proof_lines: Km above 0.4 mM, mutant enzyme V300D, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication

proof_lines: Km above 0.028 mM, mutant enzyme V300D, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication


organism: Neisseria meningitidis

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

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

km_unit: mM

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

mutation_type: substitution

proof_lines: SABIO-RK modifier species: peptide-methionine (S)-S-oxide reductase(Enzyme) mutant MsrA D129N


proof_lines: SABIO-RK modifier species: peptide-methionine (S)-S-oxide reductase(Enzyme) mutant MsrA F52L


proof_lines: SABIO-RK modifier species: peptide-methionine (S)-S-oxide reductase(Enzyme) mutant MsrA Y197F


proof_lines: SABIO-RK modifier species: peptide-methionine (S)-S-oxide reductase(Enzyme) mutant MsrA H186N


proof_lines: SABIO-RK modifier species: peptide-methionine (S)-S-oxide reductase(Enzyme) mutant MsrA Y189A


proof_lines: SABIO-RK modifier species: peptide-methionine (S)-S-oxide reductase(Enzyme) mutant MsrA W53A


proof_lines: SABIO-RK modifier species: peptide-methionine (S)-S-oxide reductase(Enzyme) mutant MsrA D129A


organism: Solanum lycopersicum

substrate_name: thioredoxin

source_db: brenda

source_license: CC BY 4.0

sequence_variant_note: Resolved canonical sequence from direct_uniprot_rest:G3JX11 plus C180S reconstruction and applied mutation signature C180S to reconstruct the assayed variant sequence.

proof_lines: mutant C180S of isoform MSRA2, in 50 mM Tris-HCl (pH 8.0), at 28°C

substrate: thioredoxin

source: brenda


sequence_variant_note: Resolved canonical sequence from UniProtKB:P54153 canonical sequence, variant reconstructed by C194S coordinate check and applied mutation signature C194S to reconstruct the assayed variant sequence.

proof_lines: mutant C194S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28°C


mutation_signature: Unknown

sequence_source: UniProtKB:P54153 canonical sequence

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

proof_lines: wild type isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P54153 canonical sequence, variant reconstructed by C188S coordinate check and applied mutation signature C188S to reconstruct the assayed variant sequence.

proof_lines: mutant C188S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P54153 canonical sequence, variant reconstructed by C180S coordinate check and applied mutation signature C180S to reconstruct the assayed variant sequence.

proof_lines: mutant C180S of isoform E4, in 50 mM Tris-HCl (pH 8.0), at 28°C


sequence_source: UniProtKB:G3JX11 canonical sequence

proof_lines: wild type isoform MSRA2, in 50 mM Tris-HCl (pH 8.0), at 28°C


organism: Treponema denticola

substrate_name: dabsyl-L-methionine (S)-S-oxide

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q73PT7 canonical sequence, variant reconstructed by Y163A/E165A coordinate check and applied mutation signature Y163A/E165A to reconstruct the assayed variant sequence.

data_origin: experimental

substrate: dabsyl-L-methionine (S)-S-oxide


sequence_source: UniProtKB:Q73PT7 canonical sequence


source_db: oed

verification_status: unverified

status: unverified

source: oed


organism: Leptospira interrogans

substrate_name: L-methionine-(S)-S-oxide

sequence_variant_note: Resolved canonical sequence from UniProt Q72UW2 canonical sequence with reviewed C25S substitution applied from the selected BRENDA paper note and applied mutation signature C25S to reconstruct the assayed variant sequence.

proof_lines: 30°C, pH 7.0, cosubstrate: thioredoxin, mutant enzyme C25S

substrate: L-methionine-(S)-S-oxide


sequence_source: UniProt Q72N60 canonical accession sequence

proof_lines: 30°C, pH 7.0, cosubstrate: L-methionine-(S)-S-oxide, wild-type enzyme

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

proof_lines: 30°C, pH 7.0, cosubstrate: N-acetyl-L-methionine-(S)-S-oxide, wild-type enzyme


sequence_source: UniProt Q72UW2 canonical accession 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: SABIO-RK modifier species: peptide-methionine (S)-S-oxide reductase(Enzyme) mutant MsrA Y189F


proof_lines: SABIO-RK modifier species: peptide-methionine (S)-S-oxide reductase(Enzyme) mutant MsrA W53F


sequence_source: UniProt Q9JWM8 canonical accession sequence

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


proof_lines: SABIO-RK modifier species: peptide-methionine (S)-S-oxide reductase(Enzyme) mutant MsrA H186A


proof_lines: SABIO-RK modifier species: peptide-methionine (S)-S-oxide reductase(Enzyme) mutant MsrA Y197A


organism: Helicobacter pylori

substrate_name: dabsyl-L-methionine (S)-sulfoxide

sequence_variant_note: Resolved canonical sequence from UniProtKB O25011 direct FASTA lookup; E193A/D197A reconstructed from the fetched canonical sequence and applied mutation signature E193A/D197A to reconstruct the assayed variant sequence.

substrate: dabsyl-L-methionine (S)-sulfoxide


sequence_variant_note: Resolved canonical sequence from UniProtKB O25011 direct FASTA lookup; D197A reconstructed from the fetched canonical sequence and applied mutation signature D197A to reconstruct the assayed variant sequence.


verification_status: verified

sequence_source: UniProtKB O25011 direct FASTA lookup

column_label: Table 2 (Kinetic analyses of H. pyroli MsrAB, HpMsrA, HpMsrB domain, and its mutants), Form row 'WT', Substrate row 'Met-S-O'; column 'K_m (mM)' = 0.17 ± 0.06; column 'k_cat (min^-1)' = 10.2 ± 1.3; column 'k_cat/K_m (mM^-1 min^-1)' = 60 ± 7.

normalized_value_unit_evidence: kcat: printed Table 2 cell 10.2 min^-1; 10.2 / 60 = 0.17 s^-1. Km: printed Table 2 cell 0.17 mM; the column is already in mM, so no conversion is applied and the value stays 0.17 mM. kcat/Km: printed Table 2 cell 60 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 60 / 60 = 1.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Form row 'WT', Substrate row 'Met-S-O': K_m = 0.17 ± 0.06 mM; k_cat = 10.2 ± 1.3 min^-1; printed k_cat/K_m = 60 ± 7 mM^-1 min^-1.

table_label: Table 2: Kinetic analyses of H. pyroli MsrAB, HpMsrA, HpMsrB domain, and its mutants (Antioxidants 2021, 10(3):389)

status: verified


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O25011 and applied mutation signature E193A/D197A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic analyses of H. pyroli MsrAB, HpMsrA, HpMsrB domain, and its mutants), Form row 'E193A/D197A', Substrate row 'Met-S-O'; column 'K_m (mM)' = 0.12 ± 0.05; column 'k_cat (min^-1)' = 5.7 ± 0.6; column 'k_cat/K_m (mM^-1 min^-1)' = 47 ± 5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 5.7 min^-1; 5.7 / 60 = 0.095 s^-1. Km: printed Table 2 cell 0.12 mM; the column is already in mM, so no conversion is applied and the value stays 0.12 mM. kcat/Km: printed Table 2 cell 47 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 47 / 60 = 0.7833333333333333 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Form row 'E193A/D197A', Substrate row 'Met-S-O': K_m = 0.12 ± 0.05 mM; k_cat = 5.7 ± 0.6 min^-1; printed k_cat/K_m = 47 ± 5 mM^-1 min^-1.

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProtKB Q72UW2 direct FASTA lookup; C25S reconstructed because Q72UW2 has C at residue 25 and applied mutation signature C25S 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.


substrate_name: N-acetyl-L-methionine-(S)-S-oxide

substrate: N-acetyl-L-methionine-(S)-S-oxide


sequence_source: UniProtKB Q72UW2 direct FASTA lookup; C25S reconstructed because Q72UW2 has C at residue 25


sequence_variant_note: Resolved canonical sequence from UniProtKB Q73PT7 REST/FASTA direct check; Y163A reconstructed by direct residue substitution. and applied mutation signature Y163A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q73PT7 REST/FASTA direct check; C285S reconstructed by direct residue substitution. and applied mutation signature C285S to reconstruct the assayed variant sequence.


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

sequence_source: UniProtKB Q73PT7 REST/FASTA direct check; row-specific isolated-domain construct boundary unresolved.

proof_lines:
isolated MrsA domain, pH 7.5, 37°C
isolated MrsA domain, pH 0.75, 37°C
Raw SKiD Env: Temp=37°C, pH=7.5

source_databases_merged: brenda skid


sequence_source: UniProtKB Q73PT7 REST/FASTA direct check; C285S reconstructed by direct residue substitution.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q73PT7 REST/FASTA direct check; D164A reconstructed by direct residue substitution. and applied mutation signature D164A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q73PT7 REST/FASTA direct check; Y163A reconstructed by direct residue substitution.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q73PT7 REST/FASTA direct check; E165A reconstructed by direct residue substitution. and applied mutation signature E165A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q73PT7 REST/FASTA direct check; Y163A/E165A reconstructed by direct residue substitution. and applied mutation signature Y163A/E165A to reconstruct the assayed variant sequence.


organism: Alkaliphilus oremlandii

substrate_name: dithiothreitol; glutaredoxin 2

sequence_source: UniProtKB:A8MI53; retrieved via https://rest.uniprot.org/uniprotkb/A8MI53.json

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

substrate: dithiothreitol; glutaredoxin 2


substrate_name: glutaredoxin 2

substrate: glutaredoxin 2


substrate_name: dithiothreitol

substrate: dithiothreitol


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Arabidopsis thaliana

sequence_source: UniProtKB:P54150; retrieved via https://rest.uniprot.org/uniprotkb/P54150.json

proof_lines: recombinant isozyme PMSRA4, with DTT, pH 8.0, 22°C

proof_lines: recombinant isozyme PMSRA3, with DTT, pH 7.5, 22°C


organism: Caenorhabditis elegans

substrate_name: dabsyl L-methionine-(S)-sulfoxide

sequence_source: UniProtKB:O02089; retrieved via https://rest.uniprot.org/uniprotkb/O02089.json

substrate: dabsyl L-methionine-(S)-sulfoxide


organism: Drosophila melanogaster

kcat_display: Not reported

sequence_source: UniProtKB:P08761; retrieved via https://rest.uniprot.org/uniprotkb/P08761.json


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A744; retrieved via https://rest.uniprot.org/uniprotkb/P0A744.json and applied mutation signature C86S/C206S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


enzyme_display_name: Peptide methionine sulfoxide reductase MsrA/MsrB

enzyme_name_source: UniProtKB O25011

assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM sodium phosphate, 50 mM NaCl, 20 mM DTT

proof_lines: PMID 33807684 Table 2 WT / Met-S-O exact kinetic row


sequence_variant_note: Resolved canonical sequence from UniProtKB:O25011 and applied mutation signature Y343F to reconstruct the assayed variant sequence.

proof_lines: PMID 33807684 Table 2 Y343F / Met-S-O exact kinetic row

enzyme: Peptide methionine sulfoxide reductase MsrA/MsrB


sequence_variant_note: Resolved canonical sequence from UniProtKB:O25011 and applied mutation signature E193A to reconstruct the assayed variant sequence.

proof_lines: PMID 33807684 Table 2 E193A / Met-S-O exact kinetic row


sequence_variant_note: Resolved canonical sequence from UniProtKB:O25011 and applied mutation signature E339A to reconstruct the assayed variant sequence.

proof_lines: PMID 33807684 Table 2 E339A / Met-S-O exact kinetic row


sequence_variant_note: Resolved canonical sequence from UniProtKB:O25011 and applied mutation signature D197A to reconstruct the assayed variant sequence.

proof_lines: PMID 33807684 Table 2 D197A / Met-S-O exact kinetic row


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E165A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D164A to reconstruct the assayed variant sequence.


organism: Trypanosoma cruzi

proof_lines: pH 7.5, 30°C, cosubstrate: L-methionine-(S)-S-oxide

proof_lines: pH 7.5, 30°C, cosubstrate: tryparedoxin I

proof_lines: pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(S)-S-oxide


enzyme_display_name: sugar-phosphatase

substrate_name: D-ribose 5-phosphate

proof_lines: wild type enzyme, in 20 mM Tris-HCl(pH 7.0), 5 mM MgCl2, at 32°C

enzyme: sugar-phosphatase

substrate: D-ribose 5-phosphate


substrate_name: D-fructose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A69M to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A69M, in 20 mM Tris-HCl(pH 7.0), 5 mM MgCl2, at 32°C

substrate: D-fructose 6-phosphate


substrate_name: 2-deoxy-D-glucose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K71R to reconstruct the assayed variant sequence.

substrate: 2-deoxy-D-glucose 6-phosphate


substrate_name: L-methionine sulfoxide

source_db: uniprot

substrate: L-methionine sulfoxide

source: uniprot


organism: Bacillus subtilis (strain 168)

substrate_name: D-xylulose 5-phosphate (at pH 7 and 37 degrees Celsius)

assay_conditions_summary: pH 7


organism: Escherichia coli (strain K12)

substrate_name: Ery4P (in the presence of magnesium ion as cofactor and at pH 9)

assay_conditions_summary: pH 9


organism: Mus musculus

substrate_name: Calmodulin

proof_lines: myristoylated enzyme, in 20 mM Tris-HCl, pH 7.5, 1 mM CaCl2, at 37°C

substrate: Calmodulin


substrate_name: L-methionine (S,R)-sulfoxide

proof_lines: pH 8.0, 25°C, MsrA, steady-state conditions

proof_lines: pH 5.5, 25°C, MsrA, steady-state conditions

substrate: L-methionine (S,R)-sulfoxide


organism: Nicotiana tabacum

substrate_name: thioredoxin

proof_lines: in 20 mM Tris-HCl, pH 8.0, 30 mM KCl, 10 mM MgCl2, at 37°C


organism: Saccharomyces cerevisiae

substrate_name: L-methionine (S)-sulfoxide

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

substrate: L-methionine (S)-sulfoxide


organism: Thermococcus kodakarensis

proof_lines: MsrA domain of MsrABTk, in the presence of 80 mM L-methionine (S)-sulfoxide

proof_lines: MsrA domain of MsrABTk, in the presence of 100 mM dithiothreiol


proof_lines: recombinant enzyme. isoform MSR10, at 30°C and pH 7.5

proof_lines: recombinant enzyme. isoform MSRA, at 30°C and pH 7.5

proof_lines: recombinant enzyme. isoform MSR180, at 30°C and pH 7.5


substrate_name: D-Ribose 5-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9ZVJ5 and applied mutation signature I68M to reconstruct the assayed variant sequence.

column_label: Table 1 stacks three panels over one substrate column and four enzyme columns 'AtSgpp', 'AtSgpp1', 'AtSgpp2' and 'AtSgpp3'. Panel head 'kcat (s−1)', enzyme column 'AtSgpp1', substrate row 'd-ribose-5-phosphate' = (3.9 ± 0.2) × 10. Panel head 'Km (M)', same enzyme column and substrate row = (3.8 ± 0.4) × 10−3. Panel head 'kcat/Km (M−1 s−1)', same enzyme column and substrate row = 10.2 × 103.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.9 x 10^1 s^-1; 3.9 x 10^1 = 39 and s^-1 is already the canonical kcat unit, so no unit conversion applies; the exported value is 39 s^(-1). Km: printed Table 1 cell 3.8 x 10^-3 M; 1 M is 1000 mM, so 3.8 x 10^-3 x 1000 = 3.8 mM; the exported value is 3.8 mM. kcat/Km: printed Table 1 cell 10.2 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 10.2 x 10^3 / 1000 = 10.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 'd-ribose-5-phosphate', enzyme column 'AtSgpp1': kcat = 3.9 x 10^1 s^-1; Km = 3.8 x 10^-3 M; printed kcat/Km = 10.2 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'd-ribose-5-phosphate', enzyme column 'AtSgpp1' (mutant protein AtSgpp-I68M)

table_label: Table 1: Kinetic parameter kcat, Km and kcat/Km of the phosphatase activity of purified AtSgpp and mutant proteins, on various organic phosphomonoesters (Planta 2014, 240:479-487)

substrate: D-Ribose 5-phosphate


sequence_source: UniProtKB Q9ZVJ5 canonical sequence

column_label: Table 1 stacks three panels over one substrate column and four enzyme columns 'AtSgpp', 'AtSgpp1', 'AtSgpp2' and 'AtSgpp3'. Panel head 'kcat (s−1)', enzyme column 'AtSgpp', substrate row 'd-ribose-5-phosphate' = (3.9 ± 0.3) × 10. Panel head 'Km (M)', same enzyme column and substrate row = (3.6 ± 0.1) × 10−3. Panel head 'kcat/Km (M−1 s−1)', same enzyme column and substrate row = 10.7 × 103.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.9 x 10^1 s^-1; 3.9 x 10^1 = 39 and s^-1 is already the canonical kcat unit, so no unit conversion applies; the exported value is 39 s^(-1). Km: printed Table 1 cell 3.6 x 10^-3 M; 1 M is 1000 mM, so 3.6 x 10^-3 x 1000 = 3.6 mM; the exported value is 3.6 mM. kcat/Km: printed Table 1 cell 10.7 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 10.7 x 10^3 / 1000 = 10.7 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 'd-ribose-5-phosphate', enzyme column 'AtSgpp': kcat = 3.9 x 10^1 s^-1; Km = 3.6 x 10^-3 M; printed kcat/Km = 10.7 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'd-ribose-5-phosphate', enzyme column 'AtSgpp' (wild-type phosphosugar phosphatase AtSgpp)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9ZVJ5 and applied mutation signature A69M to reconstruct the assayed variant sequence.

column_label: Table 1 stacks three panels over one substrate column and four enzyme columns 'AtSgpp', 'AtSgpp1', 'AtSgpp2' and 'AtSgpp3'. Panel head 'kcat (s−1)', enzyme column 'AtSgpp2', substrate row 'd-ribose-5-phosphate' = (3.3 ± 0.3) × 10. Panel head 'Km (M)', same enzyme column and substrate row = (5.9 ± 0.2) × 10−3. Panel head 'kcat/Km (M−1 s−1)', same enzyme column and substrate row = 5.6 × 103.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.3 x 10^1 s^-1; 3.3 x 10^1 = 33 and s^-1 is already the canonical kcat unit, so no unit conversion applies; the exported value is 33 s^(-1). Km: printed Table 1 cell 5.9 x 10^-3 M; 1 M is 1000 mM, so 5.9 x 10^-3 x 1000 = 5.9 mM; the exported value is 5.9 mM. kcat/Km: printed Table 1 cell 5.6 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.6 x 10^3 / 1000 = 5.6 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 'd-ribose-5-phosphate', enzyme column 'AtSgpp2': kcat = 3.3 x 10^1 s^-1; Km = 5.9 x 10^-3 M; printed kcat/Km = 5.6 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'd-ribose-5-phosphate', enzyme column 'AtSgpp2' (mutant protein AtSgpp-A69M)


substrate_name: D-Fructose 6-phosphate

column_label: Table 1 stacks three panels over one substrate column and four enzyme columns 'AtSgpp', 'AtSgpp1', 'AtSgpp2' and 'AtSgpp3'. Panel head 'kcat (s−1)', enzyme column 'AtSgpp1', substrate row 'd-fructose-6-phosphate' = (1.9 ± 0.3) × 10. Panel head 'Km (M)', same enzyme column and substrate row = (8.0 ± 0.2) × 10−3. Panel head 'kcat/Km (M−1 s−1)', same enzyme column and substrate row = 2.4 × 103.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.9 x 10^1 s^-1; 1.9 x 10^1 = 19 and s^-1 is already the canonical kcat unit, so no unit conversion applies; the exported value is 19 s^(-1). Km: printed Table 1 cell 8.0 x 10^-3 M; 1 M is 1000 mM, so 8.0 x 10^-3 x 1000 = 8 mM; the exported value is 8 mM. kcat/Km: printed Table 1 cell 2.4 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.4 x 10^3 / 1000 = 2.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 'd-fructose-6-phosphate', enzyme column 'AtSgpp1': kcat = 1.9 x 10^1 s^-1; Km = 8.0 x 10^-3 M; printed kcat/Km = 2.4 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'd-fructose-6-phosphate', enzyme column 'AtSgpp1' (mutant protein AtSgpp-I68M)

substrate: D-Fructose 6-phosphate


substrate_name: DL-glycerol 3-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9ZVJ5 and applied mutation signature K71R to reconstruct the assayed variant sequence.

smiles: O=P(O)(O)OCC(O)CO

column_label: Table 1 stacks three panels over one substrate column and four enzyme columns 'AtSgpp', 'AtSgpp1', 'AtSgpp2' and 'AtSgpp3'. Panel head 'kcat (s−1)', enzyme column 'AtSgpp3', substrate row 'dl-glycerol-3-phosphate' = (2.2 ± 0.2) × 10. Panel head 'Km (M)', same enzyme column and substrate row = (8.0 ± 0.6) × 10−3. Panel head 'kcat/Km (M−1 s−1)', same enzyme column and substrate row = 2.8 × 103.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.2 x 10^1 s^-1; 2.2 x 10^1 = 22 and s^-1 is already the canonical kcat unit, so no unit conversion applies; the exported value is 22 s^(-1). Km: printed Table 1 cell 8.0 x 10^-3 M; 1 M is 1000 mM, so 8.0 x 10^-3 x 1000 = 8 mM; the exported value is 8 mM. kcat/Km: printed Table 1 cell 2.8 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.8 x 10^3 / 1000 = 2.8 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 'dl-glycerol-3-phosphate', enzyme column 'AtSgpp3': kcat = 2.2 x 10^1 s^-1; Km = 8.0 x 10^-3 M; printed kcat/Km = 2.8 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'dl-glycerol-3-phosphate', enzyme column 'AtSgpp3' (mutant protein AtSgpp-K71R)

substrate: DL-glycerol 3-phosphate


column_label: Table 1 stacks three panels over one substrate column and four enzyme columns 'AtSgpp', 'AtSgpp1', 'AtSgpp2' and 'AtSgpp3'. Panel head 'kcat (s−1)', enzyme column 'AtSgpp', substrate row 'dl-glycerol-3-phosphate' = (2.3 ± 0.3) × 10. Panel head 'Km (M)', same enzyme column and substrate row = (7.3 ± 0.2) × 10−3. Panel head 'kcat/Km (M−1 s−1)', same enzyme column and substrate row = 3.1 × 103.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.3 x 10^1 s^-1; 2.3 x 10^1 = 23 and s^-1 is already the canonical kcat unit, so no unit conversion applies; the exported value is 23 s^(-1). Km: printed Table 1 cell 7.3 x 10^-3 M; 1 M is 1000 mM, so 7.3 x 10^-3 x 1000 = 7.3 mM; the exported value is 7.3 mM. kcat/Km: printed Table 1 cell 3.1 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.1 x 10^3 / 1000 = 3.1 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 'dl-glycerol-3-phosphate', enzyme column 'AtSgpp': kcat = 2.3 x 10^1 s^-1; Km = 7.3 x 10^-3 M; printed kcat/Km = 3.1 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'dl-glycerol-3-phosphate', enzyme column 'AtSgpp' (wild-type phosphosugar phosphatase AtSgpp)


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9ZVJ5 canonical sequence, manually reconstructed as I68M and applied mutation signature I68M to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I68M, in 20 mM Tris-HCl(pH 7.0), 5 mM MgCl2, at 32°C


column_label: Table 1 stacks three panels over one substrate column and four enzyme columns 'AtSgpp', 'AtSgpp1', 'AtSgpp2' and 'AtSgpp3'. Panel head 'kcat (s−1)', enzyme column 'AtSgpp3', substrate row 'd-fructose-6-phosphate' = (1.9 ± 0.1) × 10. Panel head 'Km (M)', same enzyme column and substrate row = (8.0 ± 0.1) × 10−3. Panel head 'kcat/Km (M−1 s−1)', same enzyme column and substrate row = 2.4 × 103.

raw_value_unit_evidence: Table 1, substrate row 'd-fructose-6-phosphate', enzyme column 'AtSgpp3': kcat = 1.9 x 10^1 s^-1; Km = 8.0 x 10^-3 M; printed kcat/Km = 2.4 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'd-fructose-6-phosphate', enzyme column 'AtSgpp3' (mutant protein AtSgpp-K71R)


substrate_name: imido-di-phosphate (in the presence of magnesium ion as cofactor and at pH 9)

sequence_source: source_record; UniProt REST cross-check

proof_lines: Glucose-6-phosphate is also a good substrate with a relative activity of 62.5% versus the activity with ribose-5-phosphate.


substrate_name: 2-deoxyglucose-6-P (with manganese ions as cofactor and at pH 9)

proof_lines: kcat is 33 sec(-1) with 2-deoxyglucose-6-P as substrate. kcat is 11 sec(-1) with mannose-6-P as substrate. kcat is 9.4 sec(-1) with 2-deoxyribose-5-P as substrate. kcat is 2.8 sec(-1) with ribose-5-P as substrate. kcat is 25 sec(-1) with gl


substrate_name: fructose-1-P (with magnesium ions as cofactor and at pH 9)

proof_lines: kcat is 3.7 sec(-1) with fructose-1-P as substrate. kcat is 2.7 sec(-1) with ribose-5-P as substrate. kcat is 13 sec(-1) with glucose-6-P as substrate. kcat is 3.1 sec(-1) with fructose-6-P as substrate. kcat is 7.5 sec(-1) with beta-D-gluc


substrate_name: PNP

proof_lines: kcat is 1.9 sec(-1) with PNP as substrate (PubMed:39133002). kcat is 2.4 sec(-1) with PLP as substrate (PubMed:39133002). kcat is 12 sec(-1) with PLP as substrate (PubMed:16990279). kcat is 14 sec(-1) with beta-glucose 6-phosphate as substr

substrate: PNP


organism: Clostridium sp.

substrate_name: dabsylated L-methionine (S)-sulfoxide

sequence_source: NCBI Protein ABW19485.1, peptide methionine sulfoxide reductase from Alkaliphilus oremlandii OhILAs; PMID 18767149 / DOI 10.1002/prot.22212.

proof_lines: wild type enzyme, using dithiothreitol as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37°C

substrate: dabsylated L-methionine (S)-sulfoxide


sequence_source: Reconstructed from NCBI Protein ABW19485.1 using PMID 18767149 U16C/Sec16-to-Cys evidence.

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

proof_lines: purified cysteine mutant form U16C, using dithiothreitol as cosubstrate, in 50 mM sodium phosphate, pH 7.5, at 37°C


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


proof_lines: pH 8.0, 25°C, substrate L-methionine (S)-sulfoxide


substrate_name: dabsyl-L-methionine-(S)-S-oxide

sequence_source: UniProtKB reviewed Q9D6Y7 (MSRA_MOUSE), isoform 1; PMID 15924425 / DOI 10.1021/bi0501131.

proof_lines: recombinant wild-type MsrA, with DTT, pH 7.5, 37°C

substrate: dabsyl-L-methionine-(S)-S-oxide


mutation_signature: recombinant truncated MsrA DELTA(1-46)

sequence_source: Reconstructed from UniProtKB reviewed Q9D6Y7 by deleting residues 1-46 according to the selected BRENDA mutation signature; PMID 15924425 / DOI 10.1021/bi0501131.

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

mutation_type: truncation

proof_lines: recombinant truncated MsrA DELTA(1-46), with DTT, pH 7.5, 37°C


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


substrate_name: N-Acetyl-L-methionine-(R)-sulfoxide

smiles: CC(=O)NC(CCS(C)=O)C(=O)O

substrate: N-Acetyl-L-methionine-(R)-sulfoxide


substrate_name: L-Methionine (R)-S-oxide

substrate: L-Methionine (R)-S-oxide


substrate_name: Dabsyl-L-methionine (R)-sulfoxide

substrate: Dabsyl-L-methionine (R)-sulfoxide


substrate_name: dabsyl-L-methionine (R)-sulfoxide

sequence_variant_note: Resolved canonical sequence from direct_uniprot_rest:O25011; reconstructed E193A/D197A variant from canonical sequence and applied mutation signature E193A/D197A to reconstruct the assayed variant sequence.

substrate: dabsyl-L-methionine (R)-sulfoxide


sequence_source: direct_uniprot_rest:O25011; reconstructed E193A/D197A variant from canonical sequence


substrate_name: dabsyl-L-methionine (R)-S-oxide

sequence_variant_note: Resolved canonical sequence from UniProt REST Q73PT7 canonical sequence with in-review substitution reconstruction and applied mutation signature Y163A/E165A to reconstruct the assayed variant sequence.

substrate: dabsyl-L-methionine (R)-S-oxide


sequence_variant_note: Resolved canonical sequence from UniProt REST Q73PT7 canonical sequence with in-review substitution reconstruction and applied mutation signature Y163A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST Q73PT7 canonical sequence with in-review substitution reconstruction and applied mutation signature C11S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST Q73PT7 canonical sequence with in-review substitution reconstruction and applied mutation signature D164A to reconstruct the assayed variant sequence.


sequence_source: UniProt REST Q73PT7 canonical sequence with in-review substitution reconstruction


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


sequence_source: UniProt REST Q73PT7 FASTA/JSON direct accession lookup


organism: Pseudomonas fluorescens

sequence_source: UniProtKB:C3K9U8 direct REST/FASTA lookup; entry C3K9U8_PSEFS, organism Pseudomonas fluorescens strain SBW25, locus PFLU_2693.


substrate_name: D-glucose 6-phosphate

substrate: D-glucose 6-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:O25011 direct REST lookup; E339A reconstructed from selected mutation signature and applied mutation signature E339A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O25011 and applied mutation signature E193A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic analyses of H. pyroli MsrAB, HpMsrA, HpMsrB domain, and its mutants), Form row 'E193A', Substrate row 'Met-R-O'; column 'K_m (mM)' = 0.06 ± 0.02; column 'k_cat (min^-1)' = 4.7 ± 0.3; column 'k_cat/K_m (mM^-1 min^-1)' = 78 ± 5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4.7 min^-1; 4.7 / 60 = 0.07833333333333334 s^-1. Km: printed Table 2 cell 0.06 mM; the column is already in mM, so no conversion is applied and the value stays 0.06 mM. kcat/Km: printed Table 2 cell 78 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 78 / 60 = 1.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Form row 'E193A', Substrate row 'Met-R-O': K_m = 0.06 ± 0.02 mM; k_cat = 4.7 ± 0.3 min^-1; printed k_cat/K_m = 78 ± 5 mM^-1 min^-1.


substrate_name: L-methionine-(R)-S-oxide

sequence_source: UniProtKB:Q72NN2 direct REST lookup

substrate: L-methionine-(R)-S-oxide


substrate_name: N-acetyl-L-methionine-(R)-S-oxide

proof_lines: 30°C, pH 7.0, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide

substrate: N-acetyl-L-methionine-(R)-S-oxide


substrate_name: thioredoxin

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q78J03 direct REST lookup; C98S reconstructed from selected mutation signature and applied mutation signature C98S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C98S, in 50 mM sodium phosphate, pH 7.5, 50 mM NaCl, at 37°C

substrate: thioredoxin


substrate_name: dithiothreitol

sequence_source: UniProtKB:Q78J03 direct REST lookup

proof_lines: wild type enzyme, in 50 mM sodium phosphate, pH 7.5, 50 mM NaCl, at 37°C

substrate: dithiothreitol


organism: Treponema denticola

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q73PT7 direct REST lookup; C11S reconstructed from selected mutation signature and applied mutation signature C11S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q73PT7 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature E165A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q73PT7 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature D164A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q73PT7 FASTA direct lookup plus row-specific mutation reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q73PT7 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature Y163A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:V5BL87 FASTA direct lookup


sequence_source: UniProtKB:V5BL87 FASTA canonical context only; row-specific variant sequence unresolved


proof_lines: pH 7.5, 30°C, cosubstrate: tryparedoxin I

proof_lines: pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide


substrate_name: trypanothione disulfide

substrate: trypanothione disulfide


proof_lines: recombinant isozyme MsrB1, with dithioerythritol

proof_lines: recombinant isozyme MsrB2, with dithioerythritol


organism: Homo sapiens

proof_lines: recombinant wild-type isozyme MsrB3 expressed in Escherichia coli


proof_lines: recombinant wild-type isozyme MsrB2 expressed in Escherichia coli

proof_lines: recombinant wild-type selenocysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells

proof_lines: recombinant wild-type cysteine-containing isozyme MsrB1 expressed in NIH 3T3 cells


enzyme_display_name: linoleate 13S-lipoxygenase

organism: Olea europaea

substrate_name: alpha-linolenate

proof_lines:
pH 6.5, 20°C, isoenzyme Oep2LOX2
isoform Oep1LOX2
pH 6.5, 20°C, isoenzyme Oep1LOX2

enzyme: linoleate 13S-lipoxygenase

substrate: alpha-linolenate


organism: Glycine max

substrate_name: cis-Resveratrol

substrate: cis-Resveratrol


substrate_name: trans-Resveratrol

substrate: trans-Resveratrol


substrate_name: linoleate

smiles: CCCCC/C=C\C/C=C\CCCCCCCC(=O)O

substrate: linoleate


substrate_name: Linoleate; O2

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I553F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: linoleate 13S-lipoxygenase(Enzyme) mutant Ile553Phe

substrate: Linoleate; O2


smiles: O=O


substrate_name: arachidonate

smiles: CCCCC/C=C\C/C=C\C/C=C\C/C=C\CCCC(=O)O

substrate: arachidonate


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

proof_lines: pH 7.5, temperature not specified in the publication


organism: Myxococcus xanthus

substrate_name: linoleic acid

sequence_source: UniProtKB:Q1DBH9 direct REST lookup on 2026-06-07

substrate: linoleic acid


substrate_name: arachidonic acid

substrate: arachidonic acid


organism: Phaseolus vulgaris

substrate_name: O2; Linoleate

sequence_source: UniProtKB:P27480 direct REST lookup on 2026-06-07

substrate: O2; Linoleate


organism: Helicobacter pylori

substrate_name: dabsyl-L-methionine (R)-sulfoxide

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O25011 and applied mutation signature Y343F to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic analyses of H. pyroli MsrAB, HpMsrA, HpMsrB domain, and its mutants), Form row 'Y343F', Substrate row 'Met-R-O'; column 'K_m (mM)' = 0.03 ± 0.02; column 'k_cat (min^-1)' = 5.2 ± 0.7; column 'k_cat/K_m (mM^-1 min^-1)' = 173 ± 23.

normalized_value_unit_evidence: kcat: printed Table 2 cell 5.2 min^-1; 5.2 / 60 = 0.08666666666666667 s^-1. Km: printed Table 2 cell 0.03 mM; the column is already in mM, so no conversion is applied and the value stays 0.03 mM. kcat/Km: printed Table 2 cell 173 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 173 / 60 = 2.8833333333333333 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Form row 'Y343F', Substrate row 'Met-R-O': K_m = 0.03 ± 0.02 mM; k_cat = 5.2 ± 0.7 min^-1; printed k_cat/K_m = 173 ± 23 mM^-1 min^-1.

substrate: dabsyl-L-methionine (R)-sulfoxide


sequence_variant_note: Resolved canonical sequence from UniProtKB:O25011 direct REST lookup on 2026-06-07 and applied mutation signature E339A to reconstruct the assayed variant sequence.


substrate_name: tryparedoxin I

sequence_source: UniProtKB:V5BL87 direct FASTA checked 2026-06-07

proof_lines: pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide, mutant enzyme C74S

proof_lines: pH 7.5, 30°C, cosubstrate: tryparedoxin I, mutant enzyme C74S

substrate: tryparedoxin I


proof_lines: pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide, mutant enzyme C72S

proof_lines: pH 7.5, 30°C, cosubstrate: tryparedoxin I, mutant enzyme C72S


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


organism: Arabidopsis thaliana

substrate_name: D-glucose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9ZVJ5 and applied mutation signature I68M to reconstruct the assayed variant sequence.

column_label: Table 1 stacks three panels over one substrate column and four enzyme columns 'AtSgpp', 'AtSgpp1', 'AtSgpp2' and 'AtSgpp3'. Panel head 'kcat (s−1)', enzyme column 'AtSgpp1', substrate row 'd-glucose-6-phosphate' = (2.6 ± 0.4) × 10. Panel head 'Km (M)', same enzyme column and substrate row = (6.7 ± 0.3) × 10−3. Panel head 'kcat/Km (M−1 s−1)', same enzyme column and substrate row = 3.8 × 103.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.6 x 10^1 s^-1; 2.6 x 10^1 = 26 and s^-1 is already the canonical kcat unit, so no unit conversion applies; the exported value is 26 s^(-1). Km: printed Table 1 cell 6.7 x 10^-3 M; 1 M is 1000 mM, so 6.7 x 10^-3 x 1000 = 6.7 mM; the exported value is 6.7 mM. kcat/Km: printed Table 1 cell 3.8 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.8 x 10^3 / 1000 = 3.8 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 'd-glucose-6-phosphate', enzyme column 'AtSgpp1': kcat = 2.6 x 10^1 s^-1; Km = 6.7 x 10^-3 M; printed kcat/Km = 3.8 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'd-glucose-6-phosphate', enzyme column 'AtSgpp1' (mutant protein AtSgpp-I68M)

substrate: D-glucose 6-phosphate


substrate_name: alpha-linolenic acid

sequence_source: UniProtKB Q9FNX8 direct REST lookup

substrate: alpha-linolenic acid


sequence_source: UniProtKB Q9LNR3 direct REST lookup


sequence_source: UniProtKB P38418 direct REST lookup


sequence_source: UniProtKB Q9CAG3 direct REST lookup


organism: Cucumis melo var. makuwa

substrate_name: linolenic acid

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

smiles: CC/C=C\C/C=C\C/C=C\CCCCCCCC(=O)O

substrate: linolenic acid


sequence_source: UniProtKB A0A125S6K7 direct REST lookup

proof_lines: pH 5.0, 45°C, recombinant Hi-tagged enzyme


sequence_source: UniProtKB A0A125S6K8 direct REST lookup


row_label: Table 2, Form row 'Y343F', Substrate row 'Met-R-O'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O25011 and applied mutation signature D197A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic analyses of H. pyroli MsrAB, HpMsrA, HpMsrB domain, and its mutants), Form row 'D197A', Substrate row 'Met-R-O'; column 'K_m (mM)' = 0.06 ± 0.02; column 'k_cat (min^-1)' = 4.4 ± 0.3; column 'k_cat/K_m (mM^-1 min^-1)' = 73 ± 5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4.4 min^-1; 4.4 / 60 = 0.07333333333333333 s^-1. Km: printed Table 2 cell 0.06 mM; the column is already in mM, so no conversion is applied and the value stays 0.06 mM. kcat/Km: printed Table 2 cell 73 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 73 / 60 = 1.2166666666666666 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Form row 'D197A', Substrate row 'Met-R-O': K_m = 0.06 ± 0.02 mM; k_cat = 4.4 ± 0.3 min^-1; printed k_cat/K_m = 73 ± 5 mM^-1 min^-1.


row_label: Table 2, Form row 'E193A', Substrate row 'Met-R-O'


row_label: Table 2, Form row 'D197A', Substrate row 'Met-R-O'


sequence_source: UniProtKB O25011 FASTA direct check.


column_label: Table 2 (Kinetic analyses of H. pyroli MsrAB, HpMsrA, HpMsrB domain, and its mutants), Form row 'WT', Substrate row 'Met-R-O'; column 'K_m (mM)' = 0.05 ± 0.02; column 'k_cat (min^-1)' = 9.4 ± 0.4; column 'k_cat/K_m (mM^-1 min^-1)' = 188 ± 8.

normalized_value_unit_evidence: kcat: printed Table 2 cell 9.4 min^-1; 9.4 / 60 = 0.15666666666666668 s^-1. Km: printed Table 2 cell 0.05 mM; the column is already in mM, so no conversion is applied and the value stays 0.05 mM. kcat/Km: printed Table 2 cell 188 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 188 / 60 = 3.1333333333333333 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Form row 'WT', Substrate row 'Met-R-O': K_m = 0.05 ± 0.02 mM; k_cat = 9.4 ± 0.4 min^-1; printed k_cat/K_m = 188 ± 8 mM^-1 min^-1.


organism: Trypanosoma cruzi

substrate_name: thioredoxin

km_display: Not reported

sequence_source: UniProtKB V5BL87 FASTA direct check.

proof_lines: pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide, wild-type enzyme

proof_lines: pH 7.5, 30°C, cosubstrate: tryparedoxin I, wild-type enzyme

substrate: thioredoxin


substrate_name: N-acetyl-L-methionine-(R)-S-oxide

sequence_source: UniProtKB V5BL87 FASTA direct check; variant sequence not reconstructed because C72S/C74S does not match canonical residues 72 and 74.

proof_lines: pH 7.5, 30°C, cosubstrate: trypanothione, mutant enzyme C72S/C74S

proof_lines: pH 7.5, 30°C, cosubstrate: N-acetyl-L-methionine-(R)-S-oxide, mutant enzyme C72S/C74S

substrate: N-acetyl-L-methionine-(R)-S-oxide


proof_lines: kcat is 14.4 sec(-1) with (9Z,12Z)-octadecadienoate as substrate.


organism: Oryctolagus cuniculus

proof_lines: kcat is 22.2 sec(-1) with (5Z,8Z,11Z,14Z)-eicosatetraenoate as substrate (PubMed:15123652). kcat is 1.34 sec(-1) with (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate as substrate (PubMed:15123652).


organism: Pleurotus sapidus

proof_lines: kcat is 157 sec(-1) for linoleic acid (at pH 7.0 and 22 degrees Celsius).


organism: Pseudomonas aeruginosa

substrate_name: linoleate (Ref.4)

proof_lines: kcat is 96 sec(-1) with linoleate as substrate (Ref.4).

substrate: linoleate (Ref.4)


substrate_name: dabsyl methionine sulfoxide

proof_lines: kcat is 0.075 sec(-1) with dabsyl-MetSO as substrate.

substrate: dabsyl methionine sulfoxide


proof_lines: kcat is 0.028 sec(-1) with dabsyl-MetSO as substrate.


organism: Arabidopsis sp.

substrate_name: glutaredoxin S12

proof_lines: pH 8.0, 37°C, cosubstrate: dabsyl-L-methionine (R)-sulfoxide, MSRB1 activity

substrate: glutaredoxin S12


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

proof_lines: isoform MSRB1 mutant T132C, in the presence of 20 mM dithioerythritol


proof_lines: isoform MSRB1 mutant C116S, in the presence of 20 mM dithioerythritol


substrate_name: thioredoxin h1

proof_lines: isoform MSRB1 wild type enzyme, in the presence of 20 mMTris(2-carboxyethyl) phosphine hydrochloride

proof_lines: isoform MSRB2 wild type enzyme, in the presence of 20 mMTris(2-carboxyethyl) phosphine hydrochloride

substrate: thioredoxin h1


substrate_name: glutaredoxin C4

proof_lines: isoform MSRB1 mutant T132A, in the presence of 20 mM dithioerythritol

substrate: glutaredoxin C4


proof_lines: isoform MSRB2 mutant C134T, in the presence of 20 mM dithioerythritol


organism: Burkholderia thailandensis

substrate_name: alpha-linolenate

substrate: alpha-linolenate


organism: Fusarium oxysporum


proof_lines: in 0.1 M borate (pH 9.0), temperature not specified in the publication

proof_lines: in the presence of 6-pentadecanylsalicylic acid


organism: Lathyrus oleraceus subsp. oleraceus

substrate_name: linoleate

proof_lines: enzyme from cultivar Irina, at pH 7.0 and 37°C

proof_lines: enzyme from cultivar Hanka, at pH 7.0 and 37°C

substrate: linoleate


organism: Lens culinaris

proof_lines: enzyme from cultivar Pinklevi, at pH 7.0 and 37°C

proof_lines: enzyme from cultivar Rezi, at pH 7.0 and 37°C


substrate_name: linoleic acid

proof_lines: pH and temperature not specified in the publication

substrate: linoleic acid


organism: Escherichia coli

substrate_name: L-methionine (R)-sulfoxide

sequence_source: UniProtKB:P0A746 FASTA, found by UniProt lit_pubmed:11677230 direct follow-up

proof_lines: in vitro, substrate free L-methionine (R)-sulfoxide

substrate: L-methionine (R)-sulfoxide


substrate_name: N-acetyl-L-methionine (R)-sulfoxide

proof_lines: isoform MSRB4, pH and temperature not specified in the publication

proof_lines: isoform MSRB2, pH and temperature not specified in the publication

substrate: N-acetyl-L-methionine (R)-sulfoxide


organism: Neisseria meningitidis

proof_lines: MsrB, pH 8.0, 25°C, cofactor thioredoxin


organism: Nicotiana tabacum


organism: Solanum lycopersicum

substrate_name: dithiothreitol

proof_lines: recombinant enzyme, in 50 mM Tris-HCl, pH 8.0, at 37°C

substrate: dithiothreitol


organism: Thermococcus kodakarensis

proof_lines: MsrB domain of MsrABTk, in the presence of 20 mM dithiothreiol

proof_lines: MsrB domain of MsrABTk, in the presence of 80 mM L-methionine (S)-sulfoxide


organism: Trypanosoma brucei

substrate_name: tryparedoxin

substrate: tryparedoxin


enzyme_display_name: bacterial sulfide:quinone reductase

organism: Acidianus ambivalens

sequence_source: UniProtKB reviewed Q7ZAG8 from lit_pubmed:19438211; PDB cross-references 3H8I and 3H8L.

enzyme: bacterial sulfide:quinone reductase


organism: Acidithiobacillus ferrooxidans

proof_lines: apparent value, at pH 7.0, temperature not specified in the publication


organism: Aquifex aeolicus

substrate_name: Sulfide

sequence_source: UniProtKB reviewed O67931 from lit_pubmed:10816041; PDB cross-references 3HYV, 3HYW, and 3HYX.

proof_lines: pH 7.4, temperature not specified in the publication

substrate: Sulfide


organism: Arenicola marina

substrate_name: cyanide

substrate: cyanide


organism: Caldivirga maquilingensis

proof_lines: pH 7.5, 60°C, membrane-bound mutant enzyme M380N


enzyme_display_name: guanine deaminase

substrate_name: guanine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P76641 FASTA; A386S reconstructed from canonical sequence and applied mutation signature A386S to reconstruct the assayed variant sequence.

enzyme: guanine deaminase

substrate: guanine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P76641 FASTA; W101H reconstructed from canonical sequence and applied mutation signature W101H to reconstruct the assayed variant sequence.


substrate_name: ammeline

sequence_source: UniProtKB:P76641 FASTA

substrate: ammeline


organism: Homo sapiens

substrate_name: Guanine

sequence_source: UniProtKB:Q9Y2T3 FASTA

substrate: Guanine


substrate_name: Guanine; 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: recombinant enzyme, expressed in DH5-alpha cells

source_databases_merged: sabio_rk brenda skid

substrate: Guanine; H2O


organism: Mus musculus

sequence_source: UniProtKB:Q9R111 FASTA


organism: Nitrosomonas europaea

sequence_source: UniProtKB:Q82Y41 checked and rejected for EC/enzyme-family contradiction


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

proof_lines: mutant F141A, pH not specified in the publication, temperature not specified in the publication


assay_conditions_summary: pH 6

proof_lines:
at pH 6
isoenzyme B
at pH 9.0


sequence_source: UniProtKB:Q82Y41 canonical sequence; RCSB 4HRQ/4LC5 link Q82Y41/NE0047 to Nitrosomonas guanine deaminase

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


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q82Y41 canonical sequence by applying N66A; direct evidence: RCSB 7C3U title confirms NE0047 (N66A) with PMID 34010666 and maps the polymer to UniProt Q82Y41. and applied mutation signature N66A to reconstruct the assayed variant sequence.

proof_lines: mutant N66A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q82Y41 canonical sequence by applying F48A; direct evidence: The selected BRENDA source note names mutant F48A; UniProt Q82Y41 has F at canonical residue 48, so the variant sequence was reconstructed from the selected mutation label. and applied mutation signature F48A to reconstruct the assayed variant sequence.

proof_lines: mutant F48A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q82Y41 canonical sequence by applying E143D; direct evidence: RCSB 7C3S title confirms NE0047 (E143D) with PMID 34010666 and maps the polymer to UniProt Q82Y41. and applied mutation signature E143D to reconstruct the assayed variant sequence.

proof_lines: mutant E143D, pH not specified in the publication, temperature not specified in the publication


organism: Saccharomyces cerevisiae

substrate_name: H2O; Guanine

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

sequence_source: UniProtKB:Q07729 canonical sequence; source records from SABIO-RK/SKiD include Q07729 for Saccharomyces cerevisiae across guanine/reaction-component substrate labels

substrate: H2O; Guanine


sequence_source: UniProtKB:Q07729 canonical sequence; OED source record links Q07729 to Saccharomyces cerevisiae ammeline with PMID 31283204


sequence_source: UniProtKB:Q07729 canonical sequence; OED source record links Q07729 to Saccharomyces cerevisiae guanine with PMID 31283204


sequence_source: UniProtKB:Q07729 canonical sequence; BRENDA source records link Q07729 to Saccharomyces cerevisiae wild type across ammeline/guanine notes


enzyme_display_name: L-allo-threonine aldolase

organism: Aeromonas jandaei

substrate_name: L-beta-Phenylserine

sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature D168S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mm

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-beta-phenylserine block, enzyme row D168S: k_cat, s^-1 = 0.83; K_m, mM = 4.1; k_cat/K_m, s^-1 M^-1 = 2 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.83 s^-1 in the l-beta-phenylserine block of enzyme row D168S; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 0.83 s^(-1). Km: printed Table 2 cell 4.1 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 4.1 mM. kcat/Km: printed Table 2 cell 2 x 10^2 under the column head k_cat/K_m, s^-1 M^-1, that is 200.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 200.0 / 1000 = 0.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-beta-phenylserine block, enzyme row D168S: k_cat = 0.83 s^-1; K_m = 4.1 mM; printed k_cat/K_m = 2 x 10^2 M^-1 s^-1.

table_label: Table 2: Kinetic parameters of the LTAaj's mutants for the retro-aldol cleavage of l-allo-threonine and l-beta-phenylserine. Conversion in the aldol reaction of glycine and benzaldehyde to synthesize l-beta-phenylserine (FEBS Open Bio 2018)

enzyme: L-allo-threonine aldolase

substrate: L-beta-Phenylserine


sequence_variant_note: Resolved canonical sequence from UniProtKB O07051 canonical sequence with R171F applied during curation exact-accession review and applied mutation signature R171F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O07051 canonical sequence with N64E applied during curation exact-accession review and applied mutation signature N64E to reconstruct the assayed variant sequence.


substrate_name: L-allo-Threonine

sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature C196T to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-allo-threonine block, enzyme row C196T: k_cat, s^-1 = 13.3; K_m, mM = 0.5; k_cat/K_m, s^-1 M^-1 = 2.6 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 13.3 s^-1 in the l-allo-threonine block of enzyme row C196T; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 13.3 s^(-1). Km: printed Table 2 cell 0.5 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 0.5 mM. kcat/Km: printed Table 2 cell 2.6 x 10^4 under the column head k_cat/K_m, s^-1 M^-1, that is 26000.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 26000.0 / 1000 = 26.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-allo-threonine block, enzyme row C196T: k_cat = 13.3 s^-1; K_m = 0.5 mM; printed k_cat/K_m = 2.6 x 10^4 M^-1 s^-1.

substrate: L-allo-Threonine


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature S198H to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-allo-threonine block, enzyme row S198H: k_cat, s^-1 = 5.1; K_m, mM = 5.7; k_cat/K_m, s^-1 M^-1 = 0.9 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 2 cell 5.1 s^-1 in the l-allo-threonine block of enzyme row S198H; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 5.1 s^(-1). Km: printed Table 2 cell 5.7 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 5.7 mM. kcat/Km: printed Table 2 cell 0.9 x 10^3 under the column head k_cat/K_m, s^-1 M^-1, that is 900.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 900.0 / 1000 = 0.9 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-allo-threonine block, enzyme row S198H: k_cat = 5.1 s^-1; K_m = 5.7 mM; printed k_cat/K_m = 0.9 x 10^3 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature N64I to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-allo-threonine block, enzyme row N64I: k_cat, s^-1 = 1; K_m, mM = 3.8; k_cat/K_m, s^-1 M^-1 = 3 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1 s^-1 in the l-allo-threonine block of enzyme row N64I; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 1.0 s^(-1). Km: printed Table 2 cell 3.8 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 3.8 mM. kcat/Km: printed Table 2 cell 3 x 10^2 under the column head k_cat/K_m, s^-1 M^-1, that is 300.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 300.0 / 1000 = 0.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-allo-threonine block, enzyme row N64I: k_cat = 1 s^-1; K_m = 3.8 mM; printed k_cat/K_m = 3 x 10^2 M^-1 s^-1.


substrate_name: L-allo-threonine

sequence_variant_note: Resolved canonical sequence from UniProtKB O07051 canonical sequence with G200S applied during curation exact-accession review and applied mutation signature G200S to reconstruct the assayed variant sequence.

substrate: L-allo-threonine


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature H85Y to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-allo-threonine block, enzyme row H85Y: k_cat, s^-1 = 0.01; K_m, mM = 14.8; k_cat/K_m, s^-1 M^-1 = 0.7.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.01 s^-1 in the l-allo-threonine block of enzyme row H85Y; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 0.01 s^(-1). Km: printed Table 2 cell 14.8 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 14.8 mM. kcat/Km: printed Table 2 cell 0.7 under the column head k_cat/K_m, s^-1 M^-1, that is 0.7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.7 / 1000 = 0.0007 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-allo-threonine block, enzyme row H85Y: k_cat = 0.01 s^-1; K_m = 14.8 mM; printed k_cat/K_m = 0.7 M^-1 s^-1.


sequence_source: UniProtKB O07051 direct REST/FASTA lookup plus selected mutation-signature reconstruction


substrate_name: L-Threonine

sequence_source: UniProtKB O07051 direct REST/FASTA lookup

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

substrate: L-Threonine


column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-beta-phenylserine block, enzyme row wt: k_cat, s^-1 = 60.5; K_m, mM = 3.7; k_cat/K_m, s^-1 M^-1 = 1.6 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 60.5 s^-1 in the l-beta-phenylserine block of enzyme row wt; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 60.5 s^(-1). Km: printed Table 2 cell 3.7 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 3.7 mM. kcat/Km: printed Table 2 cell 1.6 x 10^4 under the column head k_cat/K_m, s^-1 M^-1, that is 16000.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 16000.0 / 1000 = 16.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-beta-phenylserine block, enzyme row wt: k_cat = 60.5 s^-1; K_m = 3.7 mM; printed k_cat/K_m = 1.6 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature R313H to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-beta-phenylserine block, enzyme row R313H: k_cat, s^-1 = 0.32; K_m, mM = 5.2; k_cat/K_m, s^-1 M^-1 = 62.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.32 s^-1 in the l-beta-phenylserine block of enzyme row R313H; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 0.32 s^(-1). Km: printed Table 2 cell 5.2 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 5.2 mM. kcat/Km: printed Table 2 cell 62 under the column head k_cat/K_m, s^-1 M^-1, that is 62.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 62.0 / 1000 = 0.062 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-beta-phenylserine block, enzyme row R313H: k_cat = 0.32 s^-1; K_m = 5.2 mM; printed k_cat/K_m = 62 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature D168V to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-beta-phenylserine block, enzyme row D168V: k_cat, s^-1 = 0.6; K_m, mM = 1.3; k_cat/K_m, s^-1 M^-1 = 4 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.6 s^-1 in the l-beta-phenylserine block of enzyme row D168V; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 0.6 s^(-1). Km: printed Table 2 cell 1.3 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 1.3 mM. kcat/Km: printed Table 2 cell 4 x 10^2 under the column head k_cat/K_m, s^-1 M^-1, that is 400.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 400.0 / 1000 = 0.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-beta-phenylserine block, enzyme row D168V: k_cat = 0.6 s^-1; K_m = 1.3 mM; printed k_cat/K_m = 4 x 10^2 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature D168N to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-allo-threonine block, enzyme row D168N: k_cat, s^-1 = 0.05; K_m, mM = 2.6; k_cat/K_m, s^-1 M^-1 = 20.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.05 s^-1 in the l-allo-threonine block of enzyme row D168N; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 0.05 s^(-1). Km: printed Table 2 cell 2.6 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 2.6 mM. kcat/Km: printed Table 2 cell 20 under the column head k_cat/K_m, s^-1 M^-1, that is 20.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 20.0 / 1000 = 0.02 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-allo-threonine block, enzyme row D168N: k_cat = 0.05 s^-1; K_m = 2.6 mM; printed k_cat/K_m = 20 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB O07051 direct REST/FASTA lookup plus selected mutation-signature reconstruction and applied mutation signature R313H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature E138A to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-beta-phenylserine block, enzyme row E138A: k_cat, s^-1 = 1.9; K_m, mM = 1.2; k_cat/K_m, s^-1 M^-1 = 1.6 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.9 s^-1 in the l-beta-phenylserine block of enzyme row E138A; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 1.9 s^(-1). Km: printed Table 2 cell 1.2 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 1.2 mM. kcat/Km: printed Table 2 cell 1.6 x 10^3 under the column head k_cat/K_m, s^-1 M^-1, that is 1600.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1600.0 / 1000 = 1.6 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-beta-phenylserine block, enzyme row E138A: k_cat = 1.9 s^-1; K_m = 1.2 mM; printed k_cat/K_m = 1.6 x 10^3 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_O07051 and applied mutation signature H128Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_O07051 and applied mutation signature S292R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_O07051 and applied mutation signature H128Y/S292R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P76641 canonical sequence reconstructed with A386S; UniProtKB reviewed P76641/GUAD_ECOLI REST/FASTA: guanine deaminase, EC 3.5.4.3, Escherichia coli strain K12, canonical length 439 aa; RCSB 6OHB polymer entity maps to UniProt P76641; PMID 31283204 accession-code footnote names EcGuaD UniProt P76641. and applied mutation signature A386S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH


sequence_variant_note: Resolved canonical sequence from UniProtKB P76641 canonical sequence reconstructed with F210A; UniProtKB reviewed P76641/GUAD_ECOLI REST/FASTA: guanine deaminase, EC 3.5.4.3, Escherichia coli strain K12, canonical length 439 aa; RCSB 6OHB polymer entity maps to UniProt P76641; PMID 31283204 accession-code footnote names EcGuaD UniProt P76641. and applied mutation signature F210A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P76641 canonical sequence reconstructed with F210A; UniProtKB reviewed P76641/GUAD_ECOLI REST/FASTA: guanine deaminase, EC 3.5.4.3, Escherichia coli strain K12, canonical length 439 aa; RCSB 6OHB polymer entity maps to UniProt P76641; PMID 31283204 accession-code footnote names EcGuaD UniProt P76641.


sequence_variant_note: Resolved canonical sequence from UniProtKB P76641 canonical sequence reconstructed with W101H; UniProtKB reviewed P76641/GUAD_ECOLI REST/FASTA: guanine deaminase, EC 3.5.4.3, Escherichia coli strain K12, canonical length 439 aa; RCSB 6OHB polymer entity maps to UniProt P76641; PMID 31283204 accession-code footnote names EcGuaD UniProt P76641. and applied mutation signature W101H to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P76641 canonical wild-type sequence; UniProtKB reviewed P76641/GUAD_ECOLI REST/FASTA: guanine deaminase, EC 3.5.4.3, Escherichia coli strain K12, canonical length 439 aa; RCSB 6OHB polymer entity maps to UniProt P76641; PMID 31283204 accession-code footnote names EcGuaD UniProt P76641.


column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-allo-threonine block, enzyme row R313H: k_cat, s^-1 = 2.3; K_m, mM = 28; k_cat/K_m, s^-1 M^-1 = 80.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.3 s^-1 in the l-allo-threonine block of enzyme row R313H; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 2.3 s^(-1). Km: printed Table 2 cell 28 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 28.0 mM. kcat/Km: printed Table 2 cell 80 under the column head k_cat/K_m, s^-1 M^-1, that is 80.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 80.0 / 1000 = 0.08 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-allo-threonine block, enzyme row R313H: k_cat = 2.3 s^-1; K_m = 28 mM; printed k_cat/K_m = 80 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O07051, checked by REST/FASTA on 2026-06-07 and applied mutation signature D168N to reconstruct the assayed variant sequence.


column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-beta-phenylserine block, enzyme row N64I: k_cat, s^-1 = 0.2; K_m, mM = 0.8; k_cat/K_m, s^-1 M^-1 = 3 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.2 s^-1 in the l-beta-phenylserine block of enzyme row N64I; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 0.2 s^(-1). Km: printed Table 2 cell 0.8 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 0.8 mM. kcat/Km: printed Table 2 cell 3 x 10^2 under the column head k_cat/K_m, s^-1 M^-1, that is 300.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 300.0 / 1000 = 0.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-beta-phenylserine block, enzyme row N64I: k_cat = 0.2 s^-1; K_m = 0.8 mM; printed k_cat/K_m = 3 x 10^2 M^-1 s^-1.


column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-allo-threonine block, enzyme row D168V: k_cat, s^-1 = 0.02; K_m, mM = 2.7; k_cat/K_m, s^-1 M^-1 = 6.7.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.02 s^-1 in the l-allo-threonine block of enzyme row D168V; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 0.02 s^(-1). Km: printed Table 2 cell 2.7 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 2.7 mM. kcat/Km: printed Table 2 cell 6.7 under the column head k_cat/K_m, s^-1 M^-1, that is 6.7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.7 / 1000 = 0.0067 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-allo-threonine block, enzyme row D168V: k_cat = 0.02 s^-1; K_m = 2.7 mM; printed k_cat/K_m = 6.7 M^-1 s^-1.


sequence_source: UniProtKB reviewed accession O07051, checked by REST/FASTA on 2026-06-07


substrate_name: L-beta-Phenylserine; L-allo-threonine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O07051, checked by REST/FASTA on 2026-06-07 and applied mutation signature D168V to reconstruct the assayed variant sequence.

substrate: L-beta-Phenylserine; L-allo-threonine


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature R171Q to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-beta-phenylserine block, enzyme row R171Q: k_cat, s^-1 = 0.2; K_m, mM = 17; k_cat/K_m, s^-1 M^-1 = 11.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.2 s^-1 in the l-beta-phenylserine block of enzyme row R171Q; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 0.2 s^(-1). Km: printed Table 2 cell 17 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 17.0 mM. kcat/Km: printed Table 2 cell 11 under the column head k_cat/K_m, s^-1 M^-1, that is 11.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 11.0 / 1000 = 0.011 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-beta-phenylserine block, enzyme row R171Q: k_cat = 0.2 s^-1; K_m = 17 mM; printed k_cat/K_m = 11 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O07051, checked by REST/FASTA on 2026-06-07 and applied mutation signature K199R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature D168S to reconstruct the assayed variant sequence.

row_label: Table 2, l-beta-phenylserine block, enzyme row D168S


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature H85F to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-allo-threonine block, enzyme row H85F: k_cat, s^-1 = 0.05; K_m, mM = 11.5; k_cat/K_m, s^-1 M^-1 = 4.5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.05 s^-1 in the l-allo-threonine block of enzyme row H85F; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 0.05 s^(-1). Km: printed Table 2 cell 11.5 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 11.5 mM. kcat/Km: printed Table 2 cell 4.5 under the column head k_cat/K_m, s^-1 M^-1, that is 4.5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.5 / 1000 = 0.0045 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-allo-threonine block, enzyme row H85F: k_cat = 0.05 s^-1; K_m = 11.5 mM; printed k_cat/K_m = 4.5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature R171F to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-allo-threonine block, enzyme row R171F: k_cat, s^-1 = 0.23; K_m, mM = 18; k_cat/K_m, s^-1 M^-1 = 10.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.23 s^-1 in the l-allo-threonine block of enzyme row R171F; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 0.23 s^(-1). Km: printed Table 2 cell 18 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 18.0 mM. kcat/Km: printed Table 2 cell 10 under the column head k_cat/K_m, s^-1 M^-1, that is 10.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 10.0 / 1000 = 0.01 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-allo-threonine block, enzyme row R171F: k_cat = 0.23 s^-1; K_m = 18 mM; printed k_cat/K_m = 10 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature K199R to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-allo-threonine block, enzyme row K199R: k_cat, s^-1 = 0.08; K_m, mM = 2.7; k_cat/K_m, s^-1 M^-1 = 30.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.08 s^-1 in the l-allo-threonine block of enzyme row K199R; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 0.08 s^(-1). Km: printed Table 2 cell 2.7 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 2.7 mM. kcat/Km: printed Table 2 cell 30 under the column head k_cat/K_m, s^-1 M^-1, that is 30.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 30.0 / 1000 = 0.03 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-allo-threonine block, enzyme row K199R: k_cat = 0.08 s^-1; K_m = 2.7 mM; printed k_cat/K_m = 30 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from reconstructed_variant_sequence_from_uniprot_O07051 and applied mutation signature H85Y to reconstruct the assayed variant sequence.


column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-beta-phenylserine block, enzyme row H85F: k_cat, s^-1 = 0.3; K_m, mM = 4.6; k_cat/K_m, s^-1 M^-1 = 63.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.3 s^-1 in the l-beta-phenylserine block of enzyme row H85F; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 0.3 s^(-1). Km: printed Table 2 cell 4.6 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 4.6 mM. kcat/Km: printed Table 2 cell 63 under the column head k_cat/K_m, s^-1 M^-1, that is 63.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 63.0 / 1000 = 0.063 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-beta-phenylserine block, enzyme row H85F: k_cat = 0.3 s^-1; K_m = 4.6 mM; printed k_cat/K_m = 63 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature N64E to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-allo-threonine block, enzyme row N64E: k_cat, s^-1 = 0.3; K_m, mM = 5.7; k_cat/K_m, s^-1 M^-1 = 60.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.3 s^-1 in the l-allo-threonine block of enzyme row N64E; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 0.3 s^(-1). Km: printed Table 2 cell 5.7 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 5.7 mM. kcat/Km: printed Table 2 cell 60 under the column head k_cat/K_m, s^-1 M^-1, that is 60.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 60.0 / 1000 = 0.06 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-allo-threonine block, enzyme row N64E: k_cat = 0.3 s^-1; K_m = 5.7 mM; printed k_cat/K_m = 60 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature C196T to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-beta-phenylserine block, enzyme row C196T: k_cat, s^-1 = 84; K_m, mM = 3.7; k_cat/K_m, s^-1 M^-1 = 2.2 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 84 s^-1 in the l-beta-phenylserine block of enzyme row C196T; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 84.0 s^(-1). Km: printed Table 2 cell 3.7 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 3.7 mM. kcat/Km: printed Table 2 cell 2.2 x 10^4 under the column head k_cat/K_m, s^-1 M^-1, that is 22000.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 22000.0 / 1000 = 22.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-beta-phenylserine block, enzyme row C196T: k_cat = 84 s^-1; K_m = 3.7 mM; printed k_cat/K_m = 2.2 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O07051; row-specific substitution applied after residue-position check and applied mutation signature E138A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O07051; row-specific substitution applied after residue-position check and applied mutation signature C196T to reconstruct the assayed variant sequence.


column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-beta-phenylserine block, enzyme row R171F: k_cat, s^-1 = 0.17; K_m, mM = 7; k_cat/K_m, s^-1 M^-1 = 24.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.17 s^-1 in the l-beta-phenylserine block of enzyme row R171F; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 0.17 s^(-1). Km: printed Table 2 cell 7 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 7.0 mM. kcat/Km: printed Table 2 cell 24 under the column head k_cat/K_m, s^-1 M^-1, that is 24.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 24.0 / 1000 = 0.024 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-beta-phenylserine block, enzyme row R171F: k_cat = 0.17 s^-1; K_m = 7 mM; printed k_cat/K_m = 24 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature R231A to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-beta-phenylserine block, enzyme row R231A: k_cat, s^-1 = 2.3; K_m, mM = 4.1; k_cat/K_m, s^-1 M^-1 = 6 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.3 s^-1 in the l-beta-phenylserine block of enzyme row R231A; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 2.3 s^(-1). Km: printed Table 2 cell 4.1 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 4.1 mM. kcat/Km: printed Table 2 cell 6 x 10^2 under the column head k_cat/K_m, s^-1 M^-1, that is 600.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 600.0 / 1000 = 0.6 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-beta-phenylserine block, enzyme row R231A: k_cat = 2.3 s^-1; K_m = 4.1 mM; printed k_cat/K_m = 6 x 10^2 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O07051; row-specific substitution applied after residue-position check and applied mutation signature D168S to reconstruct the assayed variant sequence.


row_label: Table 2, l-allo-threonine block, enzyme row N64E


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature H85Y to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-beta-phenylserine block, enzyme row H85Y: k_cat, s^-1 = 0.2; K_m, mM = 3.8; k_cat/K_m, s^-1 M^-1 = 50.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.2 s^-1 in the l-beta-phenylserine block of enzyme row H85Y; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 0.2 s^(-1). Km: printed Table 2 cell 3.8 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 3.8 mM. kcat/Km: printed Table 2 cell 50 under the column head k_cat/K_m, s^-1 M^-1, that is 50.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 50.0 / 1000 = 0.05 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-beta-phenylserine block, enzyme row H85Y: k_cat = 0.2 s^-1; K_m = 3.8 mM; printed k_cat/K_m = 50 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from catalog_carried_uniprot_O07051_canonical_sequence and applied mutation signature E138A to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-allo-threonine block, enzyme row E138A: k_cat, s^-1 = 3.9; K_m, mM = 2.3; k_cat/K_m, s^-1 M^-1 = 1.7 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.9 s^-1 in the l-allo-threonine block of enzyme row E138A; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 3.9 s^(-1). Km: printed Table 2 cell 2.3 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 2.3 mM. kcat/Km: printed Table 2 cell 1.7 x 10^3 under the column head k_cat/K_m, s^-1 M^-1, that is 1700.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1700.0 / 1000 = 1.7 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-allo-threonine block, enzyme row E138A: k_cat = 3.9 s^-1; K_m = 2.3 mM; printed k_cat/K_m = 1.7 x 10^3 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A825 FASTA retrieved 2026-06-07; mutation applied from selected mutation_signature when present and applied mutation signature R235Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A825 FASTA retrieved 2026-06-07; mutation applied from selected mutation_signature when present and applied mutation signature Y55F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0A825 FASTA retrieved 2026-06-07; mutation applied from selected mutation_signature when present

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A825 FASTA retrieved 2026-06-07; mutation applied from selected mutation_signature when present and applied mutation signature R235K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-allo-threonine aldolase(Enzyme) mutant R235K


proof_lines: SABIO-RK modifier species: L-allo-threonine aldolase(Enzyme) mutant R235Q


proof_lines: SABIO-RK modifier species: L-allo-threonine aldolase(Enzyme) mutant Y55F


column_label: Table 2 carries one enzyme-label column, then a three-column span headed l-allo-threonine and a four-column span headed l-beta-phenylserine. The kinetic column heads, printed once under each span, are k_cat, s^-1 | K_m, mM | k_cat/K_m, s^-1 M^-1, and the last column of the l-beta-phenylserine span is Aldol reaction, conv. %. The cited cell set is Table 2, l-allo-threonine block, enzyme row R231A: k_cat, s^-1 = 0.7; K_m, mM = 7.5; k_cat/K_m, s^-1 M^-1 = 90.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.7 s^-1 in the l-allo-threonine block of enzyme row R231A; the printed turnover column of this paper is already per second, so no conversion applies and the paper value is 0.7 s^(-1). Km: printed Table 2 cell 7.5 under the column head K_m, mM; the column is already in mM, so no conversion applies and the paper value is 7.5 mM. kcat/Km: printed Table 2 cell 90 under the column head k_cat/K_m, s^-1 M^-1, that is 90.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 90.0 / 1000 = 0.09 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, l-allo-threonine block, enzyme row R231A: k_cat = 0.7 s^-1; K_m = 7.5 mM; printed k_cat/K_m = 90 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB O07051 FASTA and JSON direct lookup on 2026-06-07; variant reconstructed from selected mutation signature. and applied mutation signature R171Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O07051 FASTA and JSON direct lookup on 2026-06-07; variant reconstructed from selected mutation signature. and applied mutation signature K224A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB O07051 FASTA and JSON direct lookup on 2026-06-07; variant reconstructed from selected mutation signature.


sequence_source: UniProtKB O07051 FASTA and JSON direct lookup on 2026-06-07.

proof_lines:
pH 8.0, 30°C, wild-type enzyme
pH 8.0, 25°C, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB O07051 FASTA and JSON direct lookup on 2026-06-07; variant reconstructed from selected mutation signature. and applied mutation signature K51A to reconstruct the assayed variant sequence.


organism: Rattus norvegicus

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


sequence_variant_note: Resolved canonical sequence from UniProtKB O07051 FASTA direct lookup; variant reconstructed by applying the row mutation to the canonical sequence. and applied mutation signature N64I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O07051 FASTA direct lookup; variant reconstructed by applying the row mutation to the canonical sequence. and applied mutation signature S198H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O07051 FASTA direct lookup; variant reconstructed by applying the row mutation to the canonical sequence. and applied mutation signature H85F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O07051 FASTA direct lookup; variant reconstructed by applying the row mutation to the canonical sequence. and applied mutation signature R231A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O07051 FASTA direct lookup; variant reconstructed by applying the row mutation to the canonical sequence. and applied mutation signature R171Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB O07051 FASTA direct lookup; variant reconstructed by applying the row mutation to the canonical sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O07051 FASTA direct lookup; variant reconstructed by applying the row mutation to the canonical sequence. and applied mutation signature G200S to reconstruct the assayed variant sequence.


organism: Unknown


enzyme_display_name: acylphosphatase

organism: Bos taurus

substrate_name: Benzoyl phosphate; H2O

ki_unit: mM

sequence_source: UniProtKB reviewed accession P41500; direct lookup 2026-06-07

enzyme: acylphosphatase

substrate: Benzoyl phosphate; H2O


organism: Drosophila melanogaster

substrate_name: Benzoyl phosphate

sequence_source: UniProtKB reviewed accession Q9VF36; direct lookup 2026-06-07

substrate: Benzoyl phosphate


substrate_name: H2O; Benzoyl phosphate

substrate: H2O; Benzoyl phosphate


sequence_source: UniProtKB reviewed accession P56544; direct lookup 2026-06-07


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

mutation_type: deletion

proof_lines: SABIO-RK modifier species: acylphosphatase(Enzyme) mutant AcPDro delta22


organism: Escherichia coli

proof_lines: SABIO-RK modifier species: acylphosphatase(Enzyme) mutant C8A


sequence_source: UniProtKB reviewed accession P0AB65; direct lookup 2026-06-07


organism: Lactococcus lactis subsp. lactis

substrate_name: Mannitol 1-phosphate; H2O

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

substrate: Mannitol 1-phosphate; H2O


substrate_name: H2O; Mannitol 1-phosphate

substrate: H2O; Mannitol 1-phosphate


proof_lines:
SABIO-RK modifier species: HPr S46A
SABIO-RK modifier species: S46A HPr


proof_lines:
SABIO-RK modifier species: HPr S46D
SABIO-RK modifier species: S46D HPr


proof_lines: kcat is 17.4 sec(-1) with guanine as substrate.


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

substrate_name: L-serine (at 37 degrees Celsius)

proof_lines: kcat is 212 min(-1) for the L-serine hydroxymethyltransferase reaction, and 687 min(-1) for the L-allo-threonine cleavage, at 37 and 60 degrees Celsius, respectively. The presence of oxygen does not seem to affect significantly the kinetic

substrate: L-serine (at 37 degrees Celsius)


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


organism: Escherichia coli (strain K12)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


substrate_name: Sulfide

proof_lines: pH 7.5, 60°C, membrane-bound wild-type enzyme

substrate: Sulfide


organism: Bacillus subtilis

substrate_name: 4-nitrophenyl phosphate

sequence_source: UniProtKB reviewed P94526 (ARAL_BACSU), sequence version 1; PMID 21575135 evidence links AraL to EC 3.1.3.23 and the selected substrate/pH context.

substrate: 4-nitrophenyl phosphate


substrate_name: alpha-D-gentiobiose 1-phosphate

substrate: alpha-D-gentiobiose 1-phosphate


organism: Lactococcus lactis

substrate_name: mannitol 1-phosphate

substrate: mannitol 1-phosphate


sequence_source: UniProtKB reviewed accession P0AB65


organism: Gallus gallus

sequence_source: UniProtKB reviewed accession P07031


sequence_source: UniProtKB reviewed accession P07032


organism: Homo sapiens

sequence_source: UniProtKB reviewed accession P07311


proof_lines: SABIO-RK modifier species: acylphosphatase(Enzyme) mutant H25Q


sequence_source: UniProtKB reviewed accession P14621


proof_lines: SABIO-RK modifier species: acylphosphatase(Enzyme) mutant R97Q


organism: Pyrococcus horikoshii

substrate_name: benzoyl phosphate

sequence_source: UniProtKB reviewed exact accession P84142; direct UniProt REST lookup on 2026-06-07.

proof_lines:
pH 5.3, 45°C, wild-type enzyme
pH 5.3, 25°C, wild-type enzyme

substrate: benzoyl phosphate


organism: Sulfolobus solfataricus

sequence_source: UniProtKB reviewed exact accession Q97ZL0; direct UniProt REST lookup on 2026-06-07.


organism: Sus scrofa

sequence_source: UniProtKB reviewed exact accession P24540; direct UniProt REST lookup on 2026-06-07.


organism: Vibrio cholerae

substrate_name: acetyl phosphate

sequence_source: UniProtKB reviewed exact accession A5F8G9; direct UniProt REST lookup on 2026-06-07.

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

substrate: acetyl phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed exact accession A5F8G9 plus selected C20R mutation; direct UniProt REST lookup on 2026-06-07. and applied mutation signature C20R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C20R, pH and temperature not specified in the publication


proof_lines:
Raw SKiD Env: Temp=-----, pH=and
Raw SKiD Env: Temp=-----, pH=-----


mutation_signature: Δ6

proof_lines: SABIO-RK modifier species: acylphosphatase(Enzyme) wildtype delta 6 N-terminal truncated


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14621 and applied mutation signature Y98Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acylphosphatase(Enzyme) mutant Y98Q


proof_lines: SABIO-RK modifier species: acylphosphatase(Enzyme) mutant delta+2

proof_lines: SABIO-RK modifier species: acylphosphatase(Enzyme) mutant delta+4

proof_lines: SABIO-RK modifier species: acylphosphatase(Enzyme) mutant delta-2