substrate_name: L-Arg-p-nitroanilide

proof_lines: mutant enzyme D198P/F221E, at pH 8.0 and 37°C

substrate: L-Arg-p-nitroanilide


enzyme_display_name: bacterial leucyl aminopeptidase

organism: Streptomyces septatus

substrate_name: L-cystinyl-p-nitroanilide

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: bacterial leucyl aminopeptidase

substrate: L-cystinyl-p-nitroanilide

source: brenda


substrate_name: L-Leu-p-nitroanilide

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

proof_lines: mutant enzyme D198F/F221I, at pH 8.0 and 37°C

substrate: L-Leu-p-nitroanilide


organism: Treponema denticola

protein_accession_database: UniProt

sequence_source: UniProtKB Q73QZ3 direct lookup; reviewed Treponema denticola strain ATCC 35405 PepA sequence with leucine aminopeptidase alternative EC 3.4.11.10.

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

proof_lines:
recombinant enzyme, at pH 7.3
recombinant enzyme, at pH 8.0
native enzyme, at pH 7.3


organism: Vibrio proteolyticus

substrate_name: L-leucine 4-nitroanilide

sequence_source: UniProtKB Q01693 direct lookup; reviewed Vibrio proteolyticus bacterial leucyl aminopeptidase, EC 3.4.11.10.

assay_conditions_summary: pH 8; 298.15 K; buffer dependent

proof_lines: pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound

proof_lines: pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound

substrate: L-leucine 4-nitroanilide


enzyme_display_name: membrane alanyl aminopeptidase

organism: Bombyx mori

kcat_display: Not reported

assay_conditions_summary: pH 8

enzyme: membrane alanyl aminopeptidase


organism: Bos taurus

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Cavia porcellus


organism: Cucumis sativus


organism: Escherichia coli


organism: Homo sapiens

proof_lines: Ala-, Met-, Tyr-, Leu-, Phe-, Arg-, Lys-, Gly-derivatives


organism: Hordeum vulgare


organism: Spodoptera litura


organism: Streptococcus salivarius

substrate_name: Lys-4-methylcoumarin 7-amide

substrate: Lys-4-methylcoumarin 7-amide


organism: Streptomyces sp.

proof_lines:
recombinant enzyme, pH 7.0, 37°C
native enzyme, pH 7.0, 37°C


organism: Sus scrofa

proof_lines: recombinant wild-type enzyme, pH 7.4, 35°C


substrate_name: VVYPWTQRF

proof_lines: Km is pH-dependent between pH 6 and pH 9, maximum affinity at pH 7.0-7.3

substrate: VVYPWTQRF


enzyme_display_name: Xaa-Pro aminopeptidase

substrate_name: Arg-Pro-Pro

enzyme: Xaa-Pro aminopeptidase

substrate: Arg-Pro-Pro


organism: Mizuhopecten yessoensis


organism: Neisseria meningitidis

proof_lines:
pH 7.5, 37°C
pH 7.5, 37°C, value higher than
pH 7.5, 37°C, value above


organism: Novosphingobium capsulatum


organism: Oryctolagus cuniculus


organism: Plasmodium falciparum

proof_lines: pH and temperature not specified in the publication


organism: Rattus norvegicus

proof_lines:
from brain
from kidney
pH 7.4, 35°C


substrate_name: bradykinin

mutation_type: substitution

substrate: bradykinin


organism: Caenorhabditis elegans

sequence_source: UniProtKB reviewed O44750 direct EC+organism lookup; entry cites PMID 11606206 and ORF W03G9.4


substrate_name: Arg-Pro-Pro-benzylamide

substrate: Arg-Pro-Pro-benzylamide


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


proof_lines: wild type enzyme in 100 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 37°C


organism: Lactococcus lactis

substrate_name: Leu-Pro-Pro

substrate: Leu-Pro-Pro


organism: Lactococcus lactis subsp. lactis

substrate_name: L-Ile-L-Pro-L-Pro

assay_conditions_summary: pH 7

proof_lines: pH 7, temperature not specified in the publication

substrate: L-Ile-L-Pro-L-Pro


sequence_source: UniProtKB:A0A144A2H0 via direct EC 3.4.11.9 + Plasmodium falciparum lookup


substrate_name: Arg-Pro-Pro-Gly-Phe

sequence_source: UniProtKB:Q99MA2; PubMed 7669781 membrane-bound rat lung aminopeptidase P context

proof_lines:
in presence of 4 mM Mn2+
without 4 mM Mn2+
without Mn2+

substrate: Arg-Pro-Pro-Gly-Phe


organism: Streptomyces lavendulae

sequence_source: UniProtKB:M4MBM1 / EMBL KC292272 / NCBI protein AGG68151.1

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


organism: Streptomyces lividans

proof_lines:
recombinant enzyme, pH 7.4, 30°C
chimera th-sl cAPP, pH 7.0, 30°C
chimera sl-th cAPP, pH 8.2, 30°C


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q95333 using selected mutation H519K and applied mutation signature H519K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q95333 using selected mutation H519L and applied mutation signature H519L to reconstruct the assayed variant sequence.


enzyme_display_name: Xaa-Pro dipeptidase

organism: Macaca radiata

substrate_name: Gly-L-Pro; Pro-Hyp; Gly-Hyp

enzyme: Xaa-Pro dipeptidase

substrate: Gly-L-Pro; Pro-Hyp; Gly-Hyp


organism: Neurospora crassa

substrate_name: L-Val-L-Pro; Gly-L-Pro; Met-Pro

substrate: L-Val-L-Pro; Gly-L-Pro; Met-Pro


organism: Pyrococcus furiosus

substrate_name: Met-Pro

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P81535 using selected mutation G39E and applied mutation signature G39E to reconstruct the assayed variant sequence.

proof_lines:
pH 7.0, 100°C, recombinant mutant G39E
pH 7.0, 35°C, recombinant mutant G39E
pH 7.0, 70°C, recombinant mutant G39E

substrate: Met-Pro


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P81535 using selected mutation R19G/G39E/K71E/S229T and applied mutation signature R19G/G39E/K71E/S229T to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 35°C, recombinant mutant R19G/G39E/K71E/S229T

proof_lines: pH 7.0, 70°C, recombinant mutant R19G/G39E/K71E/S229T

proof_lines: pH 7.0, 100°C, recombinant mutant R19G/G39E/K71E/S229T


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P81535 using selected mutation R19G/K71E/S229T and applied mutation signature R19G/K71E/S229T to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 35°C, recombinant mutant R19G/K71E/S229T

proof_lines: pH 7.0, 70°C, recombinant mutant R19G/K71E/S229T

proof_lines: pH 7.0, 100°C, recombinant mutant R19G/K71E/S229T


sequence_source: UniProtKB:P81535 via direct EC 3.4.13.9 + Pyrococcus furiosus lookup and RCSB 1PV9 cross-check

proof_lines: pH 7.0, 70°C, recombinant wild-type enzyme

proof_lines: pH 7.0, 35°C, recombinant wild-type enzyme

proof_lines: pH 7.0, 100°C, recombinant wild-type enzyme


organism: Homo sapiens

substrate_name: Ala-Pro

proof_lines: pH 7.8, 37°C, recombinant His-tagged mutant H859A

substrate: Ala-Pro


proof_lines: pH 7.8, 37°C, recombinant His-tagged mutant Y844A


substrate_name: Gly-Pro

assay_conditions_summary: pH 7.8; 310.15 K; buffer 30 mM phosphate

proof_lines: pH 7.8, 37°C, presence of 20 mM D-valine, prolidase I

proof_lines: pH 7.8, 37°C, presence of 0.1 mM MnCl2 plus 20 mM glycine

substrate: Gly-Pro


organism: Lacticaseibacillus casei

substrate_name: Leu-Pro

substrate: Leu-Pro


organism: Lactobacillus delbrueckii

verification_status: corrected

status: corrected


organism: Lactococcus cremoris

substrate_name: Val-Pro

substrate: Val-Pro


organism: Sus scrofa

sequence_source: UniProtKB reviewed accession Q95333 (XPP2_PIG), matched by Sus scrofa, EC 3.4.11.9, membrane-bound aminopeptidase P, kidney/membrane context, and bradykinin AP-P function.


substrate_name: Gly-Pro-Hyp

sequence_source: UniProtKB reviewed accession Q95333 (XPP2_PIG), matched by Sus scrofa, EC 3.4.11.9, pig kidney membrane-bound AP-P context, and Gly-Pro-Hyp substrate context.

substrate: Gly-Pro-Hyp


organism: Trichinella spiralis

sequence_source: GenBank protein EFV57850.1 from the PMID 36089006 TsAPP source paper; sequence also matches UniProtKB TrEMBL E5SBI8.

proof_lines: pH and temperature not specified in the publication


organism: Aspergillus phoenicis


organism: Bos taurus

substrate_name: L-Val-L-Pro

substrate: L-Val-L-Pro


organism: Cavia porcellus

substrate_name: L-Met-L-Pro

substrate: L-Met-L-Pro


enzyme_display_name: pepsin A

organism: Micropterus salmoides

substrate_name: Substance P

proof_lines:
isoform PG1-1, at pH 3.0 and 37°C
isoform PG2-2, at pH 3.0 and 37°C

enzyme: pepsin A

substrate: Substance P


organism: Monopterus albus

substrate_name: hemoglobin

assay_conditions_summary: pH 3; 310.15 K; buffer sodium acetate

proof_lines: isoform pepsin 1, in 250 mM sodium acetate buffer (pH 3.0), at 37°C

substrate: hemoglobin


organism: Oncorhynchus mykiss

substrate_name: Acid-denatured hemoglobin

proof_lines:
isoform P-III, at pH 2.0 and 37°C
isoform P-I, at pH 2.0 and 37°C
isoform P-II, at pH 2.0 and 37°C

substrate: Acid-denatured hemoglobin


organism: Ovis aries

substrate_name: N,N-dimethylcasein

substrate: N,N-dimethylcasein


organism: Saurida micropectoralis

proof_lines:
pepsinogen III, pH 2.0, 40°C
pepsinogen II, pH 2.0, 40°C
pepsinogen I, pH 2.0, 40°C


proof_lines:
pH 2.1, 37°C, mutant enzyme G76A
pH 3.95, 37°C, mutant enzyme G76A


substrate_name: Phe-Pro

sequence_source: UniProtKB:P81535 direct EC+organism lookup; UniProt reference list links P81535 to PMID 9733678.

proof_lines:
native prolidase
recombinant prolidase

substrate: Phe-Pro


enzyme_display_name: angiotensin-converting enzyme 2

substrate_name: angiotensin I

sequence_source: UniProtKB:Q9BYF1 direct EC+organism lookup for human ACE2.

enzyme: angiotensin-converting enzyme 2

substrate: angiotensin I


organism: Albatrossia pectoralis


organism: Gallus gallus

substrate_name: casein

proof_lines: A B

substrate: casein


assay_conditions_summary: pH 4; 310.15 K; buffer 0.2 M sodium formate

proof_lines: in 0.2 M sodium formate buffer, pH 4.0, at 37°C


proof_lines:
pH 3.5, 25°C, wild-type enzyme
pH 3.95, 37°C, wild-type enzyme
wild-type, pH 2.0


proof_lines: pH 3.5, 25°C, mutant enzyme F111T/L112F/T222V/E287M


proof_lines: pH 3.95, 37°C, mutant enzyme L10M/T12A/E13S


proof_lines:
pH 2.1, 37°C, mutant enzyme G76V
pH 3.95, 37°C, mutant enzyme G76V


proof_lines:
pH 3.95, 37°C, mutant enzyme G76S
pH 2.1, 37°C, mutant enzyme G76S


proof_lines: pH 3.5, 25°C, mutant enzyme F111T/L112F/E287M


proof_lines: pH 3.95, 37°C, mutant enzyme G2S/D3Y/L10M/T12A/E13S


mutation_type: deletion

proof_lines: pH 3.95, 37°C, mutant enzyme DELTA240-246/+GD


assay_conditions_summary: pH 2

proof_lines: unglycosylated mutant E244N/V246T, pH 2.0


proof_lines:
glycosylated mutant T77N, pH 2.0
unglycosylated mutant T77N, pH 2.0


proof_lines: unglycosylated mutant S110N/L112T, pH 2.0


organism: Lactococcus lactis

substrate_name: L-Leu-L-Pro

proof_lines: mutant enzyme R293S/S307G, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C

substrate: L-Leu-L-Pro


proof_lines: mutant enzyme R293S, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C


proof_lines: mutant enzyme S307G, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C


proof_lines: mutant enzyme S307R, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C


proof_lines: wild type enzyme, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C


proof_lines: mutant enzyme S307D, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C


proof_lines:
unglycosylated mutant S281N, pH 2.0
glycosylated mutant S281N, pH 2.0


proof_lines: in 0.2 M sodium formate buffer, pH 4.0, at 37°C


proof_lines:
T77D/G78(S)S79 double mutant
T77D mutant


organism: Alcaligenes sp.

substrate_name: N-formyl-D-aspartate

substrate: N-formyl-D-aspartate


organism: Aspergillus melleus

substrate_name: N-acetyl-L-methionine

proof_lines: pH 8.0, 40°C, immobilized, cross-linked enzyme-bovine serum albumin aggregate

substrate: N-acetyl-L-methionine


organism: Bacillus sp. (in: firmicutes)

proof_lines:
addition of 0.2 mM Co2+
addition of 0.2 mM Mn2+


organism: Corynebacterium striatum


organism: Mycobacterium sp.

substrate_name: palmitoylaspartate

substrate: palmitoylaspartate


organism: Pseudomonas sp. AK2

substrate_name: N-acetyl-L-pipecolic acid

proof_lines: pH and temperature not specified in the publication

substrate: N-acetyl-L-pipecolic acid


organism: Rattus norvegicus

substrate_name: N-acetylmethionine

substrate: N-acetylmethionine


organism: Stenotrophomonas maltophilia

substrate_name: N-acetyl-DL-aspartate

substrate: N-acetyl-DL-aspartate


organism: Streptomyces ambofaciens

substrate_name: lauric acid

substrate: lauric acid


organism: Sus scrofa

substrate_name: N-isopentanoyl-L-methionine

assay_conditions_summary: buffer hydrolysis in D2O

proof_lines: kcat for the hydrolysis of N-acetyl-L-methionine substrates by pAcy1

proof_lines: kcat for the hydrolysis of N-acetyl-L-glutamate substrates by pAcy1

proof_lines: hydrolysis of N-acyl-L-methionine substrates by pAcy1

substrate: N-isopentanoyl-L-methionine


organism: Homo sapiens

substrate_name: Nalpha-acetylmethionine

substrate: Nalpha-acetylmethionine


substrate_name: N-alpha-acetyl-L-phenylalanine

substrate: N-alpha-acetyl-L-phenylalanine


organism: Mus musculus

substrate_name: N-acetyl-L-aspartate

verification_status: unverified

proof_lines: E167R mutant protein, pH not specified in the publication, temperature not specified in the publication

substrate: N-acetyl-L-aspartate

status: unverified


substrate_name: Unknown

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

substrate: Unknown


organism: Escherichia coli

substrate_name: alpha-D-Galactose 1-phosphate

source_db: oed

sequence_variant_note: Resolved canonical sequence from UniProtKB:P09148 canonical sequence; C160A reconstructed from selected source mutation_signature and applied mutation signature C160A to reconstruct the assayed variant sequence.

data_origin: experimental

substrate: alpha-D-Galactose 1-phosphate

source: oed


substrate_name: UDPglucose

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from UniProtKB:P09148 canonical sequence; S161A reconstructed from selected source mutation_signature and applied mutation signature S161A to reconstruct the assayed variant sequence.

substrate: UDPglucose


substrate_name: D-Glucose 1-phosphate; UDPgalactose

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

sequence_source: UniProtKB:P09148 reviewed canonical sequence; source did not explicitly mark wild type or mutant

substrate: D-Glucose 1-phosphate; UDPgalactose


sequence_variant_note: Resolved canonical sequence from UniProtKB:P09148 canonical sequence; Q168N reconstructed from selected source mutation_signature and applied mutation signature Q168N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P09148 canonical sequence; Q168N reconstructed from selected source mutation_signature

proof_lines: SABIO-RK modifier species: UDP-glucose---hexose-1-phosphate uridylyltransferase(Enzyme) mutant Q168N


sequence_source: UniProtKB:P09148 reviewed canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB:P09148 canonical sequence; Q168R reconstructed from selected source mutation_signature and applied mutation signature Q168R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-glucose---hexose-1-phosphate uridylyltransferase(Enzyme) mutant Q168R


enzyme_display_name: kynureninase

sequence_source: UniProtKB reviewed Q16719 canonical displayed sequence

enzyme: kynureninase


proof_lines: wild type enzyme, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5-phosphate, at 37°C


substrate_name: L-kynurenine

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed Q16719 canonical displayed sequence and selected mutation_signature H102W/N333T and applied mutation signature H102W/N333T to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H102W/N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5-phosphate, at 37°C

substrate: L-kynurenine


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed Q16719 canonical displayed sequence and selected mutation_signature N333T and applied mutation signature N333T to reconstruct the assayed variant sequence.

proof_lines: kcat less than 0.0039 1/s, mutant enzyme N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5-phosphate, at 37°C

proof_lines: Km above 0.2 mM, mutant enzyme N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5-phosphate, at 37°C


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed Q16719 canonical displayed sequence and selected mutation_signature H102W/S332G/N333T and applied mutation signature H102W/S332G/N333T to reconstruct the assayed variant sequence.

proof_lines: Km above 0.51 mM, mutant enzyme H102W/S332G/N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5-phosphate, at 37°C


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed Q16719 canonical displayed sequence and selected mutation_signature S332G/N333T and applied mutation signature S332G/N333T to reconstruct the assayed variant sequence.

proof_lines: kcat less than 0.0109 1/s, mutant enzyme S332G/N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5-phosphate, at 37°C

proof_lines: Km above 0.51 mM, mutant enzyme S332G/N333T, in 30 mM potassium phosphate, pH 8.0, and 0.04 mM pyridoxal 5-phosphate, at 37°C


substrate_name: L-Kynurenine; H2O

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

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

source_databases_merged: sabio_rk brenda skid

substrate: L-Kynurenine; H2O


substrate_name: UDP-galactose

sequence_variant_note: Resolved canonical sequence from UniProtKB REST 2026_01 accession P09148 plus direct E182A reconstruction and applied mutation signature E182A to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant E182A, reverse reaction, pH 8.5, 27°C

proof_lines: recombinant mutant E182A, forward reaction, pH 8.5, 27°C

substrate: UDP-galactose


sequence_source: UniProtKB REST 2026_01 accession P09148

proof_lines: recombinant wild-type, reverse reaction, pH 8.5, 27°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST 2026_01 accession P09148 plus direct S161A reconstruction and applied mutation signature S161A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST 2026_01 accession P09148 plus direct S161A reconstruction

proof_lines: SABIO-RK modifier species: UDP-glucose---hexose-1-phosphate uridylyltransferase(Enzyme) mutant S161A

proof_lines: recombinant mutant S161A, reverse reaction, pH 8.5, 27°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST 2026_01 accession P09148 plus direct C160A reconstruction and applied mutation signature C160A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-glucose---hexose-1-phosphate uridylyltransferase(Enzyme) mutant C160A

proof_lines: recombinant mutant C160A, reverse reaction, pH 8.5, 27°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07902 displayed canonical sequence; R223S reconstructed after residue-offset check and applied mutation signature R223S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-glucose---hexose-1-phosphate uridylyltransferase(Enzyme) mutant R223S


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07902 displayed canonical sequence; R201C reconstructed after residue-offset check and applied mutation signature R201C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-glucose---hexose-1-phosphate uridylyltransferase(Enzyme) mutant R201C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07902 displayed canonical sequence; L289F reconstructed after residue-offset check and applied mutation signature L289F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-glucose---hexose-1-phosphate uridylyltransferase(Enzyme) mutant L289F


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07902 displayed canonical sequence; I278N reconstructed after residue-offset check and applied mutation signature I278N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-glucose---hexose-1-phosphate uridylyltransferase(Enzyme) mutant I278N


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07902 displayed canonical sequence; E220K reconstructed after residue-offset check and applied mutation signature E220K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-glucose---hexose-1-phosphate uridylyltransferase(Enzyme) mutant E220K


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07902 displayed canonical sequence; E291V reconstructed after residue-offset check and applied mutation signature E291V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-glucose---hexose-1-phosphate uridylyltransferase(Enzyme) mutant E291V


substrate_name: UDP-alpha-D-glucose

verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07902 and applied mutation signature D28Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.8; 310.15 K; buffer 10 mM HEPES pH 8

column_label: Table 2 prints, after the hGALT Variant label, the column group 'Apparent Km' in uM (footnote a for varied UDP-Glc, footnote b for varied Gal-1P), the column 'UDP-Glc Ki' in uM, the column 'Apparent kcat' in s^-1, and the column group 'Apparent kcat/Km' scaled as x 10^5 l.mol^-1.s^-1 (footnote a for varied UDP-Glc, footnote b for varied Gal-1P). Footnote a reads [Gal-1P] = 1000 uM and footnote b reads [UDP-Glc] = 500 uM. The cell set read here is the line labelled p.D28Y: Km 448.7 uM, kcat 9.4 s^-1 and kcat/Km 0.21 x 10^5 M^-1 s^-1 in the columns bound by the table footnote to the varied substrate UDP-Glc.

normalized_value_unit_evidence: Km: printed cell 448.7 uM; 448.7 / 1000 = 0.4487 mM, which is the exported km. kcat: printed cell 9.4 s^-1; the cell is already in s^-1, so no unit conversion applies, and 9.4 s^(-1) is the exported kcat. kcat/Km: the printed cell 0.21 x 10^5 M^-1 s^-1 is the paper's own rounded rendering of the same measurement; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.21 x 10^5 / 1000 = 21.0 s^-1 mM^-1, while the exact quotient of the same two printed cells is 9.4 / 0.4487 = 20.949409404947627 s^-1 mM^-1, and that exact quotient is the value carried for this measurement.

raw_value_unit_evidence: Table 2, row p.D28Y, footnote column set for varied substrate UDP-Glc: apparent Km = 448.7 uM; apparent kcat = 9.4 s^-1; printed apparent kcat/Km = 0.21 x 10^5 M^-1 s^-1.

row_label: Table 2, canonical variant row p.D28Y, footnote column set for varied substrate UDP-Glc

table_label: Table 2: Steady state kinetic constants for the forward reaction of recombinant wild-type and active variant hGALT enzymes (Biochim Biophys Acta 2013;1832(8):1279-1293)

substrate: UDP-alpha-D-glucose

status: verified


substrate_name: alpha-D-glucose 1-phosphate

sequence_source: UniProtKB:P07902 displayed canonical sequence

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

substrate: alpha-D-glucose 1-phosphate


enzyme_display_name: aromatic-amino-acid transaminase

organism: Paracoccus denitrificans

substrate_name: L-Cysteine

sequence_source: UniProt REST accession P95468

enzyme: aromatic-amino-acid transaminase

substrate: L-Cysteine


substrate_name: L-Aspartate

substrate: L-Aspartate


sequence_variant_note: Resolved canonical sequence from UniProt P07902 canonical FASTA/REST sequence plus checked R333G substitution reconstruction and applied mutation signature R333G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P07902 canonical FASTA/REST sequence plus checked D28Y substitution reconstruction and applied mutation signature D28Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P07902 canonical FASTA/REST sequence plus checked F194L substitution reconstruction and applied mutation signature F194L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07902 and applied mutation signature F194L to reconstruct the assayed variant sequence.

column_label: Table 2 prints, after the hGALT Variant label, the column group 'Apparent Km' in uM (footnote a for varied UDP-Glc, footnote b for varied Gal-1P), the column 'UDP-Glc Ki' in uM, the column 'Apparent kcat' in s^-1, and the column group 'Apparent kcat/Km' scaled as x 10^5 l.mol^-1.s^-1 (footnote a for varied UDP-Glc, footnote b for varied Gal-1P). Footnote a reads [Gal-1P] = 1000 uM and footnote b reads [UDP-Glc] = 500 uM. The cell set read here is the line labelled p.F194L: Km 60.8 uM, kcat 2.5 s^-1 and kcat/Km 0.41 x 10^5 M^-1 s^-1 in the columns bound by the table footnote to the varied substrate UDP-Glc.

normalized_value_unit_evidence: Km: printed cell 60.8 uM; 60.8 / 1000 = 0.0608 mM, which is the exported km. kcat: printed cell 2.5 s^-1; the cell is already in s^-1, so no unit conversion applies, and 2.5 s^(-1) is the exported kcat. kcat/Km: the printed cell 0.41 x 10^5 M^-1 s^-1 is the paper's own rounded rendering of the same measurement; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.41 x 10^5 / 1000 = 41.0 s^-1 mM^-1, while the exact quotient of the same two printed cells is 2.5 / 0.0608 = 41.11842105263158 s^-1 mM^-1, and that exact quotient is the value carried for this measurement.

raw_value_unit_evidence: Table 2, row p.F194L, footnote column set for varied substrate UDP-Glc: apparent Km = 60.8 uM; apparent kcat = 2.5 s^-1; printed apparent kcat/Km = 0.41 x 10^5 M^-1 s^-1.

row_label: Table 2, canonical variant row p.F194L, footnote column set for varied substrate UDP-Glc


column_label: Table 3 prints, after the hGALT Variant label, the column group 'Apparent Km or K0.5' in uM (footnote a for varied UDP-Gal, footnote b for varied Glc-1P), the column 'Glc-1P Ki' in mM, the column 'UDP-Gal h', the column 'Apparent kcat' in s^-1, and the column group 'Apparent kcat/Km or kcat/K0.5' scaled as x 10^5 l.mol^-1.s^-1 (footnote a for varied UDP-Gal, footnote b for varied Glc-1P). Footnote a reads [Glc-1P] = 1000 uM and footnote b reads [UDP-Gal] = 500 uM. The cell set read here is the line labelled p.D28Y: Km 121 uM, kcat 9.3 s^-1 and kcat/Km 0.77 x 10^5 M^-1 s^-1 in the columns bound by the table footnote to the varied substrate Glc-1P.

normalized_value_unit_evidence: Km: printed cell 121 uM; 121 / 1000 = 0.121 mM, which is the exported km. kcat: printed cell 9.3 s^-1; the cell is already in s^-1, so no unit conversion applies, and 9.3 s^(-1) is the exported kcat. kcat/Km: the printed cell 0.77 x 10^5 M^-1 s^-1 is the paper's own rounded rendering of the same measurement; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.77 x 10^5 / 1000 = 77.0 s^-1 mM^-1, while the exact quotient of the same two printed cells is 9.3 / 0.121 = 76.85950413223141 s^-1 mM^-1, and that exact quotient is the value carried for this measurement.

raw_value_unit_evidence: Table 3, row p.D28Y, footnote column set for varied substrate Glc-1P: apparent Km = 121 uM; apparent kcat = 9.3 s^-1; printed apparent kcat/Km = 0.77 x 10^5 M^-1 s^-1.

row_label: Table 3, canonical variant row p.D28Y, footnote column set for varied substrate Glc-1P

table_label: Table 3: Steady state kinetic constants for the reverse reaction of recombinant wild-type and active variant hGALT enzymes (Biochim Biophys Acta 2013;1832(8):1279-1293)


column_label: Table 3 prints, after the hGALT Variant label, the column group 'Apparent Km or K0.5' in uM (footnote a for varied UDP-Gal, footnote b for varied Glc-1P), the column 'Glc-1P Ki' in mM, the column 'UDP-Gal h', the column 'Apparent kcat' in s^-1, and the column group 'Apparent kcat/Km or kcat/K0.5' scaled as x 10^5 l.mol^-1.s^-1 (footnote a for varied UDP-Gal, footnote b for varied Glc-1P). Footnote a reads [Glc-1P] = 1000 uM and footnote b reads [UDP-Gal] = 500 uM. The cell set read here is the line labelled p.F194L: Km 118 uM, kcat 5.5 s^-1 and kcat/Km 0.47 x 10^5 M^-1 s^-1 in the columns bound by the table footnote to the varied substrate Glc-1P.

normalized_value_unit_evidence: Km: printed cell 118 uM; 118 / 1000 = 0.118 mM, which is the exported km. kcat: printed cell 5.5 s^-1; the cell is already in s^-1, so no unit conversion applies, and 5.5 s^(-1) is the exported kcat. kcat/Km: the printed cell 0.47 x 10^5 M^-1 s^-1 is the paper's own rounded rendering of the same measurement; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.47 x 10^5 / 1000 = 47.0 s^-1 mM^-1, while the exact quotient of the same two printed cells is 5.5 / 0.118 = 46.610169491525426 s^-1 mM^-1, and that exact quotient is the value carried for this measurement.

raw_value_unit_evidence: Table 3, row p.F194L, footnote column set for varied substrate Glc-1P: apparent Km = 118 uM; apparent kcat = 5.5 s^-1; printed apparent kcat/Km = 0.47 x 10^5 M^-1 s^-1.

row_label: Table 3, canonical variant row p.F194L, footnote column set for varied substrate Glc-1P


sequence_source: UniProt P07902 canonical FASTA/REST sequence

column_label: Table 3 prints, after the hGALT Variant label, the column group 'Apparent Km or K0.5' in uM (footnote a for varied UDP-Gal, footnote b for varied Glc-1P), the column 'Glc-1P Ki' in mM, the column 'UDP-Gal h', the column 'Apparent kcat' in s^-1, and the column group 'Apparent kcat/Km or kcat/K0.5' scaled as x 10^5 l.mol^-1.s^-1 (footnote a for varied UDP-Gal, footnote b for varied Glc-1P). Footnote a reads [Glc-1P] = 1000 uM and footnote b reads [UDP-Gal] = 500 uM. The cell set read here is the line labelled WT: Km 159 uM, kcat 17.7 s^-1 and kcat/Km 1.11 x 10^5 M^-1 s^-1 in the columns bound by the table footnote to the varied substrate Glc-1P.

normalized_value_unit_evidence: Km: printed cell 159 uM; 159 / 1000 = 0.159 mM, which is the exported km. kcat: printed cell 17.7 s^-1; the cell is already in s^-1, so no unit conversion applies, and 17.7 s^(-1) is the exported kcat. kcat/Km: the printed cell 1.11 x 10^5 M^-1 s^-1 is the paper's own rounded rendering of the same measurement; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.11 x 10^5 / 1000 = 111.0 s^-1 mM^-1, while the exact quotient of the same two printed cells is 17.7 / 0.159 = 111.32075471698113 s^-1 mM^-1, and that exact quotient is the value carried for this measurement.

raw_value_unit_evidence: Table 3, row WT, footnote column set for varied substrate Glc-1P: apparent Km = 159 uM; apparent kcat = 17.7 s^-1; printed apparent kcat/Km = 1.11 x 10^5 M^-1 s^-1.

row_label: Table 3, canonical variant row WT (recombinant wild-type hGALT), footnote column set for varied substrate Glc-1P


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07902 and applied mutation signature R333G to reconstruct the assayed variant sequence.

column_label: Table 2 prints, after the hGALT Variant label, the column group 'Apparent Km' in uM (footnote a for varied UDP-Glc, footnote b for varied Gal-1P), the column 'UDP-Glc Ki' in uM, the column 'Apparent kcat' in s^-1, and the column group 'Apparent kcat/Km' scaled as x 10^5 l.mol^-1.s^-1 (footnote a for varied UDP-Glc, footnote b for varied Gal-1P). Footnote a reads [Gal-1P] = 1000 uM and footnote b reads [UDP-Glc] = 500 uM. The cell set read here is the line labelled p.R333G: Km 285.7 uM, kcat 0.98 s^-1 and kcat/Km 0.03 x 10^5 M^-1 s^-1 in the columns bound by the table footnote to the varied substrate UDP-Glc.

normalized_value_unit_evidence: Km: printed cell 285.7 uM; 285.7 / 1000 = 0.2857 mM, which is the exported km. kcat: printed cell 0.98 s^-1; the cell is already in s^-1, so no unit conversion applies, and 0.98 s^(-1) is the exported kcat. kcat/Km: the printed cell 0.03 x 10^5 M^-1 s^-1 is the paper's own rounded rendering of the same measurement; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.03 x 10^5 / 1000 = 3.0 s^-1 mM^-1, while the exact quotient of the same two printed cells is 0.98 / 0.2857 = 3.4301715085754285 s^-1 mM^-1, and that exact quotient is the value carried for this measurement.

raw_value_unit_evidence: Table 2, row p.R333G, footnote column set for varied substrate UDP-Glc: apparent Km = 285.7 uM; apparent kcat = 0.98 s^-1; printed apparent kcat/Km = 0.03 x 10^5 M^-1 s^-1.

row_label: Table 2, canonical variant row p.R333G, footnote column set for varied substrate UDP-Glc


organism: Pseudomonas fluorescens

proof_lines:
pH 8.0, 37°C, recombinant enzyme
Raw SKiD Env: Temp=37°C, pH=8
Raw SKiD Env: Temp=-----, pH=7.8


substrate_name: O-benzoyl-L-serine

substrate: O-benzoyl-L-serine


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession:P83788 and applied mutation signature Y226F to reconstruct the assayed variant sequence.


proof_lines:
enzyme mutant Y226F, pH 8.0, 37°C
pH 8.0, 37°C, mutant enzyme Y226F


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession:P83788 and applied mutation signature S36A to reconstruct the assayed variant sequence.


substrate_name: beta-benzoyl-L-alanine

substrate: beta-benzoyl-L-alanine


organism: Unknown

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


sequence_source: UniProtKB P07902 direct REST lookup

column_label: Table 2 prints, after the hGALT Variant label, the column group 'Apparent Km' in uM (footnote a for varied UDP-Glc, footnote b for varied Gal-1P), the column 'UDP-Glc Ki' in uM, the column 'Apparent kcat' in s^-1, and the column group 'Apparent kcat/Km' scaled as x 10^5 l.mol^-1.s^-1 (footnote a for varied UDP-Glc, footnote b for varied Gal-1P). Footnote a reads [Gal-1P] = 1000 uM and footnote b reads [UDP-Glc] = 500 uM. The cell set read here is the line labelled WT: Km 81.6 uM, kcat 13.6 s^-1 and kcat/Km 1.67 x 10^5 M^-1 s^-1 in the columns bound by the table footnote to the varied substrate UDP-Glc.

normalized_value_unit_evidence: Km: printed cell 81.6 uM; 81.6 / 1000 = 0.0816 mM, which is the exported km. kcat: printed cell 13.6 s^-1; the cell is already in s^-1, so no unit conversion applies, and 13.6 s^(-1) is the exported kcat. kcat/Km: the printed cell 1.67 x 10^5 M^-1 s^-1 is the paper's own rounded rendering of the same measurement; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.67 x 10^5 / 1000 = 167.0 s^-1 mM^-1, while the exact quotient of the same two printed cells is 13.6 / 0.0816 = 166.66666666666666 s^-1 mM^-1, and that exact quotient is the value carried for this measurement.

raw_value_unit_evidence: Table 2, row WT, footnote column set for varied substrate UDP-Glc: apparent Km = 81.6 uM; apparent kcat = 13.6 s^-1; printed apparent kcat/Km = 1.67 x 10^5 M^-1 s^-1.

row_label: Table 2, canonical variant row WT (recombinant wild-type hGALT), footnote column set for varied substrate UDP-Glc


sequence_variant_note: Resolved canonical sequence from UniProtKB P07902 direct REST lookup plus R333G reconstruction and applied mutation signature R333G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07902 direct REST lookup plus P185S reconstruction and applied mutation signature P185S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-glucose---hexose-1-phosphate uridylyltransferase(Enzyme) mutant P185S


sequence_variant_note: Resolved canonical sequence from UniProtKB P07902 direct REST lookup plus P185A reconstruction and applied mutation signature P185A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-glucose---hexose-1-phosphate uridylyltransferase(Enzyme) mutant P185A


proof_lines: pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P07902 direct REST lookup plus P185Q reconstruction and applied mutation signature P185Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-glucose---hexose-1-phosphate uridylyltransferase(Enzyme) mutant P185Q


sequence_variant_note: Resolved canonical sequence from UniProtKB P07902 direct REST lookup plus P185G reconstruction and applied mutation signature P185G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-glucose---hexose-1-phosphate uridylyltransferase(Enzyme) mutant P185G


sequence_variant_note: Resolved canonical sequence from UniProtKB P07902 direct REST lookup plus P185E reconstruction and applied mutation signature P185E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-glucose---hexose-1-phosphate uridylyltransferase(Enzyme) mutant P185E


organism: Klebsiella pneumoniae

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

source_db: uniprot

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

source: uniprot


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: tryptophan

substrate: tryptophan


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

substrate_name: phenylalanine

substrate: phenylalanine


organism: Escherichia coli (strain K12)

substrate_name: uridine 5'-diphosphate glucose

substrate: uridine 5'-diphosphate glucose


substrate_name: alpha-D-galactose 1-phosphate (at pH 8.7)


organism: Pyrobaculum aerophilum

sequence_source: UniProtKB Q8ZXN7 direct accession lookup


sequence_source: UniProtKB P43424 direct accession lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB P83788 direct accession lookup plus S36A reconstruction and applied mutation signature S36A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P83788 direct accession lookup

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


sequence_source: UniProtKB P83788 direct accession lookup plus S36A reconstruction


sequence_source: UniProtKB P70712 direct accession lookup


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 350 sec(-1) with phenylalanine as substrate. kcat is 278 sec(-1) with tyrosine as substrate. kcat is 960 sec(-1) with tryptophan as substrate.


substrate_name: L-kynurenine (at pH 7.0)

substrate: L-kynurenine (at pH 7.0)


organism: Bifidobacterium bifidum

substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: alpha-D-galactose 1-phosphate

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

proof_lines: recombinant mutant S161A, forward reaction, pH 8.5, 27°C

substrate: alpha-D-galactose 1-phosphate


proof_lines: recombinant mutant C160A, forward reaction, pH 8.5, 27°C


proof_lines: recombinant mutant Q168N, forward reaction, pH 8.5, 27°C


proof_lines: purified recombinant bifunctional chimeric fusion protein, pH 8.5, 27°C


substrate_name: uridine 5'-phosphoimidazolate

proof_lines: mutant H166G, forward reaction with D-glucose 1-phosphate, pH 8.5, 27°C

proof_lines: mutant H166G, forward reaction with UDP-glucose, pH 8.5, 27°C

substrate: uridine 5'-phosphoimidazolate


proof_lines: mutant H166A, forward reaction with D-glucose 1-phosphate, pH 8.5, 27°C

proof_lines: mutant H166A, forward reaction with UDP-glucose, pH 8.5, 27°C


proof_lines: recombinant wild-type, forward reaction, pH 8.5, 27°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P07902 reviewed FASTA plus explicit P185S substitution reconstruction and applied mutation signature P185S to reconstruct the assayed variant sequence.

proof_lines:
recombinant mutants P185S, pH 8.7, 37°C
recombinant mutant P185S, pH 8.7, 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P07902 reviewed FASTA plus explicit P185G substitution reconstruction and applied mutation signature P185G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07902 reviewed FASTA plus explicit P185E substitution reconstruction and applied mutation signature P185E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07902 reviewed FASTA plus explicit S135L substitution reconstruction and applied mutation signature S135L to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant S135L, pH 8.7, 42-48°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P07902 reviewed FASTA plus explicit N314D substitution reconstruction and applied mutation signature N314D to reconstruct the assayed variant sequence.

proof_lines: N314D homozygous mutant from lymphoblasts, 37°C


organism: Saccharomyces cerevisiae


organism: Galdieria sulphuraria


organism: Gracilaria firma

substrate_name: UDP-alpha-D-galactose

substrate: UDP-alpha-D-galactose


sequence_source: UniProtKB reviewed accession P07902 direct EC+organism lookup

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

proof_lines: recombinant wild-type and mutants P185E and P185A, pH 8.7, 37°C


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

proof_lines:
glucose grown cells, pH 8.2
erythrocytes
galactose grown cells, pH 8.2


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB reviewed accession P07902 after direct residue check and applied mutation signature P185A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB reviewed accession P07902 after direct residue check and applied mutation signature P185Q to reconstruct the assayed variant sequence.


organism: Deinococcus radiodurans

substrate_name: Met-Pro

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

substrate: Met-Pro


substrate_name: L-Met-L-Pro

substrate: L-Met-L-Pro


organism: Homo sapiens

substrate_name: Ala-Pro

proof_lines: pH 7.8, 37°C, recombinant His-tagged mutant V833A

substrate: Ala-Pro


proof_lines: pH 7.8, 37°C, recombinant His-tagged mutants F822A and Y844A


proof_lines: pH 7.8, 37°C, recombinant His-tagged mutant F822A


proof_lines: pH 7.8, 37°C, recombinant His-tagged wild-type enzyme


organism: Sus scrofa

substrate_name: N-benzoyl-L-methionine

proof_lines: hydrolysis of N-acetyl-L-methionine substrates by Wild-Type porcine Acy1

proof_lines: hydrolysis of N-acetyl-L-glutamate substrates by Wild-Type porcine Acy1

substrate: N-benzoyl-L-methionine


organism: Thermococcus litoralis

substrate_name: N-benzoyl-L-phenylalanine

proof_lines: S100T/M106K mutant protein, pH 8.0, 55°C

substrate: N-benzoyl-L-phenylalanine


substrate_name: N-benzoyl-L-valine

substrate: N-benzoyl-L-valine


enzyme_display_name: urease

organism: Arthrobacter mobilis

substrate_name: Urea

proof_lines: pH 4.2, temperature not specified in the publication

enzyme: urease

substrate: Urea


organism: Aspergillus nidulans

proof_lines: pH 8.5, temperature not specified in the publication


organism: Aspergillus niger

proof_lines: pH 8.0, temperature not specified in the publication


organism: bacterium strain SL100


organism: Bos taurus


organism: Brucella suis

proof_lines: pH 7.0, temperature not specified in the publication


organism: Cajanus cajan

proof_lines:
alkylamine glass-immobilized urease
soluble enzyme
arylamine glass-immobilized urease


organism: Canavalia ensiformis

proof_lines: soluble urease, 37°C, pH not specified in the publication, Vmax: 200 micromol/min/mg

proof_lines: free enzyme or enzyme bound to membrane modified with NaOH + ethylendiamine and H2O2


enzyme_display_name: riboflavin kinase

organism: Arabidopsis thaliana

substrate_name: ATP; Riboflavin

sequence_source: UniProtKB reviewed Q84MD8 residues 227-379 reconstructed from selected SABIO AtFMN C-terminal 227-379 note

assay_conditions_summary: cofactor FMN

proof_lines: SABIO-RK modifier species: riboflavin kinase(Enzyme) mutant AtFMN (C-terminal 227-379)

enzyme: riboflavin kinase

substrate: ATP; Riboflavin


sequence_source: UniProtKB reviewed Q84MD8 direct REST lookup


substrate_name: ATP

assay_conditions_summary: pH 7.5; 303.15 K; cofactor FMN

substrate: ATP


substrate_name: riboflavin

substrate: riboflavin


organism: Corynebacterium ammoniagenes

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q59263 direct REST lookup plus selected mutation signature R161A and applied mutation signature R161A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 310.15 K; cofactor FMN


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q59263 and applied mutation signature S164D to reconstruct the assayed variant sequence.

column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row S164D, ATP-varied column group; column kcat (min^-1) = 55; column Km^ATP (uM) = 10; column kcat/Km^ATP (min^-1 uM^-1) = 5.3.

raw_value_unit_evidence: Table S2, enzyme row S164D, ATP-varied column group: kcat = 55 min^-1; Km^ATP = 10 uM; printed kcat/Km^ATP = 5.3 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q59263 and applied mutation signature R161D to reconstruct the assayed variant sequence.

column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row R161D, riboflavin-varied column group; column kcat (min^-1) = 300; column Km^RF (uM) = 13; column kcat/Km^RF (min^-1 uM^-1) = 23; column Ki (uM) = 5.1.

raw_value_unit_evidence: Table S2, enzyme row R161D, riboflavin-varied column group: kcat = 300 min^-1; Km^RF = 13 uM; printed kcat/Km^RF = 23 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q59263 and applied mutation signature T165A to reconstruct the assayed variant sequence.

column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row T165A, ATP-varied column group; column kcat (min^-1) = 66; column Km^ATP (uM) = 12; column kcat/Km^ATP (min^-1 uM^-1) = 5.4.

raw_value_unit_evidence: Table S2, enzyme row T165A, ATP-varied column group: kcat = 66 min^-1; Km^ATP = 12 uM; printed kcat/Km^ATP = 5.4 min^-1 uM^-1.


substrate_name: N-Cbz-Gly-L-Ala

substrate: N-Cbz-Gly-L-Ala


substrate_name: Nalpha-acetylmethionine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q03154 (ACY1_HUMAN); D274A reconstructed by direct residue check against the canonical sequence and applied mutation signature D274A to reconstruct the assayed variant sequence.

substrate: Nalpha-acetylmethionine


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q03154 (ACY1_HUMAN); R276A reconstructed by direct residue check against the canonical sequence and applied mutation signature R276A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed Q03154 (ACY1_HUMAN)

proof_lines: pH 7.4, 22°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q03154 (ACY1_HUMAN); N263D reconstructed by direct residue check against the canonical sequence and applied mutation signature N263D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q03154 (ACY1_HUMAN); H206A reconstructed by direct residue check against the canonical sequence and applied mutation signature H206A to reconstruct the assayed variant sequence.


enzyme_display_name: serine O-acetyltransferase

substrate_name: acetyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q39218 direct lookup; row-specific G354A reconstruction from canonical sequence and applied mutation signature G354A to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor CoA

enzyme: serine O-acetyltransferase

substrate: acetyl-CoA


substrate_name: L-serine

sequence_source: UniProtKB reviewed accession Q39218 direct lookup

substrate: L-serine


substrate_name: Acetyl-CoA; L-Serine

sequence_source: UniProtKB reviewed accession Q8S895 direct lookup

substrate: Acetyl-CoA; L-Serine


substrate_name: L-Serine; Acetyl-CoA

sequence_source: UniProtKB reviewed accession Q8W2B8 direct lookup

substrate: L-Serine; Acetyl-CoA


sequence_source: UniProtKB reviewed accession Q42588 direct lookup


sequence_source: UniProtKB reviewed accession Q42538 direct lookup


organism: Escherichia coli

substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A9D4 canonical sequence with row mutation_signature V95R/D96P reconstructed after direct residue check and applied mutation signature V95R/D96P to reconstruct the assayed variant sequence.

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A9D4 canonical sequence with row mutation_signature V95G/D96G reconstructed after direct residue check and applied mutation signature V95G/D96G to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P0A9D4 canonical sequence


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


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A9D4 canonical sequence with row mutation_signature V95L/D96P reconstructed after direct residue check and applied mutation signature V95L/D96P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A9D4 canonical sequence with row mutation_signature R89H/T90V/P93A/A94T reconstructed after direct residue check and applied mutation signature R89H/T90V/P93A/A94T to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH 7.5, mutant enzyme R89H/T90V/P93A/A94T


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A9D4 canonical sequence with row mutation_signature A94T reconstructed after direct residue check and applied mutation signature A94T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A9D4 canonical sequence with row mutation_signature R89P reconstructed after direct residue check and applied mutation signature R89P to reconstruct the assayed variant sequence.


organism: Entamoeba histolytica

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

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme Q335/Q336

proof_lines: isozyme SAT3 mutant S208HS, pH 8.0, temperature not specified in the publication, in presence of 10 mM L-cysteine


mutation_signature: Δ3

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme DELTA3


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme DELTA22


mutation_signature: Δ2

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme DELTA2


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

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: 72 micromol, 0.1 M Tris-HCl, pH 7.5, room temperature


proof_lines: SABIO-RK modifier species: serine O-acetyltransferase(Enzyme) mutant 20 amino acids deleted at C-terminus


substrate_name: Coenzyme A; O-Acetyl-L-serine

substrate: Coenzyme A; O-Acetyl-L-serine


sequence_source: UniProtKB Q39218 direct REST/FASTA lookup

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


organism: Brucella abortus

proof_lines: recombinant enzyme, pH 8.0, temperature not specified in the publication, in presence of 5 mM L-cysteine

proof_lines: recombinant enzyme, pH 8.0, temperature not specified in the publication, in presence of 10 mM L-cysteine


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

sequence_source: UniProtKB Q401L4 direct REST/FASTA lookup

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

proof_lines: 50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25°C

proof_lines: SAT2, 50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C

source_databases_merged: brenda skid


sequence_source: UniProtKB Q401L5 direct REST/FASTA lookup

proof_lines: 50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C

proof_lines: SAT2, 50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q401L4 direct REST/FASTA lookup plus S208H reconstruction from selected source mutation signature and applied mutation signature S208H to reconstruct the assayed variant sequence.

proof_lines: isozyme SAT3 mutant S208H, pH 8.0, temperature not specified in the publication


proof_lines: pH 8.0, temperature not specified in the publication, wild-type

proof_lines: wild-type isozyme SAT3, pH 8.0, temperature not specified in the publication, in presence of 10 mM L-cysteine


mutation_signature: Δ5

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme DELTA5


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme DELTA68


sequence_variant_note: Resolved canonical sequence from UniProt P0A9D4 canonical sequence reconstructed with M256I from selected BRENDA mutation note and applied mutation signature M256I to reconstruct the assayed variant sequence.


sequence_source: UniProt P0A9D4/P0A9D5/P0A9D6 direct lookup; all listed E. coli CYSE accessions share this sequence


organism: Haemophilus influenzae

sequence_source: UniProt P43886 direct lookup

assay_conditions_summary: pH 7.75; cofactor CoA


sequence_variant_note: Resolved canonical sequence from UniProt P43886 canonical sequence reconstructed with H154N/H189N from selected BRENDA mutation notes and applied mutation signature H154N/H189N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P43886 canonical sequence reconstructed with H189N from selected BRENDA mutation note and applied mutation signature H189N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P43886 canonical sequence reconstructed with H154N from selected BRENDA mutation notes and applied mutation signature H154N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P43886 canonical sequence reconstructed with D139N from selected BRENDA mutation notes and applied mutation signature D139N to reconstruct the assayed variant sequence.


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA


organism: Streptomyces lavendulae

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D2Z028 and applied mutation signature P55G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; buffer 60 mM Tris-HCl; cofactor CoA

column_label: Table 2 (Kinetic parameters of DcsE and its mutants). Enzyme row 'P55G'. The table splits into two substrate column groups headed 'L-Serine' and 'L-Homoserine'; this record reads the 'L-Serine' group. Inside that group the printed column heads are 'Km (mM)' = 0.50, 'kcat (min^-1)' = 37 and 'kcat/Km (min^-1 mM^-1)' = 74. The final 'Specificity' column of the table is the ratio of the two kcat/Km cells of the row (table footnote b) and belongs to neither substrate group.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.50 mM; the printed unit is already mM, so no unit conversion applies, giving 0.5 mM. kcat: printed Table 2 cell 37 min^-1; one min^-1 is 1/60 s^-1, so 37 / 60 = 0.6166666666666667 s^(-1). kcat/Km: printed Table 2 cell 74 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 74 / 60 = 1.2333333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Enzyme row 'P55G', L-Serine column group: Km (mM) = 0.50; kcat (min^-1) = 37; kcat/Km (min^-1 mM^-1) = 74.

row_label: Table 2, Enzyme row 'P55G', L-Serine column group (Km, kcat and kcat/Km columns for L-Serine)

table_label: Table 2: Kinetic parameters of DcsE and its mutants (Journal of Bacteriology 2013, 195(8):1741-1749)


organism: Thermus thermophilus HB8

sequence_source: UniProtKB:Q6F4D7 exact accession lookup

assay_conditions_summary: pH 7.8; 303.15 K; cofactor CoA


organism: Trypanosoma cruzi

sequence_source: UniProtKB:Q9BKB1 exact accession lookup


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q59263 and applied mutation signature R161A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row R161A, ATP-varied column group; column kcat (min^-1) = 65; column Km^ATP (uM) = 12; column kcat/Km^ATP (min^-1 uM^-1) = 5.6.

raw_value_unit_evidence: Table S2, enzyme row R161A, ATP-varied column group: kcat = 65 min^-1; Km^ATP = 12 uM; printed kcat/Km^ATP = 5.6 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q59263 and applied mutation signature S164A to reconstruct the assayed variant sequence.

column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row S164A, ATP-varied column group; column kcat (min^-1) = 59; column Km^ATP (uM) = 12; column kcat/Km^ATP (min^-1 uM^-1) = 5.0.

raw_value_unit_evidence: Table S2, enzyme row S164A, ATP-varied column group: kcat = 59 min^-1; Km^ATP = 12 uM; printed kcat/Km^ATP = 5.0 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q59263 and applied mutation signature H28D to reconstruct the assayed variant sequence.

column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row H28D, riboflavin-varied column group; column kcat (min^-1) = 287; column Km^RF (uM) = 25; column kcat/Km^RF (min^-1 uM^-1) = 12; column Ki (uM) = 1.9.

raw_value_unit_evidence: Table S2, enzyme row H28D, riboflavin-varied column group: kcat = 287 min^-1; Km^RF = 25 uM; printed kcat/Km^RF = 12 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q59263 canonical sequence with H31A reconstructed and applied mutation signature H31A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q59263 and applied mutation signature R161D to reconstruct the assayed variant sequence.

row_label: Table S2, enzyme row R161D, riboflavin-varied column group

table_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WJY9 canonical sequence; A59G reconstructed during review and applied mutation signature A59G to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, serine O-acetyltransferase activity, mutant enzyme A59G


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WJY9 canonical sequence; A59G/G62P reconstructed during review and applied mutation signature A59G/G62P to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, serine O-acetyltransferase activity, mutant enzyme A59G/G62P


sequence_source: UniProtKB:P9WJY9 direct REST lookup

proof_lines: pH 7.5, 25°C, serine O-acetyltransferase activity, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WJY9 canonical sequence; G62P reconstructed during review and applied mutation signature G62P to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, serine O-acetyltransferase activity, mutant enzyme G62P


sequence_source: UniProtKB:P95231 direct REST lookup

proof_lines:
pH 7.5, 25°C, hexamer
pH 7.5, 25°C, trimer
pH 7.5, 25°C, dodecamer


organism: Neisseria gonorrhoeae

sequence_source: UniProtKB:Q5F6X0 direct REST lookup

assay_conditions_summary: pH 8; 295.15 K; cofactor CoA


organism: Salmonella enterica subsp. enterica serovar Typhimurium

sequence_source: UniProtKB:A0A0D6I3Y9 direct REST lookup

proof_lines: pH and temperature not specified in the publication


sequence_source: UniProtKB:D2Z028 direct REST lookup

proof_lines: recombinant His-tagged wild-type enzyme, pH 8.0, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q59263 and applied mutation signature H31A to reconstruct the assayed variant sequence.

column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row H31A, riboflavin-varied column group; column kcat (min^-1) = 169; column Km^RF (uM) = 4.5; column kcat/Km^RF (min^-1 uM^-1) = 37; column Ki (uM) = 6.3.

raw_value_unit_evidence: Table S2, enzyme row H31A, riboflavin-varied column group: kcat = 169 min^-1; Km^RF = 4.5 uM; printed kcat/Km^RF = 37 min^-1 uM^-1.


substrate_name: riboflavin and ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB Q59263 canonical sequence with row-specific T165D reconstruction after residue-offset check and applied mutation signature T165D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C

substrate: riboflavin and ATP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q59263 and applied mutation signature T165D to reconstruct the assayed variant sequence.

column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row T165D, riboflavin-varied column group; column kcat (min^-1) = 180; column Km^RF (uM) = 7.7; column kcat/Km^RF (min^-1 uM^-1) = 23; column Ki (uM) = 4.1.

raw_value_unit_evidence: Table S2, enzyme row T165D, riboflavin-varied column group: kcat = 180 min^-1; Km^RF = 7.7 uM; printed kcat/Km^RF = 23 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q59263 canonical sequence with row-specific N125A reconstruction after residue-offset check and applied mutation signature N125A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C


column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row R161D, ATP-varied column group; column kcat (min^-1) = 68; column Km^ATP (uM) = 11; column kcat/Km^ATP (min^-1 uM^-1) = 6.1.

raw_value_unit_evidence: Table S2, enzyme row R161D, ATP-varied column group: kcat = 68 min^-1; Km^ATP = 11 uM; printed kcat/Km^ATP = 6.1 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q59263 and applied mutation signature H28A to reconstruct the assayed variant sequence.

column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row H28A, riboflavin-varied column group; column kcat (min^-1) = 427; column Km^RF (uM) = 23; column kcat/Km^RF (min^-1 uM^-1) = 18; column Ki (uM) = 1.8.

raw_value_unit_evidence: Table S2, enzyme row H28A, riboflavin-varied column group: kcat = 427 min^-1; Km^RF = 23 uM; printed kcat/Km^RF = 18 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q59263 and applied mutation signature N125D to reconstruct the assayed variant sequence.

column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row N125D, ATP-varied column group; column kcat (min^-1) = 80; column Km^ATP (uM) = 35; column kcat/Km^ATP (min^-1 uM^-1) = 2.3.

raw_value_unit_evidence: Table S2, enzyme row N125D, ATP-varied column group: kcat = 80 min^-1; Km^ATP = 35 uM; printed kcat/Km^ATP = 2.3 min^-1 uM^-1.


column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row H28A, ATP-varied column group; column kcat (min^-1) = 45; column Km^ATP (uM) = 14; column kcat/Km^ATP (min^-1 uM^-1) = 3.1.

raw_value_unit_evidence: Table S2, enzyme row H28A, ATP-varied column group: kcat = 45 min^-1; Km^ATP = 14 uM; printed kcat/Km^ATP = 3.1 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q59263 and applied mutation signature T165A to reconstruct the assayed variant sequence.

row_label: Table S2, enzyme row T165A, ATP-varied column group


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q59263 REST/FASTA direct lookup and applied mutation signature R161A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C


column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row T165A, riboflavin-varied column group; column kcat (min^-1) = 171; column Km^RF (uM) = 10; column kcat/Km^RF (min^-1 uM^-1) = 17; column Ki (uM) = 3.2.

raw_value_unit_evidence: Table S2, enzyme row T165A, riboflavin-varied column group: kcat = 171 min^-1; Km^RF = 10 uM; printed kcat/Km^RF = 17 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q59263 and applied mutation signature N125A to reconstruct the assayed variant sequence.

column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row N125A, ATP-varied column group; column kcat (min^-1) = 46; column Km^ATP (uM) = 24; column kcat/Km^ATP (min^-1 uM^-1) = 1.9.

raw_value_unit_evidence: Table S2, enzyme row N125A, ATP-varied column group: kcat = 46 min^-1; Km^ATP = 24 uM; printed kcat/Km^ATP = 1.9 min^-1 uM^-1.


column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row N125D, riboflavin-varied column group; column kcat (min^-1) = 415; column Km^RF (uM) = 16; column kcat/Km^RF (min^-1 uM^-1) = 26; column Ki (uM) = 3.3.

raw_value_unit_evidence: Table S2, enzyme row N125D, riboflavin-varied column group: kcat = 415 min^-1; Km^RF = 16 uM; printed kcat/Km^RF = 26 min^-1 uM^-1.


column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row S164A, riboflavin-varied column group; column kcat (min^-1) = 259; column Km^RF (uM) = 8.8; column kcat/Km^RF (min^-1 uM^-1) = 29; column Ki (uM) = 4.4.

raw_value_unit_evidence: Table S2, enzyme row S164A, riboflavin-varied column group: kcat = 259 min^-1; Km^RF = 8.8 uM; printed kcat/Km^RF = 29 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q59263 REST/FASTA direct lookup and applied mutation signature S164D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C


sequence_source: UniProtKB reviewed Q59263 REST/FASTA direct lookup

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

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

proof_lines: pH 7.0, 25°C, recombinant wild-type enzyme


enzyme_display_name: insulysin

organism: Homo sapiens

substrate_name: amyloid beta-peptide 1-42

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

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

enzyme: insulysin

substrate: amyloid beta-peptide 1-42


substrate_name: Abz-GGFLRKHGQ-EDDnp

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Swiss-Prot P14735, fetched from rest.uniprot.org on 2026-06-06; row-specific variant reconstructed from the canonical sequence where applicable. and applied mutation signature D426A to reconstruct the assayed variant sequence.

substrate: Abz-GGFLRKHGQ-EDDnp


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Swiss-Prot P14735, fetched from rest.uniprot.org on 2026-06-06; row-specific variant reconstructed from the canonical sequence where applicable. and applied mutation signature F807A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Swiss-Prot P14735, fetched from rest.uniprot.org on 2026-06-06; row-specific variant reconstructed from the canonical sequence where applicable. and applied mutation signature S137A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Swiss-Prot P14735, fetched from rest.uniprot.org on 2026-06-06; row-specific variant reconstructed from the canonical sequence where applicable. and applied mutation signature K364A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Swiss-Prot P14735, fetched from rest.uniprot.org on 2026-06-06; row-specific variant reconstructed from the canonical sequence where applicable. and applied mutation signature K898A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed Swiss-Prot P14735, fetched from rest.uniprot.org on 2026-06-06; row-specific variant reconstructed from the canonical sequence where applicable.


column_label: Table S2: Steady-state kinetic parameters for the RFK activity (RF + ATP -> FMN + ADP) of the different CaFADS forms (International Journal of Molecular Sciences 2012, volume 13, issue 11, pages 14492-14517), enzyme row N125A, riboflavin-varied column group; column kcat (min^-1) = 111; column Km^RF (uM) = 1.7; column kcat/Km^RF (min^-1 uM^-1) = 65; column Ki (uM) = 4.6.

raw_value_unit_evidence: Table S2, enzyme row N125A, riboflavin-varied column group: kcat = 111 min^-1; Km^RF = 1.7 uM; printed kcat/Km^RF = 65 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q59263 direct lookup; R66A variant reconstructed after residue check. and applied mutation signature R66A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q59263 direct lookup; R66E variant reconstructed after residue check. and applied mutation signature R66E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession Q59263 direct lookup; R66E variant reconstructed after residue check.

proof_lines:
mutant enzyme R66E, at pH 7.0 and 25°C
pH 7.0, 25°C, recombinant mutant R66E


sequence_source: UniProtKB reviewed accession Q59263 direct lookup.


sequence_source: UniProtKB/RCSB identity only; construct-specific RFK-module sequence not resolved.

proof_lines: pH 7.0, 25°C, recombinant RFK activity of the RFK module, Michaelis-Menten kinetics

proof_lines: pH 7.0, 25°C, recombinant RFK activity of the RFK module, Lineweaver-Burk equation kinetics


sequence_source: UniProtKB Q969G6 direct accession lookup; reviewed entry RIFK_HUMAN


proof_lines:
pH 7.0, 25°C, recombinant enzyme
Raw SKiD Env: Temp=25°C, pH=7


organism: Streptomyces davaonensis

substrate_name: roseoflavin

sequence_source: UniProtKB A3FM23 direct accession lookup; unreviewed TrEMBL entry A3FM23_9ACTN

substrate: roseoflavin


substrate_name: Insulin

sequence_source: UniProtKB P14735 direct accession lookup; reviewed entry IDE_HUMAN

proof_lines:
isoform 15b-IDE, pH 7.4, 37°C
pH 7.4, 37°C
isoform 15a-IDE, pH 7.4, 37°C

substrate: Insulin


substrate_name: amyloid beta-peptide1-40

proof_lines: recombinant wild-type enzyme, pH 7.4, 37°C

substrate: amyloid beta-peptide1-40


sequence_variant_note: Resolved canonical sequence from UniProtKB P14735 direct accession lookup plus D426C/K899C reconstruction from the canonical FASTA sequence and applied mutation signature D426C/K899C to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant D426C/K899C, pH 7.4, 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P14735 canonical sequence with BRENDA/source mutation note F202D applied after residue check. and applied mutation signature F202D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P14735 canonical sequence with BRENDA/source mutation note W199A applied after residue check. and applied mutation signature W199A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P14735 canonical sequence with BRENDA/source mutation note F141N applied after residue check. and applied mutation signature F141N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P14735 canonical sequence with BRENDA/source mutation note F202N applied after residue check. and applied mutation signature F202N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P14735 canonical sequence with BRENDA/source mutation note W199K applied after residue check. and applied mutation signature W199K to reconstruct the assayed variant sequence.


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

proof_lines:
pH 7.3, 37°C, mutant enzyme 141Y
pH 7.3, 37°C, mutant enzyme 141A
pH 7.3, 37°C, mutant enzyme 141W


sequence_variant_note: Resolved canonical sequence from UniProtKB P14735 canonical sequence with BRENDA/source mutation note F115A applied after residue check. and applied mutation signature F115A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P14735 canonical sequence with BRENDA/source mutation note F141Y applied after residue check. and applied mutation signature F141Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14735 canonical sequence via UniProt REST; row-specific substitution applied after residue check. and applied mutation signature F807A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14735 canonical sequence via UniProt REST; row-specific substitution applied after residue check. and applied mutation signature S137A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14735 canonical sequence via UniProt REST; row-specific substitution applied after residue check. and applied mutation signature D426A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14735 canonical sequence via UniProt REST; row-specific substitution applied after residue check. and applied mutation signature K898A to reconstruct the assayed variant sequence.


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


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14735 canonical sequence via UniProt REST; row-specific substitution applied after residue check. and applied mutation signature F202Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14735 canonical sequence via UniProt REST; row-specific substitution applied after residue check. and applied mutation signature F820W to reconstruct the assayed variant sequence.


enzyme_display_name: Bifunctional riboflavin kinase/FMN adenylyltransferase

enzyme_name_source: UniProtKB Q59263

sequence_variant_note: Resolved canonical sequence from UniProtKB Q59263 canonical FASTA; variant reconstructed by applying reviewed source mutation and applied mutation signature H31A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q59263 canonical FASTA; variant reconstructed by applying reviewed source mutation and applied mutation signature H28D to reconstruct the assayed variant sequence.

enzyme: Bifunctional riboflavin kinase/FMN adenylyltransferase


sequence_variant_note: Resolved canonical sequence from UniProtKB Q59263 canonical FASTA; variant reconstructed by applying reviewed source mutation and applied mutation signature T165D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q59263 canonical FASTA; variant reconstructed by applying reviewed source mutation and applied mutation signature S164A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C


sequence_source: UniProtKB Q59263 canonical FASTA; variant reconstructed by applying reviewed source mutation

proof_lines: mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q59263 canonical FASTA; variant reconstructed by applying reviewed source mutation and applied mutation signature N125D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q59263 canonical FASTA; variant reconstructed by applying reviewed source mutation and applied mutation signature H28A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q59263 canonical FASTA; variant reconstructed by applying reviewed source mutation and applied mutation signature S164D to reconstruct the assayed variant sequence.


enzyme_display_name: adenine phosphoribosyltransferase

organism: Triticum aestivum

sequence_source: UniProtKB:Q43199 direct REST lookup 2026-06-06

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

enzyme: adenine phosphoribosyltransferase


organism: Trypanosoma brucei brucei

substrate_name: adenine

sequence_source: UniProtKB:Q57V32 direct REST lookup 2026-06-06

proof_lines: isoform APRT1, at pH 8.3, temperature not specified in the publication

proof_lines: Ki above 0.03 mM, pH and temperature not specified in the publication

substrate: adenine


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

sequence_source: UniProtKB:Q57V31 direct REST lookup 2026-06-06

proof_lines: isoform APRT2, at pH 8.3, temperature not specified in the publication

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


organism: Candida albicans

sequence_source: UniProtKB:A0A1D8PG20 direct REST lookup 2026-06-06

proof_lines: pH and temperature not specified in the publication, with L-glutamate

proof_lines: pH and temperature not specified in the publication, with 2-oxoglutarate


substrate_name: L-tryptophan

sequence_source: UniProtKB:A0A1D8PPA8 direct REST lookup 2026-06-06

proof_lines: pH and temperature not specified in the publication

substrate: L-tryptophan


sequence_source: UniProtKB:A0A1D8PMC5 direct REST lookup 2026-06-06


organism: Klebsiella pneumoniae

sequence_source: UniProtKB:O85746 direct REST lookup 2026-06-06


organism: Paracoccus denitrificans

substrate_name: L-aspartate

sequence_source: UniProtKB:P95468 direct REST lookup 2026-06-06

proof_lines:
at pH 7.4 and 30°C
pH 8.0, 25°C, cosubstrate aspartate
pH 8.0, 25°C, cosubstrate tryptophan

substrate: L-aspartate


organism: Saccharomyces cerevisiae

substrate_name: L-Tryptophan; 2-Oxoglutarate

sequence_source: UniProtKB reviewed accession P53090 direct lookup, 2026-06-06

substrate: L-Tryptophan; 2-Oxoglutarate


substrate_name: L-Tryptophan; Phenylpyruvate

sequence_source: UniProtKB reviewed accession P38840 direct lookup, 2026-06-06

substrate: L-Tryptophan; Phenylpyruvate


organism: Thermococcus litoralis

substrate_name: 2-Oxoglutarate; L-Phenylalanine

sequence_source: UniProtKB reviewed accession H3ZPU1 direct lookup, 2026-06-06; Q9UWK8 resolves to this live primary accession

substrate: 2-Oxoglutarate; L-Phenylalanine


sequence_source: UniProtKB reviewed accession H3ZPL1 direct lookup, 2026-06-06; Q9UWK9 resolves to this live primary accession


enzyme_display_name: choline kinase

substrate_name: Choline; ATP

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

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: SABIO-RK modifier species: choline kinase(Enzyme) mutant CK-alpha2 delta49N

proof_lines: mutant enzyme ChoKalphaDELTA49, pH 7.5, 37°C

enzyme: choline kinase

substrate: Choline; ATP


substrate_name: ATP

sequence_source: UniProtKB reviewed accession P35790 direct lookup, 2026-06-06

substrate: ATP


assay_conditions_summary: pH 7.5; 298.15 K; buffer 100 mM Tris-HCl; cofactor ATP

proof_lines: in 100 mM Tris-HCl pH 7.5, 100 mM KCl, 10 mM MgCl2, at 25°C

proof_lines: in 100 mM Tris-HCl buffer (pH 7.5) containing 100 mM KCl, 10 mM MgCl2, 0.5 mM phosphoenolpyruvate, 0.25 mM NADH, 4 units pyruvate kinase, and 5 units lactate dehydrogenase


substrate_name: Choline

smiles: C[N+](C)(C)CCO

substrate: Choline


sequence_source: UniProtKB:P07741 canonical sequence, direct REST lookup on 2026-06-06


organism: Mycoplasma mycoides

sequence_source: UniProtKB:Q6MTD4 canonical sequence, direct REST lookup on 2026-06-06


organism: Rattus norvegicus

sequence_source: UniProtKB:P36972 canonical sequence, direct REST lookup on 2026-06-06


organism: Saccharolobus solfataricus

sequence_source: UniProtKB:Q97W95 canonical sequence, direct REST lookup on 2026-06-06


substrate_name: Unknown

sequence_source: UniProtKB:P49435 canonical sequence, direct REST lookup on 2026-06-06

substrate: Unknown


organism: Schistosoma mansoni

sequence_source: UniProtKB:G4VQJ4 canonical sequence, direct REST lookup on 2026-06-06


enzyme_display_name: homoserine O-acetyltransferase

organism: Streptomyces lavendulae

substrate_name: L-homoserine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D2Z028 and applied mutation signature G52A/P55G to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of DcsE and its mutants). Enzyme row 'G52A-P55G'. The table splits into two substrate column groups headed 'L-Serine' and 'L-Homoserine'; this record reads the 'L-Homoserine' group. Inside that group the printed column heads are 'Km (mM)' = 2.0, 'kcat (min^-1)' = 47 and 'kcat/Km (min^-1 mM^-1)' = 24. The final 'Specificity' column of the table is the ratio of the two kcat/Km cells of the row (table footnote b) and belongs to neither substrate group.

normalized_value_unit_evidence: Km: printed Table 2 cell 2.0 mM; the printed unit is already mM, so no unit conversion applies, giving 2.0 mM. kcat: printed Table 2 cell 47 min^-1; one min^-1 is 1/60 s^-1, so 47 / 60 = 0.7833333333333333 s^(-1). kcat/Km: printed Table 2 cell 24 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 24 / 60 = 0.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Enzyme row 'G52A-P55G', L-Homoserine column group: Km (mM) = 2.0; kcat (min^-1) = 47; kcat/Km (min^-1 mM^-1) = 24.

row_label: Table 2, Enzyme row 'G52A-P55G', L-Homoserine column group (Km, kcat and kcat/Km columns for L-Homoserine)

enzyme: homoserine O-acetyltransferase

substrate: L-homoserine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D2Z028 and applied mutation signature G52A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of DcsE and its mutants). Enzyme row 'G52A'. The table splits into two substrate column groups headed 'L-Serine' and 'L-Homoserine'; this record reads the 'L-Homoserine' group. Inside that group the printed column heads are 'Km (mM)' = 25, 'kcat (min^-1)' = 13 and 'kcat/Km (min^-1 mM^-1)' = 0.52. The final 'Specificity' column of the table is the ratio of the two kcat/Km cells of the row (table footnote b) and belongs to neither substrate group.

normalized_value_unit_evidence: Km: printed Table 2 cell 25 mM; the printed unit is already mM, so no unit conversion applies, giving 25.0 mM. kcat: printed Table 2 cell 13 min^-1; one min^-1 is 1/60 s^-1, so 13 / 60 = 0.21666666666666667 s^(-1). kcat/Km: printed Table 2 cell 0.52 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.52 / 60 = 0.008666666666666666 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Enzyme row 'G52A', L-Homoserine column group: Km (mM) = 25; kcat (min^-1) = 13; kcat/Km (min^-1 mM^-1) = 0.52.

row_label: Table 2, Enzyme row 'G52A', L-Homoserine column group (Km, kcat and kcat/Km columns for L-Homoserine)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D2Z028 and applied mutation signature P55G to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of DcsE and its mutants). Enzyme row 'P55G'. The table splits into two substrate column groups headed 'L-Serine' and 'L-Homoserine'; this record reads the 'L-Homoserine' group. Inside that group the printed column heads are 'Km (mM)' = 1.0, 'kcat (min^-1)' = 38 and 'kcat/Km (min^-1 mM^-1)' = 38. The final 'Specificity' column of the table is the ratio of the two kcat/Km cells of the row (table footnote b) and belongs to neither substrate group.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.0 mM; the printed unit is already mM, so no unit conversion applies, giving 1.0 mM. kcat: printed Table 2 cell 38 min^-1; one min^-1 is 1/60 s^-1, so 38 / 60 = 0.6333333333333333 s^(-1). kcat/Km: printed Table 2 cell 38 min^-1 mM^-1; one min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 38 / 60 = 0.6333333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Enzyme row 'P55G', L-Homoserine column group: Km (mM) = 1.0; kcat (min^-1) = 38; kcat/Km (min^-1 mM^-1) = 38.

row_label: Table 2, Enzyme row 'P55G', L-Homoserine column group (Km, kcat and kcat/Km columns for L-Homoserine)


organism: Arabidopsis thaliana

sequence_source: UniProtKB P31166 canonical sequence retrieved by exact accession lookup.


substrate_name: benzyladenine

sequence_source: UniProtKB Q42563 canonical sequence retrieved by exact accession lookup.

substrate: benzyladenine


sequence_source: UniProtKB Q9SUW2 canonical sequence retrieved by exact accession lookup.


organism: Escherichia coli

sequence_source: UniProtKB P69503 canonical sequence retrieved by exact accession lookup.


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Acinetobacter baylyi

substrate_name: L-Homoserine; Acetyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q6FEQ3; variant reconstructed from selected SABIO-RK R323L note and UniProt mutagenesis evidence. and applied mutation signature R323L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: homoserine O-acetyltransferase(Enzyme) mutant MetX R323L

substrate: L-Homoserine; Acetyl-CoA


organism: Haemophilus influenzae

sequence_source: UniProtKB reviewed accession P45131 direct FASTA/TSV lookup.


organism: Leptospira interrogans

substrate_name: Acetyl-CoA; L-Homoserine

sequence_source: UniProtKB reviewed accession Q8F4I0 direct FASTA/TSV lookup.

substrate: Acetyl-CoA; L-Homoserine


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB reviewed accession P9WJY9 direct FASTA/TSV lookup.

proof_lines:
pH 7.5, 25°C
at pH 7.5 and 25°C


substrate_name: acetyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WJY9; variant reconstructed from selected BRENDA A59G/G62P note and PubMed 34090964 abstract context. and applied mutation signature A59G/G62P to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, homoserine O-acetyltransferase activity, mutant enzyme A59G/G62P

substrate: acetyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WJY9; variant reconstructed from selected BRENDA L322R note and PubMed 34090964 abstract context. and applied mutation signature L322R to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, homoserine O-acetyltransferase activity, mutant enzyme L322R


proof_lines: pH 7.5, 25°C, homoserine O-acetyltransferase activity, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P9WJY9; variant reconstructed from selected BRENDA G62P source note. and applied mutation signature G62P to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, homoserine O-acetyltransferase activity, mutant enzyme G62P


sequence_variant_note: Resolved canonical sequence from UniProt P9WJY9 canonical sequence with directly checked A59G reconstruction and applied mutation signature A59G to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, homoserine O-acetyltransferase activity, mutant enzyme A59G


organism: Mycolicibacterium smegmatis

sequence_source: UniProt A0QSZ0 via RCSB 6IOG/6IOH/6IOI SIFTS mapping from PMID 31378370

proof_lines: recombinant His-tagged enzyme, pH 8.0, 22°C


proof_lines: SABIO-RK modifier species: homoserine O-acetyltransferase(Enzyme) mutant thiosulfate deficient, requiring methionine


substrate_name: L-Homoserine

substrate: L-Homoserine


sequence_source: UniProt D2Z028 canonical sequence


proof_lines: recombinant His-tagged wild-type enzyme, pH 8.0, 30°C


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from UniProtKB:P14735 REST API exact accession lookup on 2026-06-06 and applied mutation signature F141W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14735 REST API exact accession lookup on 2026-06-06 and applied mutation signature F141A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14735 REST API exact accession lookup on 2026-06-06 and applied mutation signature W199N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14735 REST API exact accession lookup on 2026-06-06 and applied mutation signature Y150F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14735 REST API exact accession lookup on 2026-06-06 and applied mutation signature W199F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14735 REST API exact accession lookup on 2026-06-06 and applied mutation signature F115Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14735 REST API exact accession lookup on 2026-06-06 and applied mutation signature Y150K to reconstruct the assayed variant sequence.


organism: Mus musculus

sequence_source: UniProtKB:Q9JHR7 REST API 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.

proof_lines: pH and temperature not specified in the publication, substrate: insulin


substrate_name: ATP; Choline

sequence_source: UniProtKB Q9Y259 direct REST/FASTA lookup on 2026-06-06

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: phosphorylated choline kinase beta, at pH 7.5 and 30°C

substrate: ATP; Choline


substrate_name: choline

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9Y259 direct REST/FASTA lookup on 2026-06-06; F352L reconstructed by residue substitution and applied mutation signature F352L to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ATP

proof_lines: isoform ChoKbeta mutant F352L, pH and temperature not specified in the publication

substrate: choline


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9Y259 direct REST/FASTA lookup on 2026-06-06; F352A reconstructed by residue substitution and applied mutation signature F352A to reconstruct the assayed variant sequence.

proof_lines: isoform ChoKbeta mutant F352A, pH and temperature not specified in the publication


sequence_source: UniProtKB P35790 direct REST/FASTA lookup on 2026-06-06; variant not reconstructed because residue 352 is not F

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

proof_lines: isoform ChoKalpha2 mutant F352A, pH and temperature not specified in the publication


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


proof_lines: isoform ChoKalpha2 mutant F352L, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9Y259 direct REST/FASTA lookup on 2026-06-06; S39D/S40D reconstructed by residue substitutions and applied mutation signature S39D/S40D to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9Y259 direct REST/FASTA lookup on 2026-06-06; S39D/S40D reconstructed by residue substitutions


proof_lines: SABIO-RK modifier species: insulysin(Enzyme) mutant H111L


proof_lines: SABIO-RK modifier species: insulysin(Enzyme) mutant H111V


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P35559 after direct residue check; H112Q applied once to canonical rat IDE. and applied mutation signature H112Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: insulysin(Enzyme) mutant H112Q


proof_lines: SABIO-RK modifier species: insulysin(Enzyme) mutant H111F


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P35559 after direct residue check; H112D applied once to canonical rat IDE. and applied mutation signature H112D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: insulysin(Enzyme) mutant H112D


proof_lines: SABIO-RK modifier species: insulysin(Enzyme) mutant H111A


sequence_source: UniProtKB:P35559 direct REST lookup; reviewed rat IDE, EC 3.4.24.56.


organism: Danio rerio

substrate_name: CDP-choline

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q7T291 after direct residue check; H97A applied once to canonical zebrafish ADPRM. and applied mutation signature H97A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor ADP

proof_lines: mutant H97A, pH 7.5, temperature not specified in the publication

substrate: CDP-choline


sequence_source: UniProtKB Q7T291 FASTA, checked 2026-06-06

proof_lines: wild-type, pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 FASTA with residue 37 F changed to Y, checked 2026-06-06 and applied mutation signature F37Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 FASTA with residues 37 F->A and 196 L->A, checked 2026-06-06 and applied mutation signature F37A/L196A to reconstruct the assayed variant sequence.


substrate_name: ADP-ribose

sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 FASTA with residue 27 Q changed to H, checked 2026-06-06 and applied mutation signature Q27H to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP

substrate: ADP-ribose


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 FASTA with residue 111 H changed to N, checked 2026-06-06 and applied mutation signature H111N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 FASTA with residue 37 F changed to A, checked 2026-06-06 and applied mutation signature F37A to reconstruct the assayed variant sequence.