sequence_source: UniProtKB Q8NKB0 REST lookup on 2026-06-03

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


organism: Clonostachys rosea

substrate_name: zearalenone

source_db: brenda

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8NKB0 REST lookup on 2026-06-03 plus selected BRENDA mutation note and applied mutation signature D133K to reconstruct the assayed variant sequence.

mutation_type: substitution

substrate: zearalenone

source: brenda


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8NKB0 REST lookup on 2026-06-03 plus selected BRENDA mutation note and applied mutation signature L155K to reconstruct the assayed variant sequence.


kcat_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8NKB0 REST lookup on 2026-06-03 plus selected BRENDA mutation note and applied mutation signature D133K/E171K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D133K/E171K, at pH 8.0 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8NKB0 REST lookup on 2026-06-03 plus selected BRENDA mutation note and applied mutation signature M154H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8NKB0 REST lookup on 2026-06-03 plus selected BRENDA mutation note and applied mutation signature D157K/E171K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D157K/E171K, at pH 8.0 and 37°C


organism: Saccharolobus islandicus

substrate_name: nonanoic-gamma-lactone

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:C4KKZ9 and applied mutation signature Y34Q to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH not specified in the publication, mutant enzyme Y34Q

substrate: nonanoic-gamma-lactone


substrate_name: N-(3-oxooctanoyl)-DL-homoserine lactone

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:C4KKZ9 and applied mutation signature E14K/Y34Q to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH not specified in the publication, mutant enzyme E14K/Y34Q

substrate: N-(3-oxooctanoyl)-DL-homoserine lactone


substrate_name: dodecanoic-gamma-lactone

mutation_signature: Unknown

proof_lines: 25°C, pH not specified in the publication, wild-type enzyme

substrate: dodecanoic-gamma-lactone


organism: Saccharolobus solfataricus

substrate_name: N-octanoylhomoserine lactone

substrate: N-octanoylhomoserine lactone


substrate_name: N-(3-oxodecanoyl)-L-homoserine lactone

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:Q97VT7 and applied mutation signature W263T to reconstruct the assayed variant sequence.

substrate: N-(3-oxodecanoyl)-L-homoserine lactone


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:Q97VT7 and applied mutation signature W263I to reconstruct the assayed variant sequence.


substrate_name: delta-undecanolactone

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:Q97VT7 and applied mutation signature W263L to reconstruct the assayed variant sequence.

substrate: delta-undecanolactone


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:Q97VT7 and applied mutation signature W263V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt direct accession lookup on 2026-06-03 and applied mutation signature E219K to reconstruct the assayed variant sequence.


organism: Fusarium proliferatum

substrate_name: DL-pantoyllactone

sequence_source: UniProt direct accession lookup on 2026-06-03

substrate: DL-pantoyllactone


organism: Homo sapiens

substrate_name: dihydrocoumarin

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

proof_lines:
25°C, enzyme variant R192
25°C, enzyme variant Q192

substrate: dihydrocoumarin


substrate_name: 5-Valerolactone; H2O

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

sequence_variant_note: Resolved canonical sequence from UniProt direct accession lookup on 2026-06-03 and applied mutation signature H134Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

proof_lines: SABIO-RK modifier species: 1,4-lactonase(Enzyme) mutant H134Q

substrate: 5-Valerolactone; H2O


substrate_name: delta-valerolactone

proof_lines:
pH 8.0, wild-type enzyme
wild-type, pH 8.3, 25°C

substrate: delta-valerolactone


substrate_name: H2O; 5-(Thiobutyl)butyrolactone

sequence_variant_note: Resolved canonical sequence from UniProt direct accession lookup on 2026-06-03 and applied mutation signature H115Q/H134Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 1,4-lactonase(Enzyme) mutant H115Q/H134Q

substrate: H2O; 5-(Thiobutyl)butyrolactone


substrate_name: H2O; 5-Valerolactone

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

assay_conditions_summary: pH 8; buffer notes

proof_lines: pH 8.3, activity buffer with 0.1% tergitol

proof_lines: isoform PON1, pH and temperature not specified in the publication

substrate: H2O; 5-Valerolactone


substrate_name: gamma-undecanolactone

sequence_variant_note: Resolved canonical sequence from UniProtKB Q97VT7 direct REST lookup; W263M reconstructed from canonical sequence and applied mutation signature W263M to reconstruct the assayed variant sequence.

substrate: gamma-undecanolactone


sequence_variant_note: Resolved canonical sequence from UniProtKB Q97VT7 direct REST lookup; W263F reconstructed from canonical sequence and applied mutation signature W263F to reconstruct the assayed variant sequence.


organism: Sulfolobus acidocaldarius

sequence_source: UniProtKB Q4J6Z8 direct REST lookup

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


organism: Vulcanisaeta moutnovskia

substrate_name: octanoyl-L-homoserine lactone

sequence_source: UniProtKB F0QXN6 direct REST lookup

proof_lines: pH 8.3, temperature not specified in the publication

substrate: octanoyl-L-homoserine lactone


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA direct accession check and applied mutation signature H115Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 1,4-lactonase(Enzyme) mutant H115Q


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA direct accession check and applied mutation signature H115W to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST FASTA direct accession check


substrate_name: 3-oxo-dodecanoyl L-homoserine lactone

km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA direct accession check and applied mutation signature S311C to reconstruct the assayed variant sequence.

substrate: 3-oxo-dodecanoyl L-homoserine lactone


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA direct accession check and applied mutation signature A148G to reconstruct the assayed variant sequence.


organism: Rattus norvegicus


proof_lines: 25°C, pH not specified in the publication, mutant enzyme E14K


organism: Agrobacterium tumefaciens

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


organism: Mycobacterium tuberculosis

substrate_name: patulin

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

substrate: patulin


substrate_name: gamma-hydroxybutyrate

substrate: gamma-hydroxybutyrate


organism: synthetic construct

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tris

proof_lines: recombinant lactonase, in 50 mM Tris buffer, 1 mM NaCl, pH 8.0 at 25°C


organism: uncultured marine bacterium

substrate_name: N-(3-oxohexanoyl)-L-homoserine lactone

substrate: N-(3-oxohexanoyl)-L-homoserine lactone


enzyme_display_name: manganese peroxidase

organism: Moniliophthora roreri

substrate_name: veratryl alcohol

source_db: oed

verification_status: unverified

sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 plus row mutation_signature reconstruction and applied mutation signature A172W with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.

data_origin: experimental

enzyme: manganese peroxidase

substrate: veratryl alcohol

status: unverified

source: oed


sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 plus row mutation_signature reconstruction and applied mutation signature A172W/F259M with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 plus row mutation_signature reconstruction and applied mutation signature A172W/A269R with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 plus row mutation_signature reconstruction and applied mutation signature A172W/K168V with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


substrate_name: Reactive Black 5

sequence_source: UniProtKB:V2XS39 plus row mutation_signature reconstruction

substrate: Reactive Black 5


sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 plus row mutation_signature reconstruction and applied mutation signature A172W/I171V with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


kcat_over_km_origin: calculated


organism: Irpex lacteus

sequence_variant_note: Resolved canonical sequence from UniProtKB:S4W784 direct REST FASTA lookup on 2026-06-03; TrEMBL peroxidase, Irpex lacteus, EMBL AGO86670.2 evidence and applied mutation signature E166Q to reconstruct the assayed variant sequence.

proof_lines: pH 4.0, 30°C, recombinant mutant E166Q, in absence of Mn2+


sequence_source: UniProtKB:S4W784 direct REST FASTA lookup on 2026-06-03; TrEMBL peroxidase, Irpex lacteus, EMBL AGO86670.2 evidence


sequence_variant_note: Resolved canonical sequence from UniProtKB:S4W784 direct REST FASTA lookup on 2026-06-03; TrEMBL peroxidase, Irpex lacteus, EMBL AGO86670.2 evidence and applied mutation signature E166D to reconstruct the assayed variant sequence.

proof_lines: pH 4.0, 30°C, recombinant mutant E166D, in absence of Mn2+


sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 direct REST FASTA lookup on 2026-06-03; TrEMBL peroxidase, Moniliophthora roreri strain MCA 2997, EMBL ESK95360.1 evidence and applied mutation signature A172W/A269R with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 direct REST FASTA lookup on 2026-06-03; TrEMBL peroxidase, Moniliophthora roreri strain MCA 2997, EMBL ESK95360.1 evidence and applied mutation signature A172W/F259M with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 direct REST FASTA lookup on 2026-06-03; TrEMBL peroxidase, Moniliophthora roreri strain MCA 2997, EMBL ESK95360.1 evidence and applied mutation signature A172W/K168V with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:V2XS39 direct REST FASTA lookup on 2026-06-03; TrEMBL peroxidase, Moniliophthora roreri strain MCA 2997, EMBL ESK95360.1 evidence and applied mutation signature A172W with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:V2XS39 direct REST FASTA lookup on 2026-06-03; TrEMBL peroxidase, Moniliophthora roreri strain MCA 2997, EMBL ESK95360.1 evidence


organism: Gelatoporia subvermispora

sequence_variant_note: Resolved canonical sequence from https://rest.uniprot.org/uniprotkb/M2REM6 (retrieved 2026-06-03) and applied mutation signature S168W with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


substrate_name: Mn(II)

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

substrate: Mn(II)


sequence_variant_note: Resolved canonical sequence from https://rest.uniprot.org/uniprotkb/M2REM6 (retrieved 2026-06-03) and applied mutation signature T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


verification_status: verified

smiles: OO

column_label: Table 2 (Kinetic parameters of Il-DyP4 and Il-MnP6 for substrates oxidation, obtained based on the optimal pH and temperature), substrate row 'H2O2', Il-MnP6 block; column 'pH' = 4.5; column 'Temperature' = 30; the 'Kinetic constants' column of that block prints 'Km' = 194 (uM), 'kcat' = 879 (s^-1) and 'kcat/Km' = 4.5 x 10^6 (s^-1 M^-1).

normalized_value_unit_evidence: Km: printed Table 2 cell 194 uM; 194 / 1000 = 0.194 mM; the exported value is 0.194 mM. kcat: printed Table 2 cell 879 s^-1; already in s^-1, no unit conversion applies; the exported value is 879.0 s^(-1). kcat/Km: the exported value 4530.927835051546 s^(-1)*mM^(-1) is the full-precision quotient 879.0 / 0.194 of the two printed component cells; the paper's printed efficiency cell is 4.5 x 10^6 s^-1 M^-1, and 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so that cell is 4500.0 s^-1 mM^-1, the two-significant-figure rendering of the same quotient.

raw_value_unit_evidence: Table 2, Il-MnP6 half of the substrate row 'H2O2': Km = 194 uM; kcat = 879 s^-1; printed kcat/Km = 4.5 x 10^6 s^-1 M^-1; printed pH = 4.5; printed temperature = 30 C.

table_label: Table 2: Kinetic parameters - Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1) of Il-DyP4 and Il-MnP6 for substrates oxidation obtained based on the optimal pH and temperature (C) (AMB Express 2018, 8:119)

status: verified


substrate_name: Reactive Blue 19

sequence_source: UniProt REST/FASTA direct lookup for A0A2P1C6N7

proof_lines: pH 3.0, 35°C, recombinant His6-tagged enzyme

proof_lines: pH 3.5, 45°C, recombinant His6-tagged enzyme

proof_lines: pH 4.0, 45°C, recombinant His6-tagged enzyme

substrate: Reactive Blue 19


column_label: Table 2 (Kinetic parameters of Il-DyP4 and Il-MnP6 for substrates oxidation, obtained based on the optimal pH and temperature), substrate row 'ABTS', Il-MnP6 block; column 'pH' = 3.5; column 'Temperature' = 45; the 'Kinetic constants' column of that block prints 'Km' = 83 (uM), 'kcat' = 245 (s^-1) and 'kcat/Km' = 3.0 x 10^6 (s^-1 M^-1).

normalized_value_unit_evidence: Km: printed Table 2 cell 83 uM; 83 / 1000 = 0.083 mM; the exported value is 0.083 mM. kcat: printed Table 2 cell 245 s^-1; already in s^-1, no unit conversion applies; the exported value is 245.0 s^(-1). kcat/Km: the exported value 2951.8072289156626 s^(-1)*mM^(-1) is the full-precision quotient 245.0 / 0.083 of the two printed component cells; the paper's printed efficiency cell is 3.0 x 10^6 s^-1 M^-1, and 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so that cell is 3000.0 s^-1 mM^-1, the two-significant-figure rendering of the same quotient.

raw_value_unit_evidence: Table 2, Il-MnP6 half of the substrate row 'ABTS': Km = 83 uM; kcat = 245 s^-1; printed kcat/Km = 3.0 x 10^6 s^-1 M^-1; printed pH = 3.5; printed temperature = 45 C.


column_label: Table 2 (Kinetic parameters of Il-DyP4 and Il-MnP6 for substrates oxidation, obtained based on the optimal pH and temperature), substrate row 'Mn2+', Il-MnP6 block; column 'pH' = 4.5; column 'Temperature' = 30; the 'Kinetic constants' column of that block prints 'Km' = 129 (uM), 'kcat' = 369 (s^-1) and 'kcat/Km' = 2.9 x 10^6 (s^-1 M^-1).

normalized_value_unit_evidence: Km: printed Table 2 cell 129 uM; 129 / 1000 = 0.129 mM; the exported value is 0.129 mM. kcat: printed Table 2 cell 369 s^-1; already in s^-1, no unit conversion applies; the exported value is 369.0 s^(-1). kcat/Km: the exported value 2860.4651162790697 s^(-1)*mM^(-1) is the full-precision quotient 369.0 / 0.129 of the two printed component cells; the paper's printed efficiency cell is 2.9 x 10^6 s^-1 M^-1, and 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so that cell is 2900.0 s^-1 mM^-1, the two-significant-figure rendering of the same quotient.

raw_value_unit_evidence: Table 2, Il-MnP6 half of the substrate row 'Mn2+': Km = 129 uM; kcat = 369 s^-1; printed kcat/Km = 2.9 x 10^6 s^-1 M^-1; printed pH = 4.5; printed temperature = 30 C.


column_label: Table 2 (Kinetic parameters of Il-DyP4 and Il-MnP6 for substrates oxidation, obtained based on the optimal pH and temperature), substrate row 'DMP', Il-MnP6 block; column 'pH' = 4.5; column 'Temperature' = 55; the 'Kinetic constants' column of that block prints 'Km' = 53 (uM), 'kcat' = 989 (s^-1) and 'kcat/Km' = 1.9 x 10^7 (s^-1 M^-1).

normalized_value_unit_evidence: Km: printed Table 2 cell 53 uM; 53 / 1000 = 0.053 mM; the exported value is 0.053 mM. kcat: printed Table 2 cell 989 s^-1; already in s^-1, no unit conversion applies; the exported value is 989.0 s^(-1). kcat/Km: the exported value 18660.377358490565 s^(-1)*mM^(-1) is the full-precision quotient 989.0 / 0.053 of the two printed component cells; the paper's printed efficiency cell is 1.9 x 10^7 s^-1 M^-1, and 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so that cell is 19000.0 s^-1 mM^-1, the two-significant-figure rendering of the same quotient.

raw_value_unit_evidence: Table 2, Il-MnP6 half of the substrate row 'DMP': Km = 53 uM; kcat = 989 s^-1; printed kcat/Km = 1.9 x 10^7 s^-1 M^-1; printed pH = 4.5; printed temperature = 55 C.


substrate_name: guaiacol

column_label: Table 2 (Kinetic parameters of Il-DyP4 and Il-MnP6 for substrates oxidation, obtained based on the optimal pH and temperature), substrate row 'Guaiacol', Il-MnP6 block; column 'pH' = 4; column 'Temperature' = 45; the 'Kinetic constants' column of that block prints 'Km' = 2.6 (uM), 'kcat' = 184 (s^-1) and 'kcat/Km' = 7.1 x 10^7 (s^-1 M^-1).

normalized_value_unit_evidence: Km: printed Table 2 cell 2.6 uM; 2.6 / 1000 = 0.0026 mM; the exported value is 0.0026 mM. kcat: printed Table 2 cell 184 s^-1; already in s^-1, no unit conversion applies; the exported value is 184.0 s^(-1). kcat/Km: the exported value 70769.23076923077 s^(-1)*mM^(-1) is the full-precision quotient 184.0 / 0.0026 of the two printed component cells; the paper's printed efficiency cell is 7.1 x 10^7 s^-1 M^-1, and 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so that cell is 71000.0 s^-1 mM^-1, the two-significant-figure rendering of the same quotient.

raw_value_unit_evidence: Table 2, Il-MnP6 half of the substrate row 'Guaiacol': Km = 2.6 uM; kcat = 184 s^-1; printed kcat/Km = 7.1 x 10^7 s^-1 M^-1; printed pH = 4; printed temperature = 45 C.

substrate: guaiacol


verification_status: corrected

column_label: Table 2 (Kinetic parameters of Il-DyP4 and Il-MnP6 for substrates oxidation, obtained based on the optimal pH and temperature), substrate row 'RBlack 5', Il-MnP6 block; column 'pH' = 3; column 'Temperature' = 35; the 'Kinetic constants' column of that block prints 'Km' = 4.4 (uM), 'kcat' = 0.06 (s^-1) and 'kcat/Km' = 1.5 x 10^4 (s^-1 M^-1).

normalized_value_unit_evidence: Km: printed Table 2 cell 4.4 uM; 4.4 / 1000 = 0.0044 mM; the exported value is 0.0044 mM. kcat: printed Table 2 cell 0.06 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.06 s^(-1). kcat/Km: printed Table 2 cell 1.5 x 10^4 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 1.5 x 10^4 / 1000 = 15.0 s^-1 mM^-1, which is the value proposed for the efficiency metric.

raw_value_unit_evidence: Table 2, Il-MnP6 half of the substrate row 'RBlack 5': Km = 4.4 uM; kcat = 0.06 s^-1; printed kcat/Km = 1.5 x 10^4 s^-1 M^-1; printed pH = 3; printed temperature = 35 C.

status: corrected


column_label: Table 2 (Kinetic parameters of Il-DyP4 and Il-MnP6 for substrates oxidation, obtained based on the optimal pH and temperature), substrate row 'RBlue 19', Il-MnP6 block; column 'pH' = 3; column 'Temperature' = 35; the 'Kinetic constants' column of that block prints 'Km' = 81 (uM), 'kcat' = 7.3 (s^-1) and 'kcat/Km' = 9.0 x 10^4 (s^-1 M^-1).

normalized_value_unit_evidence: Km: printed Table 2 cell 81 uM; 81 / 1000 = 0.081 mM; the exported value is 0.081 mM. kcat: printed Table 2 cell 7.3 s^-1; already in s^-1, no unit conversion applies; the exported value is 7.3 s^(-1). kcat/Km: the exported value 90.12345679012346 s^(-1)*mM^(-1) is the full-precision quotient 7.3 / 0.081 of the two printed component cells; the paper's printed efficiency cell is 9.0 x 10^4 s^-1 M^-1, and 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so that cell is 90.0 s^-1 mM^-1, the two-significant-figure rendering of the same quotient.

raw_value_unit_evidence: Table 2, Il-MnP6 half of the substrate row 'RBlue 19': Km = 81 uM; kcat = 7.3 s^-1; printed kcat/Km = 9.0 x 10^4 s^-1 M^-1; printed pH = 3; printed temperature = 35 C.


sequence_variant_note: Resolved canonical sequence from UniProt REST/FASTA direct lookup for S4W784 plus local E166D reconstruction and applied mutation signature E166D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:S4W784 / NCBI Protein:AGO86670.2 with E166G and applied mutation signature E166G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:S4W784 / NCBI Protein:AGO86670.2 with E166D and applied mutation signature E166D to reconstruct the assayed variant sequence.


sequence_source: reconstructed from UniProtKB:S4W784 / NCBI Protein:AGO86670.2 with E166G


sequence_source: UniProtKB:S4W784 / NCBI Protein:AGO86670.2

proof_lines: pH 4.0, 30°C, recombinant wild-type enzyme, in presence of Mn2+

proof_lines: pH 7.4, 30°C, recombinant wild-type enzyme, in absence of Mn2+

proof_lines: pH 7.4, 30°C, recombinant wild-type enzyme, in presence of Mn2+


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:S4W784 / NCBI Protein:AGO86670.2 with E166Q and applied mutation signature E166Q to reconstruct the assayed variant sequence.


proof_lines: pH 4.0, 30°C, recombinant mutant E166G, in absence of Mn2+


organism: Phanerochaete chrysosporium

substrate_name: Hexacyanoferrate(II); H2O2; H+

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

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: manganese peroxidase(Enzyme) mutant R177K

substrate: Hexacyanoferrate(II); H2O2; H+


sequence_source: UniProtKB Q02567 REST/FASTA direct check


proof_lines: SABIO-RK modifier species: manganese peroxidase(Enzyme) mutant R177A


organism: Phanerodontia chrysosporium

substrate_name: Phenol red

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

proof_lines:
isoenzyme H3
isoenzyme H5
isoenzyme H4

substrate: Phenol red


organism: Agrocybe praecox

proof_lines: 0.1 mM H2O2, Mn2+-independent activity, MnP1


organism: Bjerkandera adusta

proof_lines:
Mn2+-dependent activity
Mn2+-independent activity


organism: Bjerkandera sp.

proof_lines:
Mn2+-dependent activity, BOS2
isoform BOS2, at pH 5.0 and 30°C
0.1 mM Mn2+, BOS1


organism: Deuteromycotina sp.


organism: Dichomitus squalens


organism: Klebsiella pneumoniae


sequence_variant_note: Resolved canonical sequence from UniProt V2XS39 FASTA, reconstructed with paper-to-UniProt residue offset +19 and applied mutation signature A172W/A273T with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_source: UniProt V2XS39 FASTA, reconstructed with paper-to-UniProt residue offset +19


sequence_variant_note: Resolved canonical sequence from UniProt V2XS39 FASTA, reconstructed with paper-to-UniProt residue offset +19 and applied mutation signature A172W/I171V with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt V2XS39 FASTA, reconstructed with paper-to-UniProt residue offset +19 and applied mutation signature A172W with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt V2XS39 FASTA, reconstructed with paper-to-UniProt residue offset +19 and applied mutation signature A172W/A269R with inferred residue-numbering offset +19 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P19136 direct FASTA lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02567 direct FASTA lookup plus mature-chain offset from UniProt feature table and applied mutation signature R177Q with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


organism: Lentinus tigrinus

proof_lines: with 1.5 mM Mn2+ as cosubstrate, pH 5.5, 45°C

proof_lines: in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2, 45°C

proof_lines: in 0.05 M malonate-NaOH buffer pH 4.0 containing 0.2 mM H2O2 and 1.5 mM Mn2+, 45°C


organism: Musa x paradisiaca


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

proof_lines: A48C/A63C double mutant MnP after thermal treatment at 37°C for 15 min

proof_lines: recombinant MnP and A48C/A63C double mutant MnP


organism: Pleurotus eryngii

assay_conditions_summary: cofactor NADH

proof_lines:
0.1 mM Mn2+, 0.1 mM H2O2
0.1 mM 2,6-dimethoxyphenol, 0.1 mM H2O2
below


organism: Pleurotus ostreatus


organism: Schizophyllum commune


organism: Schizophyllum sp.


organism: Stropharia coronilla


organism: Trichophyton rubrum

proof_lines:
reaction with Mn2+
reactioin with H2O2
reaction with H2O2


sequence_variant_note: Resolved canonical sequence from UniProtKB Q02567 (PEM1_PHACH), MNP1/MnP1 precursor for Phanerodontia chrysosporium; signal peptide 1-21, mature chain 22-378. and applied mutation signature R177E with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q02567 (PEM1_PHACH), MNP1/MnP1 precursor for Phanerodontia chrysosporium; signal peptide 1-21, mature chain 22-378. and applied mutation signature R177Q with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q02567 (PEM1_PHACH), MNP1/MnP1 precursor for Phanerodontia chrysosporium; signal peptide 1-21, mature chain 22-378. and applied mutation signature R177D with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q02567 (PEM1_PHACH), MNP1/MnP1 precursor for Phanerodontia chrysosporium; signal peptide 1-21, mature chain 22-378. and applied mutation signature R177K with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q02567 (PEM1_PHACH), MNP1/MnP1 precursor for Phanerodontia chrysosporium; signal peptide 1-21, mature chain 22-378. and applied mutation signature E35Q with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


substrate_name: ferrocyanide

sequence_variant_note: Resolved canonical sequence from UniProtKB Q02567 (PEM1_PHACH), MNP1/MnP1 precursor for Phanerodontia chrysosporium; signal peptide 1-21, mature chain 22-378. and applied mutation signature F190A with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.

proof_lines:
MnP1 from mutant F190A
mutant enzyme F190A, at pH 4.5 and 25°C

substrate: ferrocyanide


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02567 plus PMID:9100022 F190I mutation note and applied mutation signature F190I with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02567 plus PMID:9100022 F190L mutation note and applied mutation signature F190L with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F190L, at pH 4.5 and 25 °C


proof_lines: MnP1 from mutants F190Y, F190L, F190I and F190A


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

proof_lines:
wild-type MnP1
wild-type MnP
wild-type enzyme


organism: Phlebiopsis flavidoalba


organism: Gelatoporia subvermispora

sequence_variant_note: Resolved canonical sequence from UniProt REST M2REM6 FASTA; variant reconstructed from PMID 25788979 mutation context with +21 offset and applied mutation signature T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


sequence_source: UniProt REST M2REM6 FASTA; variant reconstructed from PMID 25788979 mutation context with +21 offset


sequence_source: UniProt REST M2REM6 FASTA


sequence_variant_note: Resolved canonical sequence from UniProt REST M2REM6 FASTA; variant reconstructed from PMID 25788979 mutation context with +21 offset and applied mutation signature S168W with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST M2REM6 FASTA; variant reconstructed from PMID 25788979 mutation context with +21 offset and applied mutation signature S168W with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


enzyme_display_name: cystathionine beta-synthase

organism: Unknown

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

enzyme: cystathionine beta-synthase


organism: Rattus norvegicus

substrate_name: L-Homocysteine; L-Serine

sequence_source: UniProtKB:P32232 direct REST lookup on 2026-06-03

substrate: L-Homocysteine; L-Serine


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:P32582 direct REST lookup on 2026-06-03


substrate_name: L-Serine

substrate: L-Serine


substrate_name: L-Homocysteine

substrate: L-Homocysteine


substrate_name: L-Cystathionine; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB:P32582 direct REST lookup on 2026-06-03 and applied mutation signature Y158F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant Y158F His-tagged

substrate: L-Cystathionine; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB:P32582 direct REST lookup on 2026-06-03 and applied mutation signature T85A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant T85A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:P32582 direct REST lookup on 2026-06-03 and applied mutation signature Q157H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant Q157H His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:P32582 direct REST lookup on 2026-06-03 and applied mutation signature S82A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant S82A His-tagged


organism: Bacillus anthracis

substrate_name: L-homocysteine

sequence_variant_note: Resolved canonical sequence from Reconstructed A72S from UniProt A0A6L8PXK0 canonical sequence; A0A1J9VES8 is a secondary/merged accession and RCSB 5XW3 maps to A0A6L8PXK0. and applied mutation signature A72S to reconstruct the assayed variant sequence.

substrate: L-homocysteine


organism: Homo sapiens

substrate_name: L-Serine; L-Homocysteine

sequence_variant_note: Resolved canonical sequence from Reconstructed deltaN69 by deleting residues 1-69 from UniProt P35520 canonical human CBS sequence. and applied mutation signature ΔN69 with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

mutation_type: deletion

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant deltaN69

substrate: L-Serine; L-Homocysteine


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: cystathionine beta-synthase(Enzyme) mutant deltaN69/K119A

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant K119A


substrate_name: L-Cysteine

sequence_source: Canonical wild-type sequence from UniProt P35520 reviewed human cystathionine beta-synthase.

substrate: L-Cysteine


sequence_source: Reconstructed delta411-551 by retaining residues 1-410 from UniProt P35520 canonical human CBS sequence.

sequence_variant_note: Mutation signature Δ411 references residue 411, which is outside the resolved sequence length.

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant delta411-551


proof_lines: wild-type, 37°C, pH not specified in the publication


substrate_name: L-serine

sequence_variant_note: Resolved canonical sequence from Reconstructed S500L from UniProt P35520 canonical human CBS sequence. and applied mutation signature S500L to reconstruct the assayed variant sequence.

proof_lines: mutant S500L, 37°C, pH not specified in the publication

substrate: L-serine


sequence_variant_note: Resolved canonical sequence from Reconstructed D444N from UniProt P35520 canonical human CBS sequence. and applied mutation signature D444N to reconstruct the assayed variant sequence.

proof_lines: mutant D444N, 37°C, pH not specified in the publication


organism: Aeropyrum pernix

sequence_source: UniProtKB:Q9YBL2 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A6L8PXK0 canonical sequence queried via secondary accession A0A1J9VES8; variant reconstructed from source mutation_signature A72S and applied mutation signature A72S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A6L8PXK0 canonical sequence queried via secondary accession A0A1J9VES8; variant reconstructed from source mutation_signature E220R and applied mutation signature E220R to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A0A6L8PXK0 canonical sequence queried via secondary accession A0A1J9VES8

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

proof_lines: wild-type, production of H2S, pH 8.2, 37°C


sequence_source: UniProtKB:A0A6L8PXK0 canonical sequence queried via secondary accession A0A1J9VES8; variant reconstructed from source mutation_signature E220R


substrate_name: H2O; L-Cystathionine

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

proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant Q157E His-tagged

substrate: H2O; L-Cystathionine


proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant Q157A His-tagged


proof_lines: SABIO-RK modifier species: cystathionine beta-synthase(Enzyme) mutant T81A His-tagged


organism: Toxoplasma gondii

mutation_type: truncation

assay_conditions_summary: pH 9

proof_lines: cosubstrate L-serine, C-terminally truncated R353* CBS, pH 9, 37Â°C

proof_lines: cosubstrate O-acetyl-L-serine, C-terminally truncated R353* CBS, pH 9, 37Â°C


substrate_name: O-acetyl-L-serine

sequence_source: UniProtKB A0A125YSJ9 REST accession lookup on 2026-06-03

proof_lines: cosubstrate O-acetyl-L-serine, wild-type, pH 9, 37Â°C

proof_lines: cosubstrate L-serine, wild-type, pH 9, 37Â°C

substrate: O-acetyl-L-serine


organism: Trypanosoma cruzi

substrate_name: Sulfide; O-Acetyl-L-serine

substrate: Sulfide; O-Acetyl-L-serine


substrate_name: 2-Mercaptoethanol; L-Cysteine

substrate: 2-Mercaptoethanol; L-Cysteine


sequence_variant_note: Resolved canonical sequence from UniProtKB P35520 direct lookup on 2026-06-03 and applied mutation signature P427L to reconstruct the assayed variant sequence.

proof_lines: mutant P427L, 37°C, pH not specified in the publication


proof_lines: mutant K523Sfs?18, 37°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P35520 direct lookup on 2026-06-03 and applied mutation signature L540Q to reconstruct the assayed variant sequence.

proof_lines: mutant L540Q, 37°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P35520 direct lookup on 2026-06-03 and applied mutation signature V449G to reconstruct the assayed variant sequence.

proof_lines: mutant V449G, 37°C, pH not specified in the publication


sequence_source: UniProtKB P35520 direct lookup on 2026-06-03


sequence_variant_note: Resolved canonical sequence from UniProtKB P35520 direct lookup on 2026-06-03 and applied mutation signature H2S with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

proof_lines: cosubstrate H2S, presence of S-adenosyl-L-methionine, pH 7.4, 37°C


smiles: S


organism: Haemonchus contortus

substrate_name: L-Cys

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

substrate: L-Cys


proof_lines: pH 6.8, 37°C, deltaC143 mutant after homocysteine pre-treatment

proof_lines: pH 6.8, 37°C, deltaC143 mutant after L-serine pre-treatment


proof_lines: I435T mutant, 37°C, presence of S-adenosyl-L-methionine

proof_lines: I435T mutant, 37°C, absence of S-adenosyl-L-methionine


substrate_name: homocysteine

proof_lines: S466L mutant, 37°C, absence of S-adenosyl-L-methionine

proof_lines: mutant enzyme S466L, in the presence of 0.25 mM S-adenosyl-L-methionine

substrate: homocysteine


substrate_name: L-cysteine

proof_lines: pH 8.0, 37°C, reaction with cysteamine, continous UV assay

proof_lines: pH 6.8, 37°C, full length enzyme after L-serine pre-treatment

substrate: L-cysteine


substrate_name: L-cystathionine

proof_lines: reverse reaction (L-cystathionine hydrolysis), mutant S289A

proof_lines: cosubstrate: L-homocysteine, mutant S289A

substrate: L-cystathionine


proof_lines:
37°C, pH 8.6, mutant enzyme R266K
mutant R266K


proof_lines: 37°C, pH 8.0, wild-type enzyme, without S-adenosyl-L-methionine

proof_lines: 37°C, pH 8.0, wild-type enzyme, with S-adenosyl-L-methionine


organism: Panagrellus redivivus


substrate_name: DL-homocysteine

proof_lines:
cosubstrate L-Ser
cosubstrate L-Cys
enzyme composed of MW 48000 subunits

substrate: DL-homocysteine


proof_lines:
pH 8.6, 37°C
37°C, homocysteine pre-treatment
37°C


proof_lines: presence of S-adenosyl-L-methionine, pH 8.6, 37°C

proof_lines: cosubstrate L-serine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C


organism: Lactiplantibacillus plantarum


sequence_variant_note: Resolved canonical sequence from UniProtKB:F9UT54 plus reviewed mutation signature E223G and applied mutation signature E223G to reconstruct the assayed variant sequence.


proof_lines: formation of (2R,2R)-3,3-sulfanediylbis(2-aminopropanoic acid), wild-type, pH 7.5, 37°C

proof_lines: formation of L-cystathionine, wild-type, pH 7.5, 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:F9UT54 plus reviewed mutation signature A70S and applied mutation signature A70S to reconstruct the assayed variant sequence.

proof_lines: formation of L-cystathionine, mutant A70S, pH 7.5, 37°C


sequence_source: UniProtKB:F9UT54 plus reviewed mutation signature E223G

proof_lines: formation of L-cystathionine, mutant E223G, pH 7.5, 37°C

proof_lines: formation of (2R,2R)-3,3-sulfanediylbis(2-aminopropanoic acid), mutant E223G, pH 7.5, 37°C


sequence_source: UniProtKB:F9UT54 plus reviewed mutation signature A70S


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


proof_lines:
wild-type enzyme, pH 8.6, 37°C
cosubstrate: L-homocysteine, wild-type
cosubstrate: L-serine, wild-type


enzyme_display_name: 3-mercaptopyruvate sulfurtransferase

organism: Arabidopsis thaliana

substrate_name: thiosulfate

source_db: uniprot

enzyme: 3-mercaptopyruvate sulfurtransferase

substrate: thiosulfate

source: uniprot


substrate_name: 2-Mercaptoethanol; 3-Mercaptopyruvate

sequence_source: UniProtKB:P97532 direct REST lookup

sequence_variant_note: Resolved canonical sequence from UniProtKB:P97532 direct REST lookup and applied mutation signature R187G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-mercaptopyruvate sulfurtransferase(Enzyme) mutant R187G

substrate: 2-Mercaptoethanol; 3-Mercaptopyruvate


smiles: O=C(O)C(=O)CS


sequence_variant_note: Resolved canonical sequence from UniProtKB:P97532 direct REST lookup and applied mutation signature S249A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P97532 direct REST lookup and applied mutation signature R196G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-mercaptopyruvate sulfurtransferase(Enzyme) mutant R196G


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

sequence_source: UniProtKB:P25325 canonical FASTA, direct REST lookup

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

proof_lines: isoform TUM1-Iso1, with cyanide as cosubstrate, at pH 10.5 and 37°C

proof_lines: isoform TUM1-Iso2, with cyanide as cosubstrate, at pH 10.5 and 37°C

source_databases_merged: brenda skid


substrate_name: dithiothreitol

substrate: dithiothreitol


substrate_name: cyanide

smiles: C#N

substrate: cyanide


substrate_name: L-homocysteine

substrate: L-homocysteine


substrate_name: dihydrolipoic acid

smiles: O=C(O)CCCCC(S)CCS

substrate: dihydrolipoic acid


smiles: OCCS


proof_lines: mitochondrial splice variant MPST2, Hill coefficient 1.4, pH 7.4, 37°C

proof_lines: cytosolic splice variant MPST1, Hill coefficient 1.6, pH 7.4, 37°C

proof_lines: cytosolic splice variant MPST1, Hill coefficient 1.4, pH 7.4, 37°C


substrate_name: N-acetyl-L-cysteine

substrate: N-acetyl-L-cysteine


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 H66A, enzyme displays kinetic cooperativity with respect to 3-mercaptopyruvate and thioredoxin, pH 8.0, 30°C


proof_lines: mutant S239A, enzyme displays kinetic cooperativity with respect to 3-mercaptopyruvate and thioredoxin, pH 8.0, 30°C


proof_lines: wild-type, enzyme displays kinetic cooperativity with respect to 3-mercaptopyruvate and thioredoxin, pH 8.0, 30°C


organism: Leishmania major

substrate_name: reduced thioredoxin

proof_lines:
pH 7.3, 37°C
Raw SKiD Env: Temp=37°C, pH=7.3

substrate: reduced thioredoxin


organism: Mycobacterium tuberculosis


proof_lines: SABIO-RK modifier species: 3-mercaptopyruvate sulfurtransferase(Enzyme) mutant R248G


sequence_source: UniProtKB reviewed accession P24329


substrate_name: 3-Mercaptopyruvate; 2-Mercaptoethanol

proof_lines: SABIO-RK modifier species: 3-mercaptopyruvate sulfurtransferase(Enzyme) mutant R248G K249S

substrate: 3-Mercaptopyruvate; 2-Mercaptoethanol


proof_lines: SABIO-RK modifier species: 3-mercaptopyruvate sulfurtransferase(Enzyme) mutant K249S


sequence_source: UniProtKB reviewed accession P97532


sequence_source: UniProtKB reviewed accession P97532 FASTA, checked directly during review.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P97532 FASTA plus selected source mutation signature reconstructed against PubMed 8910318 numbering. and applied mutation signature G248R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-mercaptopyruvate sulfurtransferase(Enzyme) mutant G248R


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P97532 FASTA plus selected source mutation signature reconstructed against PubMed 8910318 numbering. and applied mutation signature S249K with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P97532 FASTA plus selected source mutation signature reconstructed against PubMed 8910318 numbering. and applied mutation signature R196G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P97532 FASTA plus selected source mutation signature reconstructed against PubMed 8910318 numbering. and applied mutation signature S249A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-mercaptopyruvate sulfurtransferase(Enzyme) mutant S249A


sequence_source: UniProtKB reviewed accession P97532 FASTA plus selected source mutation signature reconstructed against PubMed 8910318 numbering.

proof_lines: SABIO-RK modifier species: 3-mercaptopyruvate sulfurtransferase(Enzyme) mutant S249K


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


organism: Escherichia coli

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


organism: Bos taurus


proof_lines: in the presence of cyanide, pH 9.55, 37°C

proof_lines: determination of thiocyanate formation, 37°C, pH 9.55

proof_lines: determination of pyruvate formation, 37°C, pH 9.55


substrate_name: Cyanide; 3-Mercaptopyruvate

sequence_source: UniProtKB direct accession lookup for Q24JL3; local identity cache accession_cd83b777468f62a6

proof_lines:
MST2, 30°C
MST1, 30°C

substrate: Cyanide; 3-Mercaptopyruvate


sequence_source: UniProtKB direct accession lookup for O64530; local identity cache accession_30cc534ada40592e


substrate_name: 3-Mercaptopyruvate; Cyanide

substrate: 3-Mercaptopyruvate; Cyanide


substrate_name: glutathione

sequence_source: UniProtKB direct accession lookup for P25325; local identity cache accession_2a6c67f5ccf0d4d7 provided identity context only

substrate: glutathione


organism: Rana temporaria

proof_lines:
mitochondrial enzyme
cytosolic enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P97532 FASTA plus selected source mutation signature reconstructed against PubMed 8910318 numbering. and applied mutation signature R187G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines:
R187G mutant
pH 9.7, 25°C, mutant R187G


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P97532 FASTA plus selected source mutation signature reconstructed against PubMed 8910318 numbering. and applied mutation signature S249A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P97532 FASTA, supported by PubMed 8910318 rat liver MST sequence context.

proof_lines:
wild-type enzyme
pH 9.7, 25°C, wild-type


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P97532 FASTA plus selected source mutation signature reconstructed against PubMed 8910318 numbering. and applied mutation signature S249K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


proof_lines:
R196G mutant
pH 9.7, 25°C, mutant R196G


organism: Trichomonas vaginalis

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


enzyme_display_name: prolyl aminopeptidase

organism: Serratia marcescens

sequence_source: UniProtKB reviewed accession O32449

enzyme: prolyl aminopeptidase


organism: Phanerodontia chrysosporium

substrate_name: Pro-beta-naphthylamide

sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 direct REST/FASTA lookup; variant rows reconstructed from the C6KI04 canonical sequence and selected mutation signature. and applied mutation signature E198Q to reconstruct the assayed variant sequence.

substrate: Pro-beta-naphthylamide


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 direct REST/FASTA lookup; variant rows reconstructed from the C6KI04 canonical sequence and selected mutation signature. and applied mutation signature F133A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 direct REST/FASTA lookup; variant rows reconstructed from the C6KI04 canonical sequence and selected mutation signature. and applied mutation signature E227A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 direct REST/FASTA lookup; variant rows reconstructed from the C6KI04 canonical sequence and selected mutation signature. and applied mutation signature F231A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 direct REST/FASTA lookup; variant rows reconstructed from the C6KI04 canonical sequence and selected mutation signature. and applied mutation signature C267A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB C6KI04 direct REST/FASTA lookup; variant rows reconstructed from the C6KI04 canonical sequence and selected mutation signature.


proof_lines: pH 8.0, 45°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 canonical sequence; reconstructed substitution E227A and applied mutation signature E227A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 canonical sequence; reconstructed substitution F223A and applied mutation signature F223A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 canonical sequence; reconstructed substitution C267A and applied mutation signature C267A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 canonical sequence; reconstructed substitution F231A and applied mutation signature F231A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 canonical sequence; reconstructed substitution F143A and applied mutation signature F143A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB C6KI04 canonical sequence; reconstructed substitution F223A


sequence_source: UniProtKB C6KI04 canonical sequence; reconstructed substitution F143A


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 canonical sequence; reconstructed substitution E198A and applied mutation signature E198A to reconstruct the assayed variant sequence.


substrate_name: L-leucine-p-nitroanilide

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

substrate: L-leucine-p-nitroanilide


organism: Heyndrickxia coagulans

substrate_name: Pro-Ala

substrate: Pro-Ala


organism: Lactobacillus delbrueckii subsp. bulgaricus

substrate_name: prolyl-pNA (at 30 degrees Celsius and pH 7.0)

assay_conditions_summary: pH 7


organism: Lactobacillus helveticus

substrate_name: Pro-pNA (at 40 degrees Celsius and pH 7.5)


organism: Rattus norvegicus

substrate_name: Unknown

substrate: Unknown


organism: Solanum lycopersicum


organism: Aspergillus oryzae

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

proof_lines: 50°C, pH 7.5, mutant enzyme V147A/C185V/Y393W/K415R


sequence_source: UniProtKB:W8GG09 direct accession lookup


sequence_source: UniProtKB:Q890D8 direct accession lookup


substrate_name: H2O; Prolyl-p-nitroanilide

sequence_source: UniProtKB:P46544 direct accession lookup; identity reuse cache source_record sequence

substrate: H2O; Prolyl-p-nitroanilide


substrate_name: Prolyl-p-nitroanilide; H2O

sequence_source: UniProtKB:P52278 direct accession lookup; identity reuse cache source_record sequence

substrate: Prolyl-p-nitroanilide; H2O


sequence_source: UniProtKB:C6KI04 direct accession lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB C6KI04 direct lookup; variant reconstructed from canonical sequence and applied mutation signature E198A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB C6KI04 direct lookup


organism: Rasamsonia emersonii

sequence_source: UniProtKB Q8X1C7 direct lookup


organism: Secale cereale x Triticum turgidum subsp. durum

substrate_name: Ala-beta-naphthylamide

sequence_source: UniProtKB G9J616 direct lookup

substrate: Ala-beta-naphthylamide


sequence_variant_note: Resolved canonical sequence from UniProtKB O32449 direct lookup; variant reconstructed from canonical sequence and applied mutation signature Y149A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O32449 direct lookup; variant reconstructed from canonical sequence and applied mutation signature C271A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O32449 direct lookup; variant reconstructed from canonical sequence and applied mutation signature F236A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O32449 direct lookup; variant reconstructed from canonical sequence and applied mutation signature F139A to reconstruct the assayed variant sequence.

proof_lines:
F139A mutant enzyme
Pro-bNA, F139A mutant enzyme


organism: Aspergillus niger

sequence_source: UniProtKB:Q96VT2 direct REST lookup


sequence_source: UniProtKB:C6L823 direct REST lookup


sequence_source: UniProtKB:W8GG09 direct REST lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:W8GG09 direct REST lookup plus explicit C185V reconstruction and applied mutation signature C185V to reconstruct the assayed variant sequence.


proof_lines: 50°C, pH 7.5, mutant enzyme V147A/C185V/K415R


proof_lines: 50°C, pH 7.5, mutant enzyme V147A/Y393W/K415R


substrate_name: Cys-Gly (at pH 6.9 and 25 degrees Celsius)

proof_lines: kcat is 3400 min(-1) for Cys-Gly hydrolysis activity (at pH 6.9 and 25 degrees Celsius). kcat is 11500 min(-1) for Leu-Gly hydrolysis activity (at pH 6.9 and 25 degrees Celsius). kcat is 8150 min(-1) for Met-Gly hydrolysis activity (at pH 6


substrate_name: Leu-Gly

proof_lines: kcat is 120 sec(-1) with Leu-Gly as substrate.

substrate: Leu-Gly


organism: Aneurinibacillus sp.

substrate_name: Pro-para-nitroanilide

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

substrate: Pro-para-nitroanilide


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


organism: Debaryomyces hansenii


organism: Grifola frondosa

substrate_name: Ala-p-nitroanilide

substrate: Ala-p-nitroanilide


organism: Lyophyllum cinerascens


organism: Penicillium camemberti

substrate_name: Pro-p-nitroanilide

substrate: Pro-p-nitroanilide


substrate_name: proline beta-naphthylamide

sequence_source: UniProtKB reviewed O32449/PIP_SERMA, literature-linked to PMID 11011150

substrate: proline beta-naphthylamide


organism: Streptomyces plicatus


organism: Triticum aestivum


organism: Priestia megaterium

substrate_name: Pro-Asp

substrate: Pro-Asp


organism: Prunus armeniaca


organism: Serratia marcescens

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O32449 (PIP_SERMA), reconstructed F139A from the canonical sequence and applied mutation signature F139A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O32449 (PIP_SERMA), reconstructed R136A from the canonical sequence and applied mutation signature R136A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O32449 (PIP_SERMA), reconstructed E204Q from the canonical sequence and applied mutation signature E204Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed O32449 (PIP_SERMA), reconstructed Y149A from the canonical sequence and applied mutation signature Y149A to reconstruct the assayed variant sequence.


enzyme_display_name: oleate hydratase

organism: Elizabethkingia meningoseptica

substrate_name: Oleate; 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

sequence_source: UniProtKB reviewed entry C7DLJ6 / OLHYD_ELIME direct lookup; canonical protein sequence, EC 4.2.1.53, Elizabethkingia meningoseptica.

assay_conditions_summary: pH 8; 303.15 K; buffer 20 mM Tris

proof_lines: at 30°C, in 20 mM Tris buffer, pH 8, 50 mM NaCl, with mixing speed of 1400 rpm

proof_lines: at 30°C, in 20 mM Tris buffer, pH 8, 50 mM NaCl, with mixing speed of 1000 rpm

proof_lines: at 22°C, in 20 mM Tris buffer, pH 8, 50 mM NaCl, with mixing speed of 2200 rpm, in the presence of 2.5% isopropyl alcoho

source_databases_merged: sabio_rk brenda skid

enzyme: oleate hydratase

substrate: Oleate; H2O


organism: Macrococcoides caseolyticum

substrate_name: palmitoleic acid

sequence_source: UniProtKB reviewed entry B9E972 / OLHYD_MACCJ direct lookup; canonical protein sequence, EC 4.2.1.53, Macrococcus caseolyticus strain JCSC5402 with Macrococcoides lineage context.

substrate: palmitoleic acid


organism: Macrococcus caseolyticus

substrate_name: gamma-linolenic acid

sequence_source: UniProtKB reviewed entry B9E972 / OLHYD_MACCJ direct lookup; canonical protein sequence, EC 4.2.1.53, Macrococcus caseolyticus strain JCSC5402.

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

substrate: gamma-linolenic acid


substrate_name: alpha-linolenic acid

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

substrate: alpha-linolenic acid


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


substrate_name: myristoleic acid

smiles: CCCCC=CCCCCCCCC(=O)O

substrate: myristoleic acid


substrate_name: oleic acid

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

substrate: oleic acid


substrate_name: linoleic acid

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

substrate: linoleic acid


organism: Lysinibacillus fusiformis

substrate_name: gamma-linolenate

substrate: gamma-linolenate


organism: Stenotrophomonas maltophilia

substrate_name: oleate

substrate: oleate


substrate_name: oleate (at 30 degrees Celsius)

assay_conditions_summary: buffer Tris; cofactor FAD

proof_lines: kcat is 1.2 sec(-1). kcat is 2.6 sec(-1) with OhyA harboring two-electron-reduced FAD (PubMed:26077980). Due to the low solubility of oleate in Tris buffer, the values given in PubMed:19465645 are approximate, the real Vmax is most likely s

substrate: oleate (at 30 degrees Celsius)


organism: Macrococcus caseolyticus (strain JCSC5402)

proof_lines: kcat is 470 min(-1) with oleate as substrate. The catalytic efficiency with oleate as substrate is 3.5-fold higher than that with palmitoleate, the second favored substrate.


organism: Streptococcus pyogenes serotype M49 (strain NZ131)

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

proof_lines: kcat is 67 min(-1) and 101 min(-1) with oleate and linoleate as substrate, respectively.


organism: Paracoccus aminophilus

sequence_source: UniProtKB REST/FASTA direct lookup for S5Y0Y3


organism: Rhodococcus erythropolis

smiles: CCCCCCCC/C=C\CCCCCCCC(=O)[O-]


organism: Staphylococcus aureus

proof_lines: K0.5 value, Hill coefficient 2.2, pH 6.0, 37°C


enzyme_display_name: 4-hydroxy-2-oxovalerate aldolase

organism: Thermus thermophilus

normalized_value_unit_evidence: kcat: printed cell 0.08 s–1 -> 0.08 s^(-1); the catalog holds 0.08 s^(-1); no unit conversion applied. Km,app: printed cell 95 μM -> 0.095 mM (1 μM = 0.001 mM); the catalog holds 0.095 mM. kcat/Km,app: The paper PRINTS this row's efficiency cell `0.08` in the `kcat/Km,app(×104 M–1 s–1)` column, i.e. 0.08 x10^4 M^-1 s^-1 = 0.8 s^-1 mM^-1. The catalog stores 0.8421052631578947 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km (0.08 / 0.095) rather than a transcription of the printed cell; the two differ. The nested oed source snapshot for this row already carries the printed value 0.8 s^(-1)*mM^(-1).

row_label: Table 2, decoded transcription, metal-ion row `Ca2+`

table_label: Table 2 'Relative Activities of TTHB246 with Various Divalent Metal Ions' (asset `tables[1]`)

enzyme: 4-hydroxy-2-oxovalerate aldolase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 0.38 sec(-1) with 4-hydroxy-2-oxohexanoate as substrate. kcat is 0.41 sec(-1) with 4-hydroxy-2-oxopentanoate as substrate.


organism: Paraburkholderia xenovorans (strain LB400)

substrate_name: (4S)-4-hydroxy-2-oxopentanoate (in the presence of NADH at pH 8 and 25 degrees Celsius)

proof_lines: The catalytic efficiency is similar when using 4-hydroxy-2-oxopentanoate or 4-hydroxy-2-oxohexanoate as substrate, but is 10-fold lower with 4-hydroxy-2-oxoheptanoate. It is also 25-fold higher when NADH is present than the value obtained w


organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: 4-hydroxy-2-oxopentanoate (in the presence of NADH at pH 8 and 25 degrees Celsius)

proof_lines: The catalytic efficiency is similar when using 4-hydroxy-2-oxopentanoate or 4-hydroxy-2-oxohexanoate as substrate. In the presence of NADH, exhibits a 2-fold increase in kcat.


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


sequence_source: UniProtKB:Q53WI0 direct accession lookup; identity reuse cache accession_234a19ae7aa140a9


normalized_value_unit_evidence: kcat: printed cell 0.57 s–1 -> 0.57 s^(-1); the catalog holds 0.57 s^(-1); no unit conversion applied. Km,app: printed cell 45 μM -> 0.045 mM (1 μM = 0.001 mM); the catalog holds 0.045 mM. kcat/Km,app: The paper PRINTS this row's efficiency cell `1.3` in the `kcat/Km,app(×104 M–1 s–1)` column, i.e. 1.3 x10^4 M^-1 s^-1 = 13.0 s^-1 mM^-1. The catalog stores 12.666666666666666 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km (0.57 / 0.045) rather than a transcription of the printed cell; the two differ. The nested oed source snapshot for this row already carries the printed value 13.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded transcription, metal-ion row `Mn2+`


normalized_value_unit_evidence: kcat: printed cell 0.13 s–1 -> 0.13 s^(-1); the catalog holds 0.13 s^(-1); no unit conversion applied. Km,app: printed cell 80 μM -> 0.08 mM (1 μM = 0.001 mM); the catalog holds 0.08 mM. kcat/Km,app: The paper PRINTS this row's efficiency cell `0.16` in the `kcat/Km,app(×104 M–1 s–1)` column, i.e. 0.16 x10^4 M^-1 s^-1 = 1.6 s^-1 mM^-1. The catalog stores 1.625 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km (0.13 / 0.08) rather than a transcription of the printed cell; the two differ. The nested oed source snapshot for this row already carries the printed value 1.6 s^(-1)*mM^(-1).

row_label: Table 2, decoded transcription, metal-ion row `Mg2+`


normalized_value_unit_evidence: kcat: printed cell 1.0 s–1 -> 1.0 s^(-1); the catalog holds 1.0 s^(-1); no unit conversion applied. Km,app: printed cell 55 μM -> 0.055 mM (1 μM = 0.001 mM); the catalog holds 0.055 mM. kcat/Km,app: The paper PRINTS this row's efficiency cell `1.9` in the `kcat/Km,app(×104 M–1 s–1)` column, i.e. 1.9 x10^4 M^-1 s^-1 = 19.0 s^-1 mM^-1. The catalog stores 18.181818181818183 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km (1.0 / 0.055) rather than a transcription of the printed cell; the two differ. The nested oed source snapshot for this row already carries the printed value 19.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded transcription, metal-ion row `Co2+`


organism: Burkholderia xenovorans


organism: Burkholderia xenovorans LB400

unit: Mswedgeone


substrate_name: glycolaldehyde

smiles: O=CCO

assay_conditions_summary: pH 8; 298.15 K; buffer 100 mM HEPES

column_label: Table 2 (Aldehyde Specificity of HpaI and BphI in the Aldol Addition Reaction), pyruvate as carbonyl donor block, aldehyde row 'glycolaldehyde', BphI column group; column 'Km,app (mM)' = 124.6; column 'kcat,app (s-1)' = 0.40; column '(kcat/Km)app (M-1 s-1)' = 3.7.

normalized_value_unit_evidence: Km: printed cell 124.6 mM; the printed column head is Km,app (mM), so no unit conversion applies and the paper value is 124.6 mM. kcat: printed cell 0.40 s^-1; the printed column head is kcat,app (s-1), so no unit conversion applies and the paper value is 0.4 s^(-1), this article printing no min^-1 kinetic cell. kcat/Km: printed cell 3.7 M^-1 s^-1 under the printed column head (kcat/Km)app (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.7 / 1000 = 0.0037 s^-1 mM^-1. Quotient disclosure for this cell group: 0.40 / 124.6 = 0.003210272873194222 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, pyruvate as carbonyl donor block, aldehyde row 'glycolaldehyde', BphI column group: Km,app = 124.6 mM; kcat,app = 0.40 s^-1; printed (kcat/Km)app = 3.7 M^-1 s^-1.

row_label: Table 2, pyruvate as carbonyl donor block, glycolaldehyde row, BphI column group

table_label: Table 2: Aldehyde Specificity of HpaI and BphI in the Aldol Addition Reaction (Biochemistry 2010, 49, 3774-3782); the HpaI column group prints Km,app (mM), kcat,app (s-1) and (kcat/Km)app in (10^3 M-1 s-1) and the BphI column group prints Km,app (mM), kcat,app (s-1) and (kcat/Km)app in (M-1 s-1)

substrate: glycolaldehyde


ki_unit: mM


organism: Paraburkholderia xenovorans

substrate_name: Butyraldehyde

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P51015 (HOA4_PARXL); variant sequence reconstructed by direct coordinate substitution when mutation_signature is present and applied mutation signature L87A to reconstruct the assayed variant sequence.

proof_lines: aldol addition reaction with propionaldehyde, L87A mutant protein, pH 8.0, 25°C

substrate: Butyraldehyde


substrate_name: pyruvate

sequence_source: UniProtKB reviewed P51015 (HOA4_PARXL); variant sequence reconstructed by direct coordinate substitution when mutation_signature is present

proof_lines: aldol addition reaction with propionaldehyde, wild type protein, pH 8.0, 25°C

substrate: pyruvate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P51015 (HOA4_PARXL); variant sequence reconstructed by direct coordinate substitution when mutation_signature is present and applied mutation signature L87A/L89A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P51015 (HOA4_PARXL); variant sequence reconstructed by direct coordinate substitution when mutation_signature is present and applied mutation signature R16K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P51015 (HOA4_PARXL); variant sequence reconstructed by direct coordinate substitution when mutation_signature is present and applied mutation signature Y290F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P51015 (HOA4_PARXL); variant sequence reconstructed by direct coordinate substitution when mutation_signature is present and applied mutation signature Y290S to reconstruct the assayed variant sequence.


organism: Escherichia coli

substrate_name: (R,S)-glyceraldehyde

smiles: O=CC(O)CO

substrate: (R,S)-glyceraldehyde


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


organism: Mycobacterium tuberculosis

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

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

proof_lines: in 100 mM HEPES (pH 8.0), 1 mM MgCl2, at 25°C

proof_lines: in 100 mM HEPES (pH 8.0), 0.4 mM NADH, 1 mM MgCl2, at 25°C


organism: Paraburkholderia xenovorans LB400

assay_conditions_summary: pH 8; 298.15 K; buffer 100 mM HEPES; cofactor NADH

proof_lines: at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate

proof_lines: in the presence of 0.4 mM NADH, 2 mM Mn2+, 20 units of ADH in 100 mM HEPES buffer, pH 8.0 at 25°C, in a total volume of 1 ml


normalized_value_unit_evidence: kcat: printed cell 0.79 s–1 -> 0.79 s^(-1); the catalog holds 0.79 s^(-1); no unit conversion applied. Km,app: printed cell 74 μM -> 0.074 mM (1 μM = 0.001 mM); the catalog holds 0.074 mM. kcat/Km,app: The paper PRINTS this row's efficiency cell `1.1` in the `kcat/Km,app(×104 M–1 s–1)` column, i.e. 1.1 x10^4 M^-1 s^-1 = 11.0 s^-1 mM^-1. The catalog stores 10.675675675675677 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km (0.79 / 0.074) rather than a transcription of the printed cell; the two differ. The nested oed source snapshot for this row already carries the printed value 11.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded transcription, metal-ion row `Ni2+`


substrate_name: propanal

column_label: Table 2 (Aldehyde Specificity of HpaI and BphI in the Aldol Addition Reaction), pyruvate as carbonyl donor block, aldehyde row 'propionaldehyde', BphI column group; column 'Km,app (mM)' = 135.9; column 'kcat,app (s-1)' = 1.79; column '(kcat/Km)app (M-1 s-1)' = 13.2.

normalized_value_unit_evidence: Km: printed cell 135.9 mM; the printed column head is Km,app (mM), so no unit conversion applies and the paper value is 135.9 mM. kcat: printed cell 1.79 s^-1; the printed column head is kcat,app (s-1), so no unit conversion applies and the paper value is 1.79 s^(-1), this article printing no min^-1 kinetic cell. kcat/Km: printed cell 13.2 M^-1 s^-1 under the printed column head (kcat/Km)app (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 13.2 / 1000 = 0.0132 s^-1 mM^-1. Quotient disclosure for this cell group: 1.79 / 135.9 = 0.013171449595290655 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, pyruvate as carbonyl donor block, aldehyde row 'propionaldehyde', BphI column group: Km,app = 135.9 mM; kcat,app = 1.79 s^-1; printed (kcat/Km)app = 13.2 M^-1 s^-1.

row_label: Table 2, pyruvate as carbonyl donor block, propionaldehyde row, BphI column group

substrate: propanal


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

column_label: Table 3 (Steady-State Kinetic Parameters of HpaI and BphI for the Aldol Addition Reaction), enzyme row 'BphI'; column 'kcat (s-1)' = 1.04; column 'KmA (mM)' = 14.8, the Michaelis constant of pyruvate (substrate A); Table 3 prints no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 1.04 s^-1; the printed column head is kcat (s-1), so no unit conversion applies and the paper value is 1.04 s^(-1), this article printing no min^-1 kinetic cell. Km: printed cell 14.8 mM; the printed column head is KmA (mM), so no unit conversion applies and the paper value is 14.8 mM. kcat/Km: this article prints no kcat/Km cell for this measurement, so the exported 0.07027027027027027 s^(-1)*mM^(-1) is not a printed value; it is the quotient 1.04 / 14.8 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'BphI': kcat = 1.04 s^-1; KmA = 14.8 mM, the Michaelis constant of pyruvate (substrate A). No kcat/Km value is printed for this measurement.

row_label: Table 3, BphI row, pyruvate (substrate A) axis

table_label: Table 3: Steady-State Kinetic Parameters of HpaI and BphI for the Aldol Addition Reaction (Biochemistry 2010, 49, 3774-3782); printed columns kcat (s-1), KiA (mM), KmA (mM) and KmB (mM), with pyruvate as substrate A and acetaldehyde as substrate B


substrate_name: Acetaldehyde

smiles: CC=O

column_label: Table 3 (Steady-State Kinetic Parameters of HpaI and BphI for the Aldol Addition Reaction), enzyme row 'BphI'; column 'kcat (s-1)' = 1.04; column 'KmB (mM)' = 67.0, the Michaelis constant of acetaldehyde (substrate B); Table 3 prints no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 1.04 s^-1; the printed column head is kcat (s-1), so no unit conversion applies and the paper value is 1.04 s^(-1), this article printing no min^-1 kinetic cell. Km: printed cell 67.0 mM; the printed column head is KmB (mM), so no unit conversion applies and the paper value is 67.0 mM. kcat/Km: this article prints no kcat/Km cell for this measurement, so the exported 0.015522388059701494 s^(-1)*mM^(-1) is not a printed value; it is the quotient 1.04 / 67.0 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'BphI': kcat = 1.04 s^-1; KmB = 67.0 mM, the Michaelis constant of acetaldehyde (substrate B). No kcat/Km value is printed for this measurement.

row_label: Table 3, BphI row, acetaldehyde (substrate B) axis

substrate: Acetaldehyde


substrate_name: acetaldehyde

column_label: Table 2 (Aldehyde Specificity of HpaI and BphI in the Aldol Addition Reaction), pyruvate as carbonyl donor block, aldehyde row 'acetaldehyde', HpaI column group; column 'Km,app (mM)' = 62.9; column 'kcat,app (s-1)' = 205.4; column '(kcat/Km)app (10^3 M-1 s-1)' = 3.3.

normalized_value_unit_evidence: Km: printed cell 62.9 mM; the printed column head is Km,app (mM), so no unit conversion applies and the paper value is 62.9 mM. kcat: printed cell 205.4 s^-1; the printed column head is kcat,app (s-1), so no unit conversion applies and the paper value is 205.4 s^(-1), this article printing no min^-1 kinetic cell. kcat/Km: printed cell 3.3 x 10^3 M^-1 s^-1 under the printed column head (kcat/Km)app (10^3 M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3300.0 / 1000 = 3.3 s^-1 mM^-1. Quotient disclosure for this cell group: 205.4 / 62.9 = 3.2655007949125596 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, pyruvate as carbonyl donor block, aldehyde row 'acetaldehyde', HpaI column group: Km,app = 62.9 mM; kcat,app = 205.4 s^-1; printed (kcat/Km)app = 3.3 x 10^3 M^-1 s^-1.

row_label: Table 2, pyruvate as carbonyl donor block, acetaldehyde row, HpaI column group

substrate: acetaldehyde


smiles: CCCC=O

column_label: Table 2 (Aldehyde Specificity of HpaI and BphI in the Aldol Addition Reaction), pyruvate as carbonyl donor block, aldehyde row 'butyraldehyde', HpaI column group; column 'Km,app (mM)' = 13.4; column 'kcat,app (s-1)' = 132.5; column '(kcat/Km)app (10^3 M-1 s-1)' = 9.9.

normalized_value_unit_evidence: Km: printed cell 13.4 mM; the printed column head is Km,app (mM), so no unit conversion applies and the paper value is 13.4 mM. kcat: printed cell 132.5 s^-1; the printed column head is kcat,app (s-1), so no unit conversion applies and the paper value is 132.5 s^(-1), this article printing no min^-1 kinetic cell. kcat/Km: printed cell 9.9 x 10^3 M^-1 s^-1 under the printed column head (kcat/Km)app (10^3 M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9900.0 / 1000 = 9.9 s^-1 mM^-1. Quotient disclosure for this cell group: 132.5 / 13.4 = 9.888059701492537 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, pyruvate as carbonyl donor block, aldehyde row 'butyraldehyde', HpaI column group: Km,app = 13.4 mM; kcat,app = 132.5 s^-1; printed (kcat/Km)app = 9.9 x 10^3 M^-1 s^-1.

row_label: Table 2, pyruvate as carbonyl donor block, butyraldehyde row, HpaI column group


column_label: Table 2 (Aldehyde Specificity of HpaI and BphI in the Aldol Addition Reaction), pyruvate as carbonyl donor block, aldehyde row 'glycolaldehyde', HpaI column group; column 'Km,app (mM)' = 33.3; column 'kcat,app (s-1)' = 175.5; column '(kcat/Km)app (10^3 M-1 s-1)' = 5.27.

normalized_value_unit_evidence: Km: printed cell 33.3 mM; the printed column head is Km,app (mM), so no unit conversion applies and the paper value is 33.3 mM. kcat: printed cell 175.5 s^-1; the printed column head is kcat,app (s-1), so no unit conversion applies and the paper value is 175.5 s^(-1), this article printing no min^-1 kinetic cell. kcat/Km: printed cell 5.27 x 10^3 M^-1 s^-1 under the printed column head (kcat/Km)app (10^3 M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5270.0 / 1000 = 5.27 s^-1 mM^-1. Quotient disclosure for this cell group: 175.5 / 33.3 = 5.270270270270271 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, pyruvate as carbonyl donor block, aldehyde row 'glycolaldehyde', HpaI column group: Km,app = 33.3 mM; kcat,app = 175.5 s^-1; printed (kcat/Km)app = 5.27 x 10^3 M^-1 s^-1.

row_label: Table 2, pyruvate as carbonyl donor block, glycolaldehyde row, HpaI column group


substrate_name: Succinic semialdehyde

smiles: O=CCCC(=O)O

substrate: Succinic semialdehyde


sequence_variant_note: Resolved canonical sequence from UniProtKB P51015 canonical sequence with direct L89A reconstruction and applied mutation signature L89A to reconstruct the assayed variant sequence.

proof_lines: aldol addition reaction with propionaldehyde, L89A mutant protein, pH 8.0, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P51015 canonical sequence with direct H20A reconstruction and applied mutation signature H20A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P51015 canonical sequence with direct H20S reconstruction and applied mutation signature H20S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P51015 canonical sequence used as BphI identity context

proof_lines: in the absence of NADH, in 100 mM HEPES pH 8.0, at 25°C

proof_lines: in the presence of NADH, in 100 mM HEPES pH 8.0, at 25°C


enzyme_display_name: aminopeptidase B

organism: Caenorhabditis elegans

substrate_name: L-Lys-pNitroaniline

proof_lines: No activity with L-Asp-pNA, L-Glu-pNA or D-Leu-pNA.

enzyme: aminopeptidase B

substrate: L-Lys-pNitroaniline


organism: Bacillus subtilis (strain 168)

substrate_name: Arg-pNA

substrate: Arg-pNA


organism: Aspergillus niger


organism: Bos taurus

substrate_name: L-Lys-p-nitroanilide

substrate: L-Lys-p-nitroanilide


organism: Capra aegagrus

proof_lines:
free enzyme
immobilized enzyme


organism: Colwellia psychrerythraea


substrate_name: Cys-Gly

substrate: Cys-Gly


organism: Homo sapiens

substrate_name: L-Arg-beta-naphthylamide

proof_lines:
enzyme I
enzyme II

substrate: L-Arg-beta-naphthylamide


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F297Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y414F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y409F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y409F/Y414F to reconstruct the assayed variant sequence.


organism: Streptococcus gordonii

substrate_name: H2O; Arginine-4-nitroanilide / Arg-4-nitroanilide

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


organism: Bacillus subtilis

sequence_source: UniProtKB REST exact accession lookup: P25152


sequence_source: UniProtKB REST exact accession lookup: A2T1U6


substrate_name: H2O; Ala-p-nitroanilide

sequence_source: UniProtKB REST exact accession lookup: P09960

substrate: H2O; Ala-p-nitroanilide


substrate_name: Ala-p-nitroanilide

substrate: Ala-p-nitroanilide


substrate_name: H2O; Arg-4-methylcoumaryl-7-amide

sequence_source: UniProtKB REST exact accession lookup: Q6P179

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

substrate: H2O; Arg-4-methylcoumaryl-7-amide


sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession lookup: Q9H4A4 and applied mutation signature F297Y to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST exact accession lookup: Q9H4A4

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


substrate_name: Met-enkephalin

substrate: Met-enkephalin


substrate_name: Lys 4-methylcoumarin 7-amide

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

substrate: Lys 4-methylcoumarin 7-amide


organism: Latilactobacillus sakei


organism: Mycosarcoma maydis


organism: Pediococcus acidilactici


organism: Rattus norvegicus


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


assay_conditions_summary: pH 7.4; 301.15 K; buffer complemented with 0

proof_lines:
at pH 7.4 and 28°C
recombinant Ap-B, at pH 7.4 and 25°C
Ap-B


organism: Streptococcus mitis

proof_lines:
enzyme II
enzyme I


organism: Sus scrofa

substrate_name: L-Lys-beta-naphthylamide

substrate: L-Lys-beta-naphthylamide


organism: Unknown


enzyme_display_name: dTDP-glucose 4,6-dehydratase

organism: Saccharothrix syringae

substrate_name: dTDP-alpha-D-glucose

sequence_source: UniProtKB live REST lookup for A0A5Q0HAF3

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

enzyme: dTDP-glucose 4,6-dehydratase

substrate: dTDP-alpha-D-glucose


organism: Salmonella typhimurium

substrate_name: dTDPglucose

sequence_source: UniProtKB live REST lookup for P26391

substrate: dTDPglucose


organism: Streptomyces venezuelae

substrate_name: UDP-alpha-D-glucose

sequence_source: UniProtKB live REST lookup for Q9ZGH3

proof_lines: 23°C, pH not specified in the publication

substrate: UDP-alpha-D-glucose


organism: Escherichia coli

substrate_name: dTDP-glucose

sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 FASTA direct check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature T134S to reconstruct the assayed variant sequence.

substrate: dTDP-glucose


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 FASTA direct check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature K164M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 FASTA direct check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature Y160A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 FASTA direct check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature K199R to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme K199R
pH 7.5, 37°C, mutant enzyme K199R


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 FASTA direct check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature Y301F to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme Y301F
pH 7.5, 37°C, mutant enzyme Y301F


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 FASTA direct check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature D135N/E136Q to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme D135N/E136Q
pH 7.5, 37°C, mutant enzyme D135N/E136Q


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 FASTA direct check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature E136A to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme E136A
pH 7.5, 37°C, mutant enzyme E136A


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 FASTA direct check; row-specific variant reconstructed from selected mutation_signature and applied mutation signature D135N to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme D135N
pH 7.5, 37°C, mutant enzyme D135N


organism: Acanthamoeba polyphaga Mimivirus

sequence_source: UniProtKB Q5UR12 direct accession lookup on 2026-06-04

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


organism: Aneurinibacillus thermoaerophilus

substrate_name: dTDP-D-glucose

sequence_source: UniProtKB Q93F85 direct accession lookup on 2026-06-04

substrate: dTDP-D-glucose


column_label: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes; block 'DSM 10155 RmlB'; substrate row 'dTDP-d-glucose'; column 'Km (mM)' = 0.012 +/- 0.0016; column 'kcat (s-1)' = 1.9 +/- 0.079; the table has no kcat/Km column.

normalized_value_unit_evidence: Km: paper cell 0.012 mM; the column is already mM, so normalized Km = 0.012 mM. kcat: paper cell 1.9 s-1; the column is already s^(-1), so normalized kcat = 1.9 s^(-1). kcat/Km: not printed anywhere in the paper; the full-precision quotient of the row's own cells is 1.9 / 0.012 = 158.33333333333331 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes, block 'DSM 10155 RmlB', substrate row 'dTDP-d-glucose': Km = 0.012 +/- 0.0016 mM; kcat = 1.9 +/- 0.079 s-1; no kcat/Km cell is printed.

row_label: Table 4, block 'DSM 10155 RmlB', substrate row 'dTDP-d-glucose'


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 direct accession lookup plus H232N reconstruction on 2026-06-04 and applied mutation signature H232N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 direct accession lookup plus H232Q reconstruction on 2026-06-04 and applied mutation signature H232Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 direct accession lookup plus C187S reconstruction on 2026-06-04 and applied mutation signature C187S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P27830 direct accession lookup on 2026-06-04

proof_lines:
pH 7.5, 18°C, wild-type enzyme
wild-type enzyme
pH 7.5, 37°C, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB P27830 direct accession lookup plus N190H reconstruction on 2026-06-04 and applied mutation signature N190H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P27830, followed by single-substitution reconstruction. and applied mutation signature E198Q to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme E198Q
pH 7.5, 37°C, mutant enzyme E198Q


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P27830, followed by single-substitution reconstruction. and applied mutation signature E136Q to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme E136Q
pH 7.5, 37°C, mutant enzyme E136Q


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P27830, followed by single-substitution reconstruction. and applied mutation signature K199M to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme K199M
pH 7.5, 37°C, mutant enzyme K199M


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB REST lookup for P27830, followed by single-substitution reconstruction. and applied mutation signature D135A to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme D135A
pH 7.5, 37°C, mutant enzyme D135A


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


sequence_source: Direct UniProtKB REST lookup for reviewed accession P55293.


sequence_source: Direct UniProtKB REST lookup for reviewed accession P27830.

proof_lines:
Raw SKiD Env: Temp=18°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----


organism: Mycobacterium tuberculosis

sequence_source: Direct UniProtKB REST lookup for reviewed accession P9WN65.


assay_conditions_summary: cofactor NAD+


organism: Saccharopolyspora erythraea


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Streptomyces peucetius

substrate_name: NAD+

substrate: NAD+


organism: Streptomyces rimosus


organism: Streptomyces sp. C5


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


organism: Acanthamoeba polyphaga mimivirus

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

proof_lines: kcat is 0.27 sec(-1) for UDP-alpha-D-glucose (PubMed:32083779). kcat is 0.18 sec(-1) for dTDP-alpha-D-glucose (PubMed:32083779).


enzyme_display_name: acetyl-CoA C-acyltransferase

organism: Bos taurus

substrate_name: Acetyl-CoA; Acetyldithio-CoA

assay_conditions_summary: cofactor CoA

enzyme: acetyl-CoA C-acyltransferase

substrate: Acetyl-CoA; Acetyldithio-CoA


organism: Caenorhabditis elegans

substrate_name: 3-Oxooctanoyl-CoA; Coenzyme A

substrate: 3-Oxooctanoyl-CoA; Coenzyme A


organism: Candida tropicalis

substrate_name: Acetoacetyl-CoA; Coenzyme A

substrate: Acetoacetyl-CoA; Coenzyme A


substrate_name: Coenzyme A; Acetoacetyl-CoA

proof_lines: SABIO-RK modifier species: acetyl-CoA C-acyltransferase(Enzyme) mutant G116F

substrate: Coenzyme A; Acetoacetyl-CoA


substrate_name: Coenzyme A

assay_conditions_summary: pH 8.1; 298.15 K; cofactor CoA

substrate: Coenzyme A


organism: Helianthus annuus


organism: Homo sapiens

substrate_name: Coenzyme A; 3-Oxodecanoyl-CoA

substrate: Coenzyme A; 3-Oxodecanoyl-CoA


substrate_name: acetyl-CoA

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

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

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

substrate: acetyl-CoA


organism: Rattus norvegicus


organism: Thermobifida fusca

substrate_name: glutaryl-CoA

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

substrate: glutaryl-CoA


substrate_name: malonyl-CoA

substrate: malonyl-CoA


substrate_name: alpha-D-Glucose 1-phosphate

sequence_source: UniProtKB:Q9AGY4 direct accession lookup; sequence version 2; source PMID 12147463.

column_label: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes; block 'DSM 10155 RmlA'; substrate row 'alpha-d-Glucose 1-phosphate'; column 'Km (mM)' = 0.20 +/- 0.036; column 'kcat (s-1)' = 13 +/- 1.1; the table has no kcat/Km column.

normalized_value_unit_evidence: Km: paper cell 0.20 mM; the column is already mM, so normalized Km = 0.20 mM. kcat: paper cell 13 s-1; the column is already s^(-1), so normalized kcat = 13 s^(-1). kcat/Km: not printed anywhere in the paper; the full-precision quotient of the row's own cells is 13 / 0.20 = 65.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes, block 'DSM 10155 RmlA', substrate row 'alpha-d-Glucose 1-phosphate': Km = 0.20 +/- 0.036 mM; kcat = 13 +/- 1.1 s-1; no kcat/Km cell is printed.

row_label: Table 4, block 'DSM 10155 RmlA', substrate row 'alpha-d-Glucose 1-phosphate'

substrate: alpha-D-Glucose 1-phosphate


substrate_name: dTTP

column_label: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes; block 'DSM 10155 RmlA'; substrate row 'dTTP'; column 'Km (mM)' = 0.031 +/- 0.0040; column 'kcat (s-1)' = 8.9 +/- 0.24; the table has no kcat/Km column.

normalized_value_unit_evidence: Km: paper cell 0.031 mM; the column is already mM, so normalized Km = 0.031 mM. kcat: paper cell 8.9 s-1; the column is already s^(-1), so normalized kcat = 8.9 s^(-1). kcat/Km: not printed anywhere in the paper; the full-precision quotient of the row's own cells is 8.9 / 0.031 = 287.0967741935484 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes, block 'DSM 10155 RmlA', substrate row 'dTTP': Km = 0.031 +/- 0.0040 mM; kcat = 8.9 +/- 0.24 s-1; no kcat/Km cell is printed.

row_label: Table 4, block 'DSM 10155 RmlA', substrate row 'dTTP'

substrate: dTTP


substrate_name: diphosphate

column_label: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes; block 'DSM 10155 RmlA'; substrate row 'Pyrophosphate'; column 'Km (mM)' = 0.055 +/- 0.0082; column 'kcat (s-1)' = 10 +/- 0.32; the table has no kcat/Km column.

normalized_value_unit_evidence: Km: paper cell 0.055 mM; the column is already mM, so normalized Km = 0.055 mM. kcat: paper cell 10 s-1; the column is already s^(-1), so normalized kcat = 10 s^(-1). kcat/Km: not printed anywhere in the paper; the full-precision quotient of the row's own cells is 10 / 0.055 = 181.8181818181818 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes, block 'DSM 10155 RmlA', substrate row 'Pyrophosphate': Km = 0.055 +/- 0.0082 mM; kcat = 10 +/- 0.32 s-1; no kcat/Km cell is printed.

row_label: Table 4, block 'DSM 10155 RmlA', substrate row 'Pyrophosphate'

substrate: diphosphate


substrate_name: alpha-D-Glucose 1-phosphate; dTTP

substrate: alpha-D-Glucose 1-phosphate; dTTP


enzyme_display_name: succinyl-CoA:acetate CoA-transferase

organism: Acetobacter aceti

substrate_name: Acetyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:B3EY95 canonical sequence; reconstructed N347A variant after residue-coordinate check and applied mutation signature N347A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

enzyme: succinyl-CoA:acetate CoA-transferase

substrate: Acetyl-CoA


substrate_name: succinate

sequence_variant_note: Resolved canonical sequence from UniProtKB:B3EY95 canonical sequence; reconstructed E435D variant after residue-coordinate check and applied mutation signature E435D to reconstruct the assayed variant sequence.

smiles: O=C(O)CCC(=O)O

substrate: succinate


substrate_name: Propanoate

sequence_variant_note: Resolved canonical sequence from UniProtKB:B3EY95 canonical sequence; reconstructed S71A variant after residue-coordinate check and applied mutation signature S71A to reconstruct the assayed variant sequence.

smiles: CCC(=O)O

substrate: Propanoate


substrate_name: succinyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:B3EY95 canonical sequence; reconstructed R228E variant after residue-coordinate check and applied mutation signature R228E to reconstruct the assayed variant sequence.

substrate: succinyl-CoA


substrate_name: Acetate

sequence_source: UniProtKB:B3EY95 canonical sequence; reconstructed S71A variant after residue-coordinate check

smiles: CC(=O)O

substrate: Acetate


substrate_name: Succinyl-CoA; Acetate

sequence_source: UniProtKB:B3EY95 canonical sequence; reconstructed E435D variant after residue-coordinate check

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines: SABIO-RK modifier species: succinyl-CoA:acetate CoA-transferase(Enzyme) mutant E435D AarC His6-tagged

proof_lines: mutant E435D, pH 8.0, temperature not specified in the publication

substrate: Succinyl-CoA; Acetate


sequence_source: UniProtKB:B3EY95 canonical sequence; reconstructed N347A variant after residue-coordinate check


substrate_name: dTDP-D-glucose

sequence_source: UniProtKB canonical FASTA:Q9AGY4; fetched 2026-06-04 via rest.uniprot.org

column_label: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes; block 'DSM 10155 RmlA'; substrate row 'dTDP-d-glucose'; column 'Km (mM)' = 0.13 +/- 0.036; column 'kcat (s-1)' = 15 +/- 2.0; the table has no kcat/Km column.

normalized_value_unit_evidence: Km: paper cell 0.13 mM; the column is already mM, so normalized Km = 0.13 mM. kcat: paper cell 15 s-1; the column is already s^(-1), so normalized kcat = 15 s^(-1). kcat/Km: not printed anywhere in the paper; the full-precision quotient of the row's own cells is 15 / 0.13 = 115.38461538461539 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes, block 'DSM 10155 RmlA', substrate row 'dTDP-d-glucose': Km = 0.13 +/- 0.036 mM; kcat = 15 +/- 2.0 s-1; no kcat/Km cell is printed.

row_label: Table 4, block 'DSM 10155 RmlA', substrate row 'dTDP-d-glucose'

substrate: dTDP-D-glucose


substrate_name: UTP

sequence_source: UniProtKB canonical FASTA:Q9XUS5; fetched 2026-06-04 via rest.uniprot.org

substrate: UTP


substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


proof_lines:
pH 7.5, 25°C
cosubstrate: UTP, pH 7.5, 25°C
cosubstrate: dTTP, pH 7.5, 25°C


sequence_source: UniProtKB canonical FASTA:P9WH13; fetched 2026-06-04 via rest.uniprot.org


proof_lines:
at pH 7.5 and 25Â°C
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.5


organism: Saccharothrix syringae

sequence_source: UniProtKB:A0A5Q0HD10 REST lookup on 2026-06-04


organism: Salmonella typhimurium

substrate_name: dTDP-D-glucose; Diphosphate

sequence_source: UniProtKB:P26393 REST lookup on 2026-06-04

substrate: dTDP-D-glucose; Diphosphate


sequence_source: UniProtKB:C6K8M0 REST lookup on 2026-06-04; canonical sequence only

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


sequence_source: UniProtKB:C6K8M0 REST lookup on 2026-06-04; canonical DnmL sequence only

proof_lines: pH 7.2, 37°C, fusion protein of isoform DnmL with C-terminal sequence of isoform RmbA


organism: Sulfurisphaera tokodaii

sequence_source: UniProtKB:Q975F9 REST lookup on 2026-06-04

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


sequence_source: UniProtKB:B3EY95 REST lookup on 2026-06-04


substrate_name: Acetoacetate

smiles: CC(=O)CC(=O)O

substrate: Acetoacetate