 FASTA/source sequence for PDE9A(Q453E), linked to PMID 21483814.


sequence_source: UniProtKB O76074 reviewed canonical sequence fetched by exact accession lookup on 2026-06-06.


organism: Dictyostelium discoideum

substrate_name: cAMP

substrate: cAMP


organism: Drosophila melanogaster


substrate_name: cAMP (isoform 1)

substrate: cAMP (isoform 1)


substrate_name: 3',5'-cyclic GMP (with the chimera containing the N-terminal regulatory GAF domains of PDE6C and the C-terminal catalytic domain of PDE6B)


substrate_name: 3',5'-cyclic GMP (with the chimera containing the N-terminal regulatory GAF domains of PDE6C and the C-terminal catalytic domain of PDE6A)


sequence_source: UniProtKB REST B0G0Y8 (PDE3_DICDI), UniProtKB reviewed (Swiss-Prot), retrieved 2026-06-06


sequence_source: UniProtKB REST Q8MM62 (PDE6_DICDI), UniProtKB reviewed (Swiss-Prot), retrieved 2026-06-06


sequence_source: UniProtKB REST Q8MLZ3 (PDE5_DICDI), UniProtKB reviewed (Swiss-Prot), retrieved 2026-06-06


sequence_source: UniProtKB REST Q54HY0 (PDE7_DICDI), UniProtKB reviewed (Swiss-Prot), retrieved 2026-06-06


organism: Gallus gallus

sequence_source: UniProtKB REST P52731 (PDE6C_CHICK), UniProtKB reviewed (Swiss-Prot), retrieved 2026-06-06

proof_lines:
enzyme from rod
enzyme from cone
Raw SKiD Env: Temp=-----, pH=-----


organism: Aquarana catesbeiana

proof_lines:
8fold higher on illumination
value of the dark


organism: Bacillus licheniformis


organism: Bombyx mori


organism: Bos taurus

proof_lines: chimaeric PDE5/PDE6 catalytic domain, pH and temperature not specified in the publication


organism: Canis lupus familiaris


organism: Cavia porcellus

proof_lines:
high affinity components
low affinity components


organism: Onchocerca volvulus

substrate_name: putrescine

substrate: putrescine


assay_conditions_summary: pH 7.8; 310.15 K; cofactor CoA


organism: Zea mays

proof_lines: isoform SSAT2, with 1,3-diaminopropane as cosubstrate, at pH 7.5 and 30°C

substrate: spermidine


organism: Haemophilus influenzae

substrate_name: phosphoenolpyruvate

substrate: phosphoenolpyruvate


organism: Mycobacterium tuberculosis


organism: Dictyostelium


proof_lines: isoform PDE5, high affinity form, pH 7.0, 22°C

proof_lines: isoform PDE5, low affinity form, pH 7.0, 22°C

proof_lines: isoform PDE6, high affinity form, pH 7.0, 22°C


assay_conditions_summary: pH 7.4; buffer conditions

proof_lines: mutant enzyme C1128S, in 50 mM KCl, 10 mM EGTA, 1.92 mM MgCl2, 1 mM dithiothreitol, and 50 mM HEPES, pH 7.4


assay_conditions_summary: pH 7.4; buffer conditions but gives no UniProt id

proof_lines: wild type enzyme, in 50 mM KCl, 10 mM EGTA, 1.92 mM MgCl2, 1 mM dithiothreitol, and 50 mM HEPES, pH 7.4


organism: Mus musculus


organism: Mycolicibacterium smegmatis

substrate_name: UDP-N-acetyl-alpha-D-glucosamine

substrate: UDP-N-acetyl-alpha-D-glucosamine


organism: Pseudomonas aeruginosa

substrate_name: UDP-N-acetyl-D-glucosamine

proof_lines: pH and temperature not specified in the publication

proof_lines: the calculated value for UDP is 40times higher than that of ADP

substrate: UDP-N-acetyl-D-glucosamine


organism: Staphylococcus aureus

proof_lines: 50 mM HEPES, 250 mM methylthioguanosine, 0.1 U/ml purine-nucleoside phosphorylase, 100 mM dithiothreitol, pH 7.6


organism: Streptococcus pneumoniae


organism: Escherichia coli

substrate_name: Alpha-naphthyl acetate

proof_lines: pH 8.0, 37°C, recombinant YeiG mutant D255A

substrate: Alpha-naphthyl acetate


proof_lines: pH 8.0, 37°C, recombinant YeiG mutant C26A


organism: Homo sapiens

substrate_name: S-formylglutathione

sequence_source: UniProtKB reviewed P10768 (ESTD_HUMAN)

substrate: S-formylglutathione


organism: Kloeckera sp.


organism: Saccharomyces cerevisiae

substrate_name: 4-nitrophenyl acetate

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed P40363 (SFGH_YEAST) using selected mutation H160S and applied mutation signature H160S to reconstruct the assayed variant sequence.

substrate: 4-nitrophenyl acetate


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed P40363 (SFGH_YEAST) using selected mutation W197I/H160I and applied mutation signature W197I/H160I to reconstruct the assayed variant sequence.


substrate_name: S-Lactoylglutathione

sequence_source: UniProtKB reviewed P40363 (SFGH_YEAST), supported by RCSB/PDB 3C6B mapping

proof_lines: wild-type, 22°C, pH 7.4, in the absence of substrate

substrate: S-Lactoylglutathione


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed P40363 (SFGH_YEAST) using selected mutation N64A and applied mutation signature N64A to reconstruct the assayed variant sequence.


organism: Dictyostelium discoideum

substrate_name: cGMP


proof_lines: kcat is 0.18 sec(-1) for cGMP. kcat is 2.37 sec(-1) for cAMP.


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


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: cGMP (for catalytic domain residues 610-954 and in presence of Zn(2+))


organism: Rattus norvegicus


enzyme_display_name: uridine/cytidine kinase

organism: Thermus thermophilus

substrate_name: uridine

sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q5SKR5 canonical sequence with reconstructed Y93H substitution after direct residue-93 check and applied mutation signature Y93H to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93H

enzyme: uridine/cytidine kinase

substrate: uridine


substrate_name: cytidine

sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q5SKR5 canonical sequence with reconstructed Y93F substitution after direct residue-93 check and applied mutation signature Y93F to reconstruct the assayed variant sequence.

substrate: cytidine


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q5SKR5 canonical sequence with reconstructed Y93V substitution after direct residue-93 check and applied mutation signature Y93V to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93V


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q5SKR5 canonical sequence with reconstructed Y93S substitution after direct residue-93 check and applied mutation signature Y93S to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93S


sequence_source: UniProtKB REST Q5SKR5 canonical sequence with reconstructed Y93F substitution after direct residue-93 check

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93F


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q5SKR5 canonical sequence with reconstructed Y93N substitution after direct residue-93 check and applied mutation signature Y93N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q5SKR5 canonical sequence with reconstructed Y93C substitution after direct residue-93 check and applied mutation signature Y93C to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q5SKR5 canonical sequence with reconstructed Y93Q substitution after direct residue-93 check and applied mutation signature Y93Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q5SKR5 canonical sequence with reconstructed Y93Q substitution from selected source/paper mutation evidence and applied mutation signature Y93Q to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93Q


sequence_variant_note: Resolved canonical sequence from UniProtKB Q5SKR5 canonical sequence with reconstructed Y93L substitution from selected source/paper mutation evidence and applied mutation signature Y93L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q5SKR5 canonical sequence with reconstructed Y93D substitution from selected source/paper mutation evidence and applied mutation signature Y93D to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93D


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5SKR5 and applied mutation signature Y93D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADH

column_label: Table 3: Kinetic parameters of ttCK and hsUCK2 mutants (Biochemistry and Biophysics Reports 2017, 11:93-98), ttCK enzyme block, row 'Y93D'; cytidine column 'kcat (s^-1)' = 1.4; cytidine column 'KM (uM)' = 236; cytidine column 'kcat/KM (M^-1 s^-1)' = 5.8 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.4 s^-1; already in s^-1, no conversion; the paper value is 1.4 s^(-1). Km: printed Table 3 cell 236 uM; 236 / 1000 = 0.236 mM. kcat/Km: printed Table 3 cell 5.8 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5800 / 1000 = 5.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, ttCK row Y93D, cytidine block: kcat = 1.4 s^-1; KM = 236 uM; printed kcat/KM = 5.8 x 10^3 M^-1 s^-1.

row_label: Table 3, ttCK enzyme block, row Y93D, cytidine columns


sequence_variant_note: Resolved canonical sequence from UniProtKB Q5SKR5 canonical sequence with reconstructed Y93W substitution from selected source/paper mutation evidence and applied mutation signature Y93W to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93W


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5SKR5 and applied mutation signature Y93I to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic parameters of ttCK and hsUCK2 mutants (Biochemistry and Biophysics Reports 2017, 11:93-98), ttCK enzyme block, row 'Y93I'; cytidine column 'kcat (s^-1)' = 2.9; cytidine column 'KM (uM)' = 574; cytidine column 'kcat/KM (M^-1 s^-1)' = 5.1 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 3 cell 2.9 s^-1; already in s^-1, no conversion; the paper value is 2.9 s^(-1). Km: printed Table 3 cell 574 uM; 574 / 1000 = 0.574 mM. kcat/Km: printed Table 3 cell 5.1 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5100 / 1000 = 5.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, ttCK row Y93I, cytidine block: kcat = 2.9 s^-1; KM = 574 uM; printed kcat/KM = 5.1 x 10^3 M^-1 s^-1.

row_label: Table 3, ttCK enzyme block, row Y93I, cytidine columns


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5SKR5 and applied mutation signature Y93V to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic parameters of ttCK and hsUCK2 mutants (Biochemistry and Biophysics Reports 2017, 11:93-98), ttCK enzyme block, row 'Y93V'; cytidine column 'kcat (s^-1)' = 3.9; cytidine column 'KM (uM)' = 965; cytidine column 'kcat/KM (M^-1 s^-1)' = 4.1 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.9 s^-1; already in s^-1, no conversion; the paper value is 3.9 s^(-1). Km: printed Table 3 cell 965 uM; 965 / 1000 = 0.965 mM. kcat/Km: printed Table 3 cell 4.1 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4100 / 1000 = 4.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, ttCK row Y93V, cytidine block: kcat = 3.9 s^-1; KM = 965 uM; printed kcat/KM = 4.1 x 10^3 M^-1 s^-1.

row_label: Table 3, ttCK enzyme block, row Y93V, cytidine columns


sequence_source: UniProtKB Q5SKR5 canonical sequence with reconstructed Y93L substitution from selected source/paper mutation evidence

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93L


sequence_source: UniProtKB Q9BZX2 direct REST lookup on 2026-06-06

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

proof_lines: pH 7.2, 25°C, recombinant wild-type enzyme UCK2


substrate_name: Uridine; ATP

sequence_source: UniProtKB Q9HA47 direct REST lookup on 2026-06-06

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines: pH 7.6, 37°C, recombinant uridine kinase 2

proof_lines: pH 7.6, 37°C, recombinant uridine kinase 1

substrate: Uridine; ATP


sequence_source: UniProtKB P52623 direct REST lookup on 2026-06-06

assay_conditions_summary: cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB Q5SKR5 direct REST lookup plus Y59F reconstruction on 2026-06-06 and applied mutation signature Y59F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q5SKR5 direct REST lookup plus Y59F reconstruction on 2026-06-06


sequence_source: UniProtKB Q5SKR5 direct REST lookup on 2026-06-06


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5SKR5 and applied mutation signature Y93C to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic parameters of ttCK and hsUCK2 mutants (Biochemistry and Biophysics Reports 2017, 11:93-98), ttCK enzyme block, row 'Y93C'; cytidine column 'kcat (s^-1)' = 1.9; cytidine column 'KM (uM)' = 215; cytidine column 'kcat/KM (M^-1 s^-1)' = 9.0 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.9 s^-1; already in s^-1, no conversion; the paper value is 1.9 s^(-1). Km: printed Table 3 cell 215 uM; 215 / 1000 = 0.215 mM. kcat/Km: printed Table 3 cell 9.0 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9000 / 1000 = 9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, ttCK row Y93C, cytidine block: kcat = 1.9 s^-1; KM = 215 uM; printed kcat/KM = 9.0 x 10^3 M^-1 s^-1.

row_label: Table 3, ttCK enzyme block, row Y93C, cytidine columns


proof_lines: pH 7.2, 25°C, recombinant wild-type enzyme ttCK


organism: Arabidopsis thaliana

substrate_name: Cytidine; ATP

sequence_source: UniProtKB:Q9FKS0 direct accession lookup on 2026-06-06

substrate: Cytidine; ATP


sequence_source: UniProtKB:Q8VYB2 direct accession lookup on 2026-06-06


substrate_name: ATP; Cytidine

sequence_source: UniProtKB:Q9LK34 direct accession lookup on 2026-06-06

substrate: ATP; Cytidine


organism: Entamoeba histolytica

sequence_source: UniProtKB:C4M4T4 direct accession lookup on 2026-06-06


sequence_source: UniProtKB:Q9BZX2 direct accession lookup on 2026-06-06

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

proof_lines: dependent on the assay method, pH 8.5, temperature not specified in the publication


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


organism: Unknown

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


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


sequence_variant_note: Resolved canonical sequence from UniProt REST Q5SKR5 canonical sequence fetched 2026-06-06; Y93T reconstructed after direct residue check. and applied mutation signature Y93T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST Q5SKR5 canonical sequence fetched 2026-06-06; Y93P reconstructed after direct residue check. and applied mutation signature Y93P to reconstruct the assayed variant sequence.


sequence_source: UniProt REST Q5SKR5 canonical sequence fetched 2026-06-06; Y93P reconstructed after direct residue check.

proof_lines: pH 7.2, 25°C, recombinant ttCK mutant Y93P


sequence_source: UniProt REST Q5SKR5 canonical sequence fetched 2026-06-06.

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=25°C, pH=7.2


organism: Geobacillus stearothermophilus


proof_lines:
pH 7.6, 37°C, ovarian carcinoma
pH 7.6, 37°C, normal ovary


organism: Mus musculus

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


proof_lines:
37°C, foetal liver uridine kinase
ATP in form of MgATP2-
pH 7.6, 37°C, normal liver


organism: Oryctolagus cuniculus

substrate: cGMP


proof_lines:
37°C, pH 7.4
sham-operated rats


organism: Strongylocentrotus purpuratus


organism: Acetivibrio thermocellus

substrate_name: cyclic 2',3'-AMP

substrate: cyclic 2',3'-AMP


enzyme_display_name: nicotinamide N-methyltransferase

substrate_name: nicotinamide (at pH 7.5 and 37 degrees Celsius)

enzyme: nicotinamide N-methyltransferase


substrate_name: nicotinamide

sequence_variant_note: Resolved canonical sequence from UniProt P40261 canonical sequence with direct one-based mutation reconstruction and applied mutation signature Y20F to reconstruct the assayed variant sequence.

substrate: nicotinamide


sequence_variant_note: Resolved canonical sequence from UniProt P40261 canonical sequence with direct one-based mutation reconstruction and applied mutation signature K100A/E101A/E103A to reconstruct the assayed variant sequence.

proof_lines: K100A/E101A/E103A mutant protein, pH 8.6, 37°C