smiles: C(CO)C(CO)O


enzyme_display_name: glucose oxidase

organism: Streptomyces coelicolor

substrate_name: L-Threitol

source_db: brenda

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

smiles: C(C(C(CO)O)O)O

column_label: Table 1 row L-threitol, columns KM (mM), kcat (s^-1), and kcat/KM (mM^-1 s^-1).

normalized_value_unit_evidence: Table 1 normalized central values: KM=25 mM; kcat=6.3 s^-1; kcat/KM=0.25 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row L-threitol: KM=25 ± 1 mM; kcat=6.3 ± 0.1 s^-1; kcat/KM=0.25 mM^-1 s^-1.

row_label: L-threitol

table_label: Table 1, Steady-state kinetic parameters for m-AldO

data_origin: experimental

enzyme: glucose oxidase

substrate: L-Threitol

status: corrected

source: brenda


organism: Phanerodontia chrysosporium

verification_status: unverified

kcat_display: Not reported

kcat_over_km_display: Not reported

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

smiles: O=O

status: unverified


substrate_name: beta-D-glucose

substrate: beta-D-glucose


substrate_name: D-maltose

substrate: D-maltose


substrate_name: D-xylose

substrate: D-xylose


substrate_name: L-sorbose

substrate: L-sorbose


organism: Methylomonas sp. LW13

smiles: CCCCCCO


substrate_name: ethanol

smiles: CCO

substrate: ethanol


smiles: CCCCO


smiles: CCCO


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


enzyme_display_name: L-lactate oxidase

organism: Aerococcus viridans

substrate_name: (S)-lactate

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

mutation_type: substitution

enzyme: L-lactate oxidase

substrate: (S)-lactate


proof_lines:
wild-type, pH 6.5, 37°C
wild-type, pH 7.0, 25°C


proof_lines:
wild-type, pH 6.5, 20°C
wild-type, pH 6.5, 37°C
wild-type, pH 7.0, 25°C


organism: Pleurotus ostreatus

km_display: Not reported


enzyme_display_name: glucoside 3-dehydrogenase (cytochrome c)

organism: Agrobacterium fabrum

substrate_name: cytochrome c

substrate: cytochrome c


substrate_name: methyl alpha-D-glucoside

enzyme: glucoside 3-dehydrogenase (cytochrome c)

substrate: methyl alpha-D-glucoside


organism: Leeuwenhoekiella marinoflava

substrate_name: D-glucose

substrate: D-glucose


substrate_name: L-alpha-hydroxy-beta-methylvalerate

substrate: L-alpha-hydroxy-beta-methylvalerate


substrate_name: methanol

smiles: CO

proof_lines: in the presence of a mixture of La3+, Ce3+, Pr3+, Nd3+, at pH 7.2 and 60°C

proof_lines: pH and temperature not specified in the publication, lanthanide: La3+, Ce3+, Pr3+, Nd3+

substrate: methanol


organism: Methyloversatilis discipulorum

proof_lines: pH and temperature not specified in the publication


organism: Bradyrhizobium diazoefficiens


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R181K with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R181M with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


substrate_name: L-lactate

substrate: L-lactate


organism: Rhodovulum kholense


organism: Sinorhizobium meliloti


organism: Grimontia marina


organism: Tistlia consotensis


proof_lines: pH and temperature not specified in the publication, lanthanide: Ce3+


organism: Methylotenera mobilis

proof_lines: pH and temperature not specified in the publication, methanol dehydrogenase XoxF4-1


organism: Chlamydomonas reinhardtii


organism: Nostoc sp. PCC 7120 = FACHB-418


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


ki_unit: mM


organism: Gram-negative soil bacterium

substrate_name: (R)-lactate

substrate: (R)-lactate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A95G to reconstruct the assayed variant sequence.

proof_lines:
mutant A95G, pH 6.5, 20°C
mutant A95G, pH 7.0, 25°C


substrate_name: Unknown

substrate: Unknown


organism: Phanerochaete chrysosporium

substrate_name: beta-D-Glucose; O2

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

substrate: beta-D-Glucose; O2


organism: Goffeauzyma gastrica

proof_lines: 64°C, pH not specified in the publication


organism: Bombyx mori

proof_lines: immobilized enzyme, immobilized membrane with ratio stretching 1.25

proof_lines: immobilized enzyme, immobilized membrane with ratio stretching 3


enzyme_display_name: hexose oxidase

organism: Mazzaella flaccida

enzyme: hexose oxidase


organism: Talaromyces purpureogenus


organism: Penicillium amagasakiense

protein_accession_database: UniProt

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K424I with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant K424I, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme

proof_lines: recombinant mutant K424I, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K424E with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant K424E, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme

proof_lines: recombinant mutant K424E, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme


organism: Aspergillus niger

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T30V/I94V/A162T with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T30V/R37K/I94V/V106I/A162T/M556V with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: pH 5.5, temperature not specified in the publication, mutant enzyme T30V/R37K/I94V/V106I/A162T/M556V


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T30V/I94V/A162T/R537K/M556V with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T/R537K/M556V


sequence_source: multiple

smiles: C(C=O)C(C(C(CO)O)O)O

source_databases_merged: brenda uniprot


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P81156 and applied mutation signature H520V with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 298.15 K; buffer 0.1 M sodium acetate

column_label: Table 1 (Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6), GOX variant row 'H520V'; column 'Vmax (units/mg)' = 0.01; column 'Km (app) (mM)' = 6.7; column 'kcat (s^-1)' = 0.03; column 'kcat/Km (mM^-1 s^-1)' = 0.004; column '10^3 x Specificity (variant/wild-type)' = 0.01.

normalized_value_unit_evidence: Km: printed Table 1 cell 6.7 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 6.7 mM. kcat: printed Table 1 cell 0.03 s^-1; the printed unit is already s^-1, so no unit conversion applies; the paper value is 0.03 s^(-1). kcat/Km: printed Table 1 cell 0.004 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies; the paper value is 0.004 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GOX variant row 'H520V': Km (app) = 6.7 mM; kcat = 0.03 s^-1; printed kcat/Km = 0.004 mM^-1 s^-1.

row_label: Table 1, GOX variant row 'H520V'

table_label: Table 1: Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6 (Biochemical Journal 2000, 347:553-559)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P81156 and applied mutation signature H520A with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6), GOX variant row 'H520A'; column 'Vmax (units/mg)' = 0.08; column 'Km (app) (mM)' = 5.8; column 'kcat (s^-1)' = 0.16; column 'kcat/Km (mM^-1 s^-1)' = 0.03; column '10^3 x Specificity (variant/wild-type)' = 0.1.

normalized_value_unit_evidence: Km: printed Table 1 cell 5.8 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 5.8 mM. kcat: printed Table 1 cell 0.16 s^-1; the printed unit is already s^-1, so no unit conversion applies; the paper value is 0.16 s^(-1). kcat/Km: printed Table 1 cell 0.03 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies; the paper value is 0.03 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GOX variant row 'H520A': Km (app) = 5.8 mM; kcat = 0.16 s^-1; printed kcat/Km = 0.03 mM^-1 s^-1.

row_label: Table 1, GOX variant row 'H520A'


assay_conditions_summary: pH 6


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P81156 and applied mutation signature W430A with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6), GOX variant row 'W430A'; column 'Vmax (units/mg)' = 10.5; column 'Km (app) (mM)' = 27; column 'kcat (s^-1)' = 23; column 'kcat/Km (mM^-1 s^-1)' = 0.8; column '10^3 x Specificity (variant/wild-type)' = 2.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 27 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 27.0 mM. kcat: printed Table 1 cell 23 s^-1; the printed unit is already s^-1, so no unit conversion applies; the paper value is 23.0 s^(-1). kcat/Km: printed Table 1 cell 0.8 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies; the paper value is 0.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GOX variant row 'W430A': Km (app) = 27 mM; kcat = 23 s^-1; printed kcat/Km = 0.8 mM^-1 s^-1.

row_label: Table 1, GOX variant row 'W430A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P81156 and applied mutation signature R516Q with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6), GOX variant row 'R516Q'; column 'Vmax (units/mg)' = 33; column 'Km (app) (mM)' = 733; column 'kcat (s^-1)' = 71; column 'kcat/Km (mM^-1 s^-1)' = 0.1; column '10^3 x Specificity (variant/wild-type)' = 0.3.

normalized_value_unit_evidence: Km: printed Table 1 cell 733 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 733.0 mM. kcat: printed Table 1 cell 71 s^-1; the printed unit is already s^-1, so no unit conversion applies; the paper value is 71.0 s^(-1). kcat/Km: printed Table 1 cell 0.1 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies; the paper value is 0.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GOX variant row 'R516Q': Km (app) = 733 mM; kcat = 71 s^-1; printed kcat/Km = 0.1 mM^-1 s^-1.

row_label: Table 1, GOX variant row 'R516Q'


proof_lines: recombinant wild-type enzyme, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme

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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P81156 and applied mutation signature F418V with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6), GOX variant row 'F418V'; column 'Vmax (units/mg)' = 147; column 'Km (app) (mM)' = 13.3; column 'kcat (s^-1)' = 318; column 'kcat/Km (mM^-1 s^-1)' = 24; column '10^3 x Specificity (variant/wild-type)' = 74.3.

normalized_value_unit_evidence: Km: printed Table 1 cell 13.3 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 13.3 mM. kcat: printed Table 1 cell 318 s^-1; the printed unit is already s^-1, so no unit conversion applies; the paper value is 318.0 s^(-1). kcat/Km: printed Table 1 cell 24 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies; the paper value is 24.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GOX variant row 'F418V': Km (app) = 13.3 mM; kcat = 318 s^-1; printed kcat/Km = 24 mM^-1 s^-1.

row_label: Table 1, GOX variant row 'F418V'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P81156 and applied mutation signature R516K with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6), GOX variant row 'R516K'; column 'Vmax (units/mg)' = 279; column 'Km (app) (mM)' = 513; column 'kcat (s^-1)' = 603; column 'kcat/Km (mM^-1 s^-1)' = 1.2; column '10^3 x Specificity (variant/wild-type)' = 3.7.

normalized_value_unit_evidence: Km: printed Table 1 cell 513 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 513.0 mM. kcat: printed Table 1 cell 603 s^-1; the printed unit is already s^-1, so no unit conversion applies; the paper value is 603.0 s^(-1). kcat/Km: printed Table 1 cell 1.2 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies; the paper value is 1.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GOX variant row 'R516K': Km (app) = 513 mM; kcat = 603 s^-1; printed kcat/Km = 1.2 mM^-1 s^-1.

row_label: Table 1, GOX variant row 'R516K'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P81156 and applied mutation signature Y73F with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6), GOX variant row 'Y73F'; column 'Vmax (units/mg)' = 295; column 'Km (app) (mM)' = 24; column 'kcat (s^-1)' = 639; column 'kcat/Km (mM^-1 s^-1)' = 26; column '10^3 x Specificity (variant/wild-type)' = 80.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 24 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 24.0 mM. kcat: printed Table 1 cell 639 s^-1; the printed unit is already s^-1, so no unit conversion applies; the paper value is 639.0 s^(-1). kcat/Km: printed Table 1 cell 26 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies; the paper value is 26.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GOX variant row 'Y73F': Km (app) = 24 mM; kcat = 639 s^-1; printed kcat/Km = 26 mM^-1 s^-1.

row_label: Table 1, GOX variant row 'Y73F'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P81156 and applied mutation signature N518T with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6), GOX variant row 'N518T'; column 'Vmax (units/mg)' = 539; column 'Km (app) (mM)' = 36; column 'kcat (s^-1)' = 1166; column 'kcat/Km (mM^-1 s^-1)' = 33; column '10^3 x Specificity (variant/wild-type)' = 102.2.

normalized_value_unit_evidence: Km: printed Table 1 cell 36 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 36.0 mM. kcat: printed Table 1 cell 1166 s^-1; the printed unit is already s^-1, so no unit conversion applies; the paper value is 1166.0 s^(-1). kcat/Km: printed Table 1 cell 33 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies; the paper value is 33.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GOX variant row 'N518T': Km (app) = 36 mM; kcat = 1166 s^-1; printed kcat/Km = 33 mM^-1 s^-1.

row_label: Table 1, GOX variant row 'N518T'


organism: Methylorubrum extorquens

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

proof_lines: in the presence of Nd3+, at pH 7.0 and 30°C

proof_lines: Nd-XoxF, pH 7.0, 30°C, determined using the dye-linked activity, DCPIP reduction

proof_lines: in the presence of Ce3+, at pH 7.0 and 30°C

source_databases_merged: brenda skid


organism: Penicillium adametzii

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

assay_conditions_summary: pH 5

proof_lines:
pH 5.0, 25°C, enzyme fraction 1
pH 5.0, 25°C, enzyme fraction 2
pH 5.0, 25°C


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


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

proof_lines: XoxF1, in the absence of lanthanides, pH and temperature not specified in the publication

proof_lines: XoxF1, in the presence of La3+, pH and temperature not specified in the publication


assay_conditions_summary: pH 9


proof_lines: recombinant enzyme yGOXpenag, using ferrocinium-methanol as cosubstrate, pH 6.0, 50°C

proof_lines: recombinant enzyme yGOXpenag, using O2 as cosubstrate, pH 6.0, 50°C

source_databases_merged: brenda skid uniprot


organism: Chondrus crispus

proof_lines: pH 7.0, temperature not specified in the publication


organism: Talaromyces variabilis

proof_lines:
pH 5.0, 28°C, native enzyme
pH 5.0, 28°C, recombinant enzyme


enzyme_display_name: Transferred entry: 1.13.12.4

organism: Aerococcus viridans

source_db: oed

enzyme: Transferred entry: 1.13.12.4

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y215F with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y215H with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P81156 and applied mutation signature F418V with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6; row F418V; columns Km(app) (mM), kcat (s^-1), and kcat/Km (mM^-1*s^-1); F418V: Km(app) 13.3 +/- 0.7 mM; kcat 318 s^-1; kcat/Km 24 mM^-1*s^-1. The printed central Km value is 13.3 mM and the independently printed efficiency is 24 mM^-1*s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P81156 and applied mutation signature H520A with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6; row H520A; columns Km(app) (mM), kcat (s^-1), and kcat/Km (mM^-1*s^-1); H520A: Km(app) 5.8 +/- 0.7 mM; kcat 0.16 s^-1; kcat/Km 0.03 mM^-1*s^-1. The printed central Km value is 5.8 mM and the independently printed efficiency is 0.03 mM^-1*s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P81156 and applied mutation signature N518T with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6; row N518T; columns Km(app) (mM), kcat (s^-1), and kcat/Km (mM^-1*s^-1); N518T: Km(app) 36 +/- 2 mM; kcat 1166 s^-1; kcat/Km 33 mM^-1*s^-1. The printed central Km value is 36 mM and the independently printed efficiency is 33 mM^-1*s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P81156 and applied mutation signature R516K with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6; row R516K; columns Km(app) (mM), kcat (s^-1), and kcat/Km (mM^-1*s^-1); R516K: Km(app) 513 +/- 90 mM; kcat 603 s^-1; kcat/Km 1.2 mM^-1*s^-1. The printed central Km value is 513 mM and the independently printed efficiency is 1.2 mM^-1*s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P81156 and applied mutation signature W430A with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6; row W430A; columns Km(app) (mM), kcat (s^-1), and kcat/Km (mM^-1*s^-1); W430A: Km(app) 27 +/- 4 mM; kcat 23 s^-1; kcat/Km 0.8 mM^-1*s^-1. The printed central Km value is 27 mM and the independently printed efficiency is 0.8 mM^-1*s^-1.


column_label: Primary-paper Table 1 lists Wild type kcat 2003, Km 6.2 +/- 0.5, and kcat/Km 323; export kcat/Km is 323.06451612903226.

row_label: Wild type row

table_label: Table 1: Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P81156 and applied mutation signature Y73F with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6; row Y73F; columns Km(app) (mM), kcat (s^-1), and kcat/Km (mM^-1*s^-1); Y73F: Km(app) 24 +/- 2 mM; kcat 639 s^-1; kcat/Km 26 mM^-1*s^-1. The printed central Km value is 24 mM and the independently printed efficiency is 26 mM^-1*s^-1.


verification_status: verified

column_label: Primary-paper PMC Table 4 reports 2-Deoxy-D-glucose columns Km 8.3 +/- 0.7 mM, kcat 83 s^-1, and kcat/Km 10.0 s^-1 mM^-1.

raw_value_unit_evidence: 2-Deoxy-D-glucose Km 8.3 +/- 0.7 mM; kcat 83 s^-1; kcat/Km 10.0 s^-1 mM^-1

row_label: 2-Deoxy-D-glucose row

table_label: Table 4: Kinetic parameters of recombinant GOX for different sugars

status: verified


substrate_name: D-Galactose

column_label: Primary-paper PMC Table 4 reports D-Galactose columns Km 952 +/- 9 mM, kcat 159 s^-1, and kcat/Km 0.2 s^-1 mM^-1.

raw_value_unit_evidence: D-Galactose Km 952 +/- 9 mM; kcat 159 s^-1; kcat/Km 0.2 s^-1 mM^-1

row_label: D-Galactose row

substrate: D-Galactose


substrate_name: D-Mannose

column_label: Primary-paper PMC Table 4 reports D-Mannose columns Km 106 +/- 8 mM, kcat 401 s^-1, and kcat/Km 3.8 s^-1 mM^-1.

raw_value_unit_evidence: D-Mannose Km 106 +/- 8 mM; kcat 401 s^-1; kcat/Km 3.8 s^-1 mM^-1

row_label: D-Mannose row

substrate: D-Mannose


substrate_name: D-Xylose

column_label: Primary-paper PMC Table 4 reports D-Xylose columns Km 384 +/- 27 mM, kcat 72 s^-1, and kcat/Km 0.2 s^-1 mM^-1.

normalized_value_unit_evidence: Km 384 mM = 384 mM; kcat 72 s^-1 = 72 s^-1; table kcat/Km 0.2 is a one-decimal display of 72/384 = 0.1875 s^-1 mM^-1

row_label: D-Xylose row

substrate: D-Xylose


organism: Penicillium sp. MX3343

substrate_name: beta-D-glucose

substrate: beta-D-glucose


column_label: Table 2 GOxP5 row lists Km / kcat / kcat/Km as 0.0657 mol L^-1 / 137.1 s^-1 / 2086.758 mol^-1 L s^-1

row_label: GOxP5 row

table_label: Frontiers PDF Table 2


proof_lines:
hexose oxidase
Chondrus crispus
Km(O2)


substrate_name: lactose

proof_lines:
hexose oxidase
Chondrus crispus
lactose

substrate: lactose


enzyme_display_name: 1-butanol dehydrogenase (cytochrome c)

organism: Thauera butanivorans (strain ATCC 43655 / DSM 2080 / JCM 20651 / CCUG 51053 / NBRC 103042 / IAM 12574 / Bu B1211)

substrate_name: butyraldehyde

source_db: uniprot

smiles: CCCC=O

assay_conditions_summary: pH 8

column_label: Catalytic-properties prose reports butyraldehyde Km 535 +/- 13 uM and states that BDH affinity for 1-butanol is 76-fold higher.

raw_value_unit_evidence: Km=535 +/- 13 uM for butyraldehyde.

row_label: butyraldehyde

table_label: Primary article PDF page 9 / printed page 753, Catalytic properties prose

enzyme: 1-butanol dehydrogenase (cytochrome c)

substrate: butyraldehyde

source: uniprot


enzyme_display_name: Carbohydrate oxidase

organism: Microdochium nivale

substrate_name: cellobiose (at pH 6 and 30 degrees Celsius)

enzyme: Carbohydrate oxidase


substrate_name: glucose (at pH 6 and 40 degrees Celsius)

column_label: Results prose reports Km values of 42, 11, and 59 mM for Glc, maltose, and cellobiose, respectively.

raw_value_unit_evidence: Km raw_value=42 raw_unit=mM

row_label: r-MnCO / Glc

table_label: Wiley full-text results prose, enzymatic properties of r-MnCO


organism: Thauera butanivorans

column_label: The abstract reports BDH exhibited its lowest Km, 7+/-1 microM, towards 1-butanol.

raw_value_unit_evidence: Km raw_value=7 microM raw_unit=microM

row_label: Prose segment: 1-butanol Km

table_label: PubMed PMID 11238982 abstract


substrate_name: acetaldehyde

smiles: CC=O

column_label: Fig. 3D two-carbon-substrate table lists acetaldehyde Km 285 uM.

raw_value_unit_evidence: Km raw_value=285 raw_unit=uM

row_label: ExaF-La / acetaldehyde row

table_label: Fig. 3D, ExaF kinetic parameters with two-carbon substrates

substrate: acetaldehyde


substrate_name: Acceptor

smiles: [At]

substrate: Acceptor


enzyme_display_name: UniProt P13006

source_db: skid

proof_lines:
Raw SKiD Env: Temp=37°C, pH=5.1
Raw SKiD Env: Temp=25°C, pH=6
Raw SKiD Env: Temp=25°C, pH=7.4

source_databases_merged: skid uniprot

enzyme: UniProt P13006

source: skid


enzyme_display_name: Glucose oxidase

proof_lines: kinetic analysis of a yeast-derived enzyme

enzyme: Glucose oxidase


organism: Penicillium chrysogenum

substrate_name: D-xylose

column_label: OUP full text reports Km,xylose = 690 mmol l^-1 for Penicillium chrysogenum GOX.

raw_value_unit_evidence: Km raw_value=690 mmol l^-1 raw_unit=mmol l^-1

row_label: Penicillium chrysogenum GOX / D-xylose

table_label: Results prose: GOX kinetic parameters

substrate: D-xylose


substrate_name: oxygen

column_label: Abstract reports K(m) for oxygen was 0.97 mM.

raw_value_unit_evidence: Km raw_value=0.97 mM raw_unit=mM

row_label: Microdochium nivale carbohydrate oxidase / oxygen

table_label: PubMed XML abstract PMID 17154316

substrate: oxygen


enzyme_display_name: L-lactate dehydrogenase (cytochrome)

organism: Saccharomyces cerevisiae

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

proof_lines: influence of anions (400 mM KBr) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration

proof_lines: influence of anions (400 mM potassium acetate) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration

enzyme: L-lactate dehydrogenase (cytochrome)


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

proof_lines: influence of anions (400 mM KBr) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration

proof_lines: influence of anions (400 mM KCl) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration

proof_lines: influence of anions (400 mM potassium acetate) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration


assay_conditions_summary: pH 7; 278.15 K; cofactor FMN

proof_lines: influence of anions (400 mM KBr) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration

proof_lines: influence of anions (200 mM phsophate) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration

proof_lines: influence of anions (400 mM KCl) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration


mutation_signature: stopped-flow kinetic parameters for flavin reduction by L-lactate using holo- , reaction conditions: 100 mM phosphate , 1 mM EDTA, , , in the absence of ferrocy

mutation_type: truncation

proof_lines: stopped-flow kinetic parameters for flavin reduction by L-lactate using holo-enzyme, reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, in the absence of ferrocyanide


mutation_signature: stopped-flow kinetic parameters for flavin reduction by L-lactate using FDH domain, reaction conditions: 100 mM phosphate , 1 mM EDTA, , , in the absence of fer

proof_lines: stopped-flow kinetic parameters for flavin reduction by L-lactate using FDH domain, reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, in the absence of ferrocyanide


enzyme_display_name: D-lactate dehydrogenase (cytochrome)

organism: Arabidopsis thaliana

substrate_name: glycolate

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

enzyme: D-lactate dehydrogenase (cytochrome)

substrate: glycolate


substrate_name: D-glycerate

substrate: D-glycerate


substrate_name: L-lactate


substrate_name: D-lactate

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

substrate: D-lactate


enzyme_display_name: aryl-alcohol oxidase

organism: Bjerkandera adusta

substrate_name: anisyl alcohol

enzyme: aryl-alcohol oxidase

substrate: anisyl alcohol


organism: Sphingobacterium sp.

substrate_name: veratryl alcohol

substrate: veratryl alcohol


substrate_name: 3,4-dimethoxybenzyl alcohol

substrate: 3,4-dimethoxybenzyl alcohol


enzyme_display_name: UniProt G2PZJ2

organism: Thermothelomyces thermophilus

source_license: CC BY-NC-ND 4.0

enzyme: UniProt G2PZJ2


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


organism: Colletotrichum graminicola

substrate_name: 3-anisyl alcohol

substrate: 3-anisyl alcohol


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -8, so it is treated as a source-provided variant sequence.


substrate_name: 4-anisyl alcohol

substrate: 4-anisyl alcohol


substrate_name: 4-Hydroxybenzyl alcohol

substrate: 4-Hydroxybenzyl alcohol


sequence_variant_note: Mutation signature Y334W could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: benzyl alcohol

substrate: benzyl alcohol


enzyme_display_name: pyranose oxidase

organism: Irpex lacteus

substrate_name: D-fructose

enzyme: pyranose oxidase

substrate: D-fructose


substrate_name: cellobiose

substrate: cellobiose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: D-xylose


substrate_name: sucrose

substrate: sucrose


organism: Trametes versicolor

substrate_name: beta-D-glucose

substrate: beta-D-glucose


organism: Trametes hirsuta

substrate_name: D-glucose

substrate: D-glucose


enzyme_display_name: UniProt Q7ZA32

organism: Trametes ochracea

substrate_name: D-melibiose

enzyme: UniProt Q7ZA32

substrate: D-melibiose


enzyme_display_name: Pyranose 2-oxidase

enzyme: Pyranose 2-oxidase


enzyme_display_name: UniProt Q5NT46

organism: Mesorhizobium loti

substrate_name: pyridoxine

enzyme: UniProt Q5NT46

substrate: pyridoxine


enzyme_display_name: alcohol oxidase

organism: Phanerodontia chrysosporium

substrate_name: n-butanol

enzyme: alcohol oxidase

substrate: n-butanol


enzyme_display_name: UniProt P04842

organism: Komagataella pastoris

substrate_name: methanol

enzyme: UniProt P04842

substrate: methanol


enzyme_display_name: UniProt Q7X2H8

organism: Arthrobacter globiformis

enzyme: UniProt Q7X2H8


enzyme_display_name: UniProt T2M2J4

proof_lines:
Raw SKiD Env: Temp=23°C, pH=7.5
Raw SKiD Env: Temp=50°C, pH=9

enzyme: UniProt T2M2J4


substrate_name: diethylene glycol

smiles: C(COCCO)O

substrate: diethylene glycol


smiles: CC(CO)O


substrate_name: ethanol

substrate: ethanol


smiles: CC(CCCO)O


smiles: C(CCO)CCO


smiles: C(CCCO)CCO


smiles: C(CCO)CO


smiles: C(CSCCO)O


substrate_name: n-Pentanol

smiles: CCCCCO

substrate: n-Pentanol


smiles: CCCCCCCCCCO


smiles: CCCCCCCO


smiles: CCCCCCCCO


enzyme_display_name: scyllo-inositol 2-dehydrogenase (NADP+)

organism: Bacillus subtilis

substrate_name: NADPH

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

enzyme: scyllo-inositol 2-dehydrogenase (NADP+)

substrate: NADPH


substrate_name: NADP+

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

substrate: NADP+


substrate_name: scyllo-Inositol

substrate: scyllo-Inositol


enzyme_display_name: 3alpha-hydroxysteroid 3-dehydrogenase

organism: Homo sapiens

substrate_name: allopregnanolone

proof_lines: in 100 mM potassium phosphate, pH 7.0, at 25°C

enzyme: 3alpha-hydroxysteroid 3-dehydrogenase

substrate: allopregnanolone


assay_conditions_summary: pH 7; cofactor NADPH


assay_conditions_summary: pH 7; cofactor NADP+


enzyme_display_name: cholesterol oxidase

organism: Rhodococcus erythropolis

substrate_name: cholesterol

enzyme: cholesterol oxidase

substrate: cholesterol


organism: Coprinopsis cinerea

substrate_name: benzyl alcohol

substrate: benzyl alcohol


substrate_name: isovanillyl alcohol

substrate: isovanillyl alcohol


substrate_name: 4-Hydroxybenzyl alcohol

substrate: 4-Hydroxybenzyl alcohol


substrate_name: 3-Hydroxybenzyl alcohol

substrate: 3-Hydroxybenzyl alcohol


substrate_name: 3-anisyl alcohol

substrate: 3-anisyl alcohol


substrate_name: veratryl alcohol

substrate: veratryl alcohol


substrate_name: 4-anisyl alcohol

substrate: 4-anisyl alcohol


substrate_name: Vanillyl alcohol

substrate: Vanillyl alcohol


smiles: CC=CC=CCO


smiles: C/C=C/C=C/CO


organism: Nocardia erythropolis


proof_lines: Km increases when enzyme is entrapped in reverse micelles of the synthetic surfactant aerosol-OT-isooctane


organism: Pimelobacter simplex

substrate_name: stigmasterol

protein_accession_database: NCBI Protein

sequence_source: GenBank protein WP_052138420.1 translated from CP009896.1 (Pimelobacter simplex PsChO)

sequence_variant_note: Mutation signature F70V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.5, temperature not specified in the publication, mutant enzyme F70V

substrate: stigmasterol


assay_conditions_summary: pH 7.5; buffer phosphate

normalized_value_unit_evidence: Km normalized_value=0.78961 normalized_unit=mM; kcat normalized_value=1.58 normalized_unit=s^-1; kcat/Km normalized_value=2.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=789.61 +/- 4.71 raw_unit=uM; kcat raw_value=1.58 +/- 0.07 raw_unit=s^-1; kcat/Km raw_value=0.002 +/- 0.0001 raw_unit=uM^-1 s^-1

row_label: stigmasterol; WT

table_label: Table 1. Kinetic parameters of PsChO WT and variants toward five substrates


sequence_variant_note: Mutation signature V64C could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.5, temperature not specified in the publication, mutant enzyme V64C


substrate_name: dehydroepiandrosterone

column_label: Table 1 row dehydroepiandrosterone, column WT, lists K_m 341.21 +/- 3.79 uM, kcat 6.82 +/- 0.14 s^-1, and kcat/K_m 0.02 +/- 0.0004 uM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.34121 normalized_unit=mM; kcat normalized_value=6.82 normalized_unit=s^-1; kcat/Km normalized_value=20.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=341.21 +/- 3.79 raw_unit=uM; kcat raw_value=6.82 +/- 0.14 raw_unit=s^-1; kcat/Km raw_value=0.02 +/- 0.0004 raw_unit=uM^-1 s^-1

row_label: dehydroepiandrosterone; WT

substrate: dehydroepiandrosterone


substrate_name: beta-sitosterol

column_label: Table 1 row beta-sitosterol, column WT, lists K_m 328.61 +/- 3.60 uM, kcat 9.86 +/- 0.35 s^-1, and kcat/K_m 0.03 +/- 0.0005 uM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.32861 normalized_unit=mM; kcat normalized_value=9.86 normalized_unit=s^-1; kcat/Km normalized_value=30.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=328.61 +/- 3.60 raw_unit=uM; kcat raw_value=9.86 +/- 0.35 raw_unit=s^-1; kcat/Km raw_value=0.03 +/- 0.0005 raw_unit=uM^-1 s^-1

row_label: beta-sitosterol; WT

substrate: beta-sitosterol


substrate_name: pregnenolone

normalized_value_unit_evidence: Km normalized_value=0.29455 normalized_unit=mM; kcat normalized_value=11.78 normalized_unit=s^-1; kcat/Km normalized_value=40.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=294.55 +/- 2.97 raw_unit=uM; kcat raw_value=11.78 +/- 0.34 raw_unit=s^-1; kcat/Km raw_value=0.04 +/- 0.0005 raw_unit=uM^-1 s^-1

row_label: pregnenolone; WT

substrate: pregnenolone


normalized_value_unit_evidence: Km normalized_value=0.20485 normalized_unit=mM; kcat normalized_value=12.29 normalized_unit=s^-1; kcat/Km normalized_value=60.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=204.85 +/- 3.14 raw_unit=uM; kcat raw_value=12.29 +/- 0.32 raw_unit=s^-1; kcat/Km raw_value=0.06 +/- 0.0003 raw_unit=uM^-1 s^-1

row_label: cholesterol; WT


organism: Mycolicibacterium neoaurum

proof_lines:
pH 7.5, 37°C, full-length isozyme ChoM2
pH 7.5, 37°C


mutation_signature: truncated isozyme ChoM2


substrate_name: dehydroandrosterone

substrate: dehydroandrosterone


substrate_name: diosgenin

proof_lines:
pH 7.5, 37°C
pH 7.5, 37°C, full-length isozyme ChoM2

substrate: diosgenin


sequence_source: UniProtKB E3Q9X3 (CgrAAO; GLRG_02805)

sequence_variant_note: Resolved canonical sequence from UniProtKB E3Q9X3 (CgrAAO; GLRG_02805) and applied mutation signature Y334F with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB E3Q9X3 (CgrAAO; GLRG_02805) and applied mutation signature Y334W with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


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


organism: Cornu aspersum

substrate_name: Octanol

substrate: Octanol


substrate_name: Tetradecanol

smiles: CCCCCCCCCCCCCCO

substrate: Tetradecanol


substrate_name: Decanol

substrate: Decanol


substrate_name: hexadecanol

smiles: CCCCCCCCCCCCCCCCO

substrate: hexadecanol


substrate_name: Hexanol

smiles: CCCCCCO

substrate: Hexanol


substrate_name: Dodecanol

smiles: CCCCCCCCCCCCO

substrate: Dodecanol


substrate_name: Propanol

smiles: CCCO

substrate: Propanol


substrate_name: butanol

smiles: CCCCO

substrate: butanol


smiles: CCC=CCCCO


organism: Fusarium oxysporum f. sp. lycopersici


substrate_name: veratryl alcohol

substrate: veratryl alcohol


substrate_name: benzyl alcohol

substrate: benzyl alcohol


substrate_name: 4-methoxybenzyl alcohol

substrate: 4-methoxybenzyl alcohol


substrate_name: 3-Methoxybenzyl alcohol

substrate: 3-Methoxybenzyl alcohol


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


organism: Fusarium graminearum


organism: Poria contigua

substrate_name: methanol

smiles: CO

substrate: methanol


substrate_name: ethanol

smiles: CCO

substrate: ethanol


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: n-Propanol

substrate: n-Propanol


substrate_name: n-butanol

substrate: n-butanol


substrate_name: Isopropanol

smiles: CC(C)O

substrate: Isopropanol


smiles: C(CS)O


organism: Ogataea angusta

substrate_name: p-benzoquinone

substrate: p-benzoquinone


smiles: O=O


substrate_name: allyl alcohol

smiles: C=CCO

substrate: allyl alcohol


organism: Mycosarcoma maydis

substrate_name: 2,4-Dimethoxybenzyl alcohol

substrate: 2,4-Dimethoxybenzyl alcohol


substrate_name: anisyl alcohol

substrate: anisyl alcohol


substrate_name: 4-Hydroxybenzyl alcohol

substrate: 4-Hydroxybenzyl alcohol


organism: Ochrobactrum sp.

smiles: CCCCCCCCCCO


smiles: CCCCCCCCO


smiles: CCCCCO


substrate_name: Lactate

substrate: Lactate


substrate_name: glycolate

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

substrate: glycolate


organism: Colletotrichum graminicola


smiles: CCCCCCCO

column_label: PDF Table 1 CgrAlcOx row 1-Heptanol; paper tuple kcat=100 s^-1, Km=0.19 mM, kcat/Km=530 s^-1*mM^-1 differs from export tuple kcat=85.8, Km=0.19, kcat/Km=451.57894736842104.

normalized_value_unit_evidence: kcat normalized_value=100 normalized_unit=s^-1; Km normalized_value=0.19 normalized_unit=mM; kcat/Km normalized_value=530 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: kcat raw_value=100 raw_unit=s^-1; Km raw_value=0.19 raw_unit=mM; kcat/Km raw_value=5.3e5 raw_unit=s^-1*M^-1.

table_label: Table 1. Substrate specificity of CgrAlcOx and CglAlcOx


organism: Phlebiopsis gigantea


substrate_name: D-ribose

substrate: D-ribose


substrate_name: ribitol

smiles: C(C(C(C(CO)O)O)O)O

substrate: ribitol


substrate_name: erythritol

smiles: C(C(C(CO)O)O)O

substrate: erythritol


organism: Schizophyllum commune

substrate_name: beta-sitosterol

substrate: beta-sitosterol


substrate_name: stigmasterol

substrate: stigmasterol


substrate_name: pregnenolone

substrate: pregnenolone


substrate_name: dehydroepiandrosterone

proof_lines: in the presence and absence of undecanol

substrate: dehydroepiandrosterone


enzyme_display_name: galactose oxidase

organism: Polyporus circinatus

substrate_name: ganglioside

proof_lines: gangliosides in aqueous solution from Tay Sachs disease, competitive non-substrate inhibition

proof_lines: bovine brain gangliosides in aqueous solution, competitive non-substrate inhibition

proof_lines: bovine brain gangliosides in 70% n-propanol, competitive substrate inhibition

enzyme: galactose oxidase

substrate: ganglioside


substrate_name: N-acetyl-D-galactosamine

substrate: N-acetyl-D-galactosamine


substrate_name: D-galactosamine

substrate: D-galactosamine


smiles: C(C=O)C(C(C(CO)O)O)O


organism: Aspergillus terreus

substrate_name: n-Heptanol

substrate: n-Heptanol


substrate_name: n-dodecanol

smiles: CCCCCCCCCCCCO

substrate: n-dodecanol


proof_lines:
substrate: R-(-)-2-octanol
substrate: n-dodecanol
substrate: n-heptanol


smiles: CCCCCCC(C)O


organism: Basidiomycota

substrate_name: methanol

smiles: CO

substrate: methanol


substrate_name: ethanol

smiles: CCO

substrate: ethanol


substrate_name: n-Propanol

smiles: CCCO

substrate: n-Propanol


substrate_name: n-butanol

smiles: CCCCO

substrate: n-butanol


organism: Thermothelomyces thermophilus

assay_conditions_summary: pH 6; buffer pH 6

column_label: Table 1; row 5-HMF; KM, kcat, and kcat/KM columns.

table_label: Table 1. MtAAOx substrate specificity and kinetic parameters


substrate_name: veratryl alcohol

column_label: Table 1; row veratryl alcohol; KM, kcat, and kcat/KM columns.

row_label: veratryl alcohol

substrate: veratryl alcohol


substrate_name: cinnamyl alcohol

column_label: Table 1; row cinnamyl alcohol; KM, kcat, and kcat/KM columns.

row_label: cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: anisyl alcohol

column_label: Table 1; row anisyl alcohol; KM, kcat, and kcat/KM columns.

row_label: anisyl alcohol

substrate: anisyl alcohol


organism: Pseudomonas sp. 11/12A


organism: Nocardia erythropolis


substrate_name: sitosterol

substrate: sitosterol


substrate_name: fucosterol

substrate: fucosterol


organism: Aspergillus oryzae

substrate_name: D-galactose

substrate: D-galactose


substrate_name: D-xylose

column_label: Table 2; row D-Xylose; AoPOx columns Km, kcat, and kcat/Km.

row_label: D-Xylose / AoPOx

table_label: Table 2

substrate: D-xylose


substrate_name: L-sorbose

column_label: Table 2; row L-Sorbose; AoPOx columns Km, kcat, and kcat/Km.

row_label: L-Sorbose / AoPOx

substrate: L-sorbose


substrate_name: ferricenium hexafluorophosphate

column_label: Table 3; row AoPOx Fc+PF6-; columns Km, kcat, and kcat/Km; footnote b pH 8.0.

row_label: Fc+PF6- / AoPOx

table_label: Table 3

substrate: ferricenium hexafluorophosphate


column_label: Table 3; row AoPOx 1,4-Benzoquinone; columns Km, kcat, and kcat/Km; footnote a pH 4.5.

row_label: 1,4-Benzoquinone / AoPOx


organism: Hypomyces rosellus


proof_lines:
native wild-type enzyme
recombinant wild-type enzyme


organism: Pseudomonas nitroreducens

column_label: TABLE 3. Steady-state kinetic constants for the oxidation of vanillyl alcohol, HMF, DFF, and FDCA by HMFOs; row FFCA / 5-formylfuran-2-carboxylate / PseniHMFOHis; columns kcat, Km, kcat/Km; kcat raw_value=0.05 +/- 0.01 raw_unit=min^-1; Km raw_value=0.6 +/- 0.3 raw_unit=mM; kcat/Km raw_value=0.09 +/- 0.05 raw_unit=mM^-1*min^-1

normalized_value_unit_evidence: kcat normalized_value=0.00083 normalized_unit=s^-1; Km normalized_value=0.6 normalized_unit=mM; kcat/Km normalized_value=0.0013833333333333334 normalized_unit=s^-1*mM^-1


column_label: TABLE 3. Steady-state kinetic constants for the oxidation of vanillyl alcohol, HMF, DFF, and FDCA by HMFOs; row DFF / furan-2,5-dicarbaldehyde / PseniHMFOHis; columns kcat, Km, kcat/Km; kcat raw_value=1.0 +/- 0.1 raw_unit=min^-1; Km raw_value=4.8 +/- 1.9 raw_unit=mM; kcat/Km raw_value=0.2 +/- 0.08 raw_unit=mM^-1*min^-1

normalized_value_unit_evidence: kcat normalized_value=0.017 normalized_unit=s^-1; Km normalized_value=4.8 normalized_unit=mM; kcat/Km normalized_value=0.003541666666666667 normalized_unit=s^-1*mM^-1


column_label: TABLE 3. Steady-state kinetic constants for the oxidation of vanillyl alcohol, HMF, DFF, and FDCA by HMFOs; row HMF / 5-(hydroxymethyl)furfural / PseniHMFOHis; columns kcat, Km, kcat/Km; kcat raw_value=14.3 +/- 0.9 raw_unit=min^-1; Km raw_value=5.1 +/- 1.1 raw_unit=mM; kcat/Km raw_value=2.8 +/- 0.6 raw_unit=mM^-1*min^-1

normalized_value_unit_evidence: kcat normalized_value=0.24 normalized_unit=s^-1; Km normalized_value=5.1 normalized_unit=mM; kcat/Km normalized_value=0.047058823529411764 normalized_unit=s^-1*mM^-1


organism: Pseudarthrobacter siccitolerans

substrate_name: D-glucose

proof_lines: with O2 as electron acceptor, at pH 6.5 and 37°C

proof_lines: with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 37°C

substrate: D-glucose


substrate_name: L-arabinose

substrate: L-arabinose


proof_lines: with D-glucose as cosubstrate, at pH 6.5 and 37°C


substrate_name: formaldehyde

smiles: C=O

proof_lines:
pH 7.5, 30°C
cosubstrate: p-benzoquinone
cosubstrate: O2

substrate: formaldehyde


proof_lines:
pH 7.5, 30°C
free enzyme
immobilized enzyme


organism: Paecilomyces variotii


organism: Methylovorus sp. MP688

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

column_label: TABLE 3. Steady-state kinetic constants for the oxidation of vanillyl alcohol, HMF, DFF, and FDCA by HMFOs; row DFF / furan-2,5-dicarbaldehyde / MetspHMFO; columns kcat, Km, kcat/Km; kcat raw_value=6.1 +/- 0.2 raw_unit=min^-1; Km raw_value=6.8 +/- 0.6 raw_unit=mM; kcat/Km raw_value=0.9 +/- 0.1 raw_unit=mM^-1*min^-1

normalized_value_unit_evidence: kcat normalized_value=0.1 normalized_unit=s^-1; Km normalized_value=6.8 normalized_unit=mM; kcat/Km normalized_value=0.014705882352941178 normalized_unit=s^-1*mM^-1


column_label: TABLE 3. Steady-state kinetic constants for the oxidation of vanillyl alcohol, HMF, DFF, and FDCA by HMFOs; row HMF / 5-(hydroxymethyl)furfural / MetspHMFO; columns kcat, Km, kcat/Km; kcat raw_value=82.5 +/- 1.6 raw_unit=min^-1; Km raw_value=9.1 +/- 0.7 raw_unit=mM; kcat/Km raw_value=9.1 +/- 0.8 raw_unit=mM^-1*min^-1

normalized_value_unit_evidence: kcat normalized_value=1.38 normalized_unit=s^-1; Km normalized_value=9.1 normalized_unit=mM; kcat/Km normalized_value=0.15164835164835164 normalized_unit=s^-1*mM^-1


organism: Paenibacillus sp. AIU 311

substrate_name: glyceraldehyde

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

substrate: glyceraldehyde


substrate_name: glycolaldehyde

smiles: C(C=O)O

substrate: glycolaldehyde


enzyme_display_name: L-sorbose oxidase

organism: Trametes sanguinea

proof_lines:
acceptor O2
acceptor 2,6-dichlorophenolindophenol

enzyme: L-sorbose oxidase


enzyme_display_name: pyridoxine 4-oxidase

organism: Pseudomonas sp.

enzyme: pyridoxine 4-oxidase


substrate_name: pyridoxine

substrate: pyridoxine


organism: Mesorhizobium loti

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H460A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant His6-tagged mutant H460A


sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.

proof_lines: pH 8.0, 30°C, recombinant His6-tagged mutant H462A


proof_lines: pH 8.0, 30°C, recombinant His6-tagged wild-type enzyme


organism: Levilactobacillus brevis

substrate_name: Cyclohexanol

proof_lines: fusion protein with phenylacetone monooxygenase, pH 7.5, 25°C

substrate: Cyclohexanol


smiles: O=O


organism: Fungi

substrate_name: hexadecanol

smiles: CCCCCCCCCCCCCCCCO

substrate: hexadecanol


substrate_name: methanol

substrate: methanol


organism: Penicillium purpurescens

substrate_name: ethylene glycol

smiles: C(CO)O

substrate: ethylene glycol


substrate_name: ethanol

substrate: ethanol


organism: Thermoascus aurantiacus

proof_lines:
extracellular enzyme, pH 5.9, 30°C
intracellular enzyme, pH 5.9, 30°C


organism: Aspergillus terreus

substrate_name: n-butanol

substrate: n-butanol


substrate_name: n-Octanol

smiles: CCCCCCCCO

substrate: n-Octanol


organism: Aspergillus ochraceus


organism: Thermoanaerobacter brockii


organism: gamma proteobacterium Y-134

substrate_name: cholesterol

substrate: cholesterol


organism: Streptomyces aegyptia


organism: Schizophyllum commune


organism: Bordetella sp.


organism: Pleurotus ostreatus


organism: Komagataella pastoris

substrate_name: (R,S)-4-methoxybenzyl alcohol

proof_lines: protein fused to peroxidase, linker (GGGGS)12, pH 4, 25°C

proof_lines: protein fused to peroxidase, linker (GGGGS)9, pH 4, 25°C

proof_lines: protein fused to peroxidase, linker (AP)5(GGGGS)1, pH 4, 25°C

substrate: (R,S)-4-methoxybenzyl alcohol


organism: Lentinus sajor-caju

substrate_name: 3,4-dimethoxybenzyl alcohol

proof_lines:
enzyme form VAO II
enzyme form VAO I

substrate: 3,4-dimethoxybenzyl alcohol


organism: Bacillus subtilis


organism: Phanerodontia chrysosporium

substrate_name: Vanillyl alcohol

substrate: Vanillyl alcohol


organism: Phratora vitellinae

substrate_name: 2-hydroxybenzyl alcohol

substrate: 2-hydroxybenzyl alcohol


substrate_name: veratryl alcohol

substrate: veratryl alcohol


organism: Trametes versicolor

substrate_name: 4-methoxybenzyl alcohol

substrate: 4-methoxybenzyl alcohol


enzyme_display_name: L-gulonolactone oxidase

organism: Grifola frondosa

enzyme: L-gulonolactone oxidase


organism: Hypomyces rosellus

substrate_name: 1-O-methyl beta-D-galactopyranoside

proof_lines: Cu(II)-bound H2O is required in the protonated aquo state for catalysis and is responsible for the kinetic solvent isotope effect

substrate: 1-O-methyl beta-D-galactopyranoside


proof_lines: substrate 1-O-methyl-alpha-D-galactopyranoside, 2 H-atoms in position 6 are substituted by D-atoms

proof_lines: substrate oxygen at saturated 1-O-methyl-alpha-D-galactopyranoside concentration, 2 H-atoms in position 6 are substituted by D-atoms


organism: Aspergillus nidulans

substrate_name: O2; D-Galactose

substrate: O2; D-Galactose


organism: Mycobacterium tuberculosis

assay_conditions_summary: cofactor FAD

proof_lines: the FAD-binding motif Rv1771 protein is a metalloenzyme that oxidizes L-gulono-1,4-lactone


substrate_name: D-galactose

substrate: D-galactose


organism: Fusarium acuminatum


organism: Gloeophyllum sepiarium

substrate_name: D-glucose

substrate: D-glucose


organism: Lenzites styracinus


organism: Fusarium sambucinum

substrate_name: melibiose

proof_lines: recombinant His-tagged enzyme, pH 7.0, 30°C

substrate: melibiose


organism: Trametes ochracea

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V546C/T169G to reconstruct the assayed variant sequence.

proof_lines: V546C/T169G mutant, substrate 1,4-benzoquinone (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(

proof_lines: V546C/T169G mutant, substrate 1,4-benzoquinone (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobi


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V546C/T169G/L537W to reconstruct the assayed variant sequence.

proof_lines: V546C/T169G/L537W mutant, substrate 1,4-benzoquinone (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azi

proof_lines: V546C/T169G/L537W mutant, substrate 1,4-benzoquinone (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-a


substrate_name: ferricenium hexafluorophosphate

proof_lines: V546C/T169G/L537W mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay

proof_lines: mutant enzyme V546C/T169G/L537W, at pH 6.5 and 30°C

proof_lines: V546C/T169G/L537W mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled ass

substrate: ferricenium hexafluorophosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V546C/E542K to reconstruct the assayed variant sequence.

proof_lines: V546C/E542K mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay usi

proof_lines: mutant enzyme V546C/E542K, at pH 6.5 and 30°C

proof_lines: V546C/E542K mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using


proof_lines: V546C/T169G mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay usi

proof_lines: mutant enzyme V546C/T169G, at pH 6.5 and 30°C

proof_lines: V546C/T169G mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using


proof_lines: V546C/E542K mutant, substrate 1,4-benzoquinone (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(

proof_lines: V546C/E542K mutant, substrate 1,4-benzoquinone (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobi


proof_lines: V546C/T169G mutant, substrate D-galactose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolin

proof_lines: V546C/T169G mutant, substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolines


proof_lines: V546C/T169G/L537W mutant, substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiaz

proof_lines: V546C/T169G/L537W mutant, substrate D-galactose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthi


proof_lines: V546C/E542K mutant, substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolines

proof_lines: V546C/E542K mutant, substrate D-galactose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolin


proof_lines: substrate 2-methyl-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzt


proof_lines: substrate 2-chloro-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzt


substrate_name: ferricyanide

proof_lines: substrate ferricyanide (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulf

substrate: ferricyanide


substrate_name: D-fructose

proof_lines: substrate D-fructose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as th

proof_lines: substrate L-sorbose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the

substrate: D-fructose


proof_lines: substrate D-galactose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as t

proof_lines: substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the


proof_lines: substrate tetrafluoro-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbe


proof_lines: substrate 2,6-dimethyl-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylb


proof_lines: substrate 2-methoxy-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenz


substrate_name: D-xylose

proof_lines: substrate D-xylose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) as the

substrate: D-xylose


proof_lines: substrate 2,6-dichloroindophenol (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthia


proof_lines: substrate O2 (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid)


proof_lines: substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethy


proof_lines: substrate 1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2'-azinobis(3-ethylbenzthiazoline


sequence_variant_note: Mutation signature F454A/S455A/Y456A/H2P could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 6.5; buffer 50 mM KH2PO4

proof_lines: mutant enzyme F454A/S455A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


substrate_name: D-melibiose

substrate: D-melibiose


sequence_variant_note: Mutation signature F454P/H2P could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme F454P, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


sequence_variant_note: Mutation signature F454A/Y456A/H2P could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme F454A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +29, so it is treated as a source-provided variant sequence.

proof_lines: mutant enzyme F454N, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


proof_lines: mutant enzyme F454A/S455A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454A/S455A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +30, so it is treated as a source-provided variant sequence.

proof_lines: mutant enzyme Y456W, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


sequence_variant_note: Mutation signature H450Q/H2P could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme H450Q, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


proof_lines: mutant enzyme F454P, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454P, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


proof_lines: mutant enzyme F454N, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454N, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


proof_lines: mutant enzyme F454A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


substrate_name: ferrocenium hexafluorophosphate

substrate: ferrocenium hexafluorophosphate


proof_lines: mutant enzyme H450Q, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme H450Q, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


proof_lines: mutant enzyme Y456W, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme Y456W, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


proof_lines: wild type enzyme, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: wild-type, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: wild-type, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


proof_lines: mutant enzyme F454A/S455A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


proof_lines: wild type enzyme, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E542R to reconstruct the assayed variant sequence.

proof_lines: E542R mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: E542R mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L537G/E542K to reconstruct the assayed variant sequence.

proof_lines: L537G/E542K mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537G/E542K mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L537G/E542R to reconstruct the assayed variant sequence.

proof_lines: L537G/E542R mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537G/E542R mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L537W/E542R to reconstruct the assayed variant sequence.

proof_lines: L537W/E542R mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537W/E542R mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L537W/E542K to reconstruct the assayed variant sequence.

proof_lines: L537W/E542K mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537W/E542K mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L537G to reconstruct the assayed variant sequence.

proof_lines: L537G mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537G mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E542K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; buffer 50 mM phosphate

proof_lines: E542K mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: mutant enzyme E542K, in 50 mM phosphate buffer (pH 6.5) at 60°C

proof_lines: E542K mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L537W to reconstruct the assayed variant sequence.

proof_lines: L537W mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537W mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


proof_lines: E542R mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


proof_lines: L537G mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537G mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


proof_lines: L537G/E542K mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5

proof_lines: L537G/E542K mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,


proof_lines: L537G/E542R mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5

proof_lines: L537G/E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,


proof_lines: L537W/E542R mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5

proof_lines: L537W/E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,


proof_lines: L537W/E542K mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5

proof_lines: L537W/E542K mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,


proof_lines: L537W mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537W mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


proof_lines: E542K mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: E542K mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


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

proof_lines: wild type enzyme, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


proof_lines: mutant enzyme H450Q, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme H450Q, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


organism: Phlebiopsis gigantea

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K312E to reconstruct the assayed variant sequence.

proof_lines: pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E540K to reconstruct the assayed variant sequence.

proof_lines: pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag


substrate_name: L-sorbose

substrate: L-sorbose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V546G/T169G to reconstruct the assayed variant sequence.

proof_lines: V546G/T169G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: V546G/T169G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V546P/T169G to reconstruct the assayed variant sequence.

proof_lines: V546P/T169G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: V546P/T169G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H548R with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: H548R, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: H548R, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q448N to reconstruct the assayed variant sequence.

proof_lines: Q448N, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: Q448N, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q448C to reconstruct the assayed variant sequence.

proof_lines: Q448C, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: Q448C, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V546C/T169N to reconstruct the assayed variant sequence.

proof_lines: V546C/T169N, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: V546C/T169N, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q448S to reconstruct the assayed variant sequence.

proof_lines: Q448S, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: Q448S, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N593R with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: N593R, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: N593R, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V546P to reconstruct the assayed variant sequence.

proof_lines: V546P, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: V546P, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R472L to reconstruct the assayed variant sequence.

proof_lines: R472L, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: R472L, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R472G to reconstruct the assayed variant sequence.

proof_lines: R472G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: R472G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H548I with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: H548I, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: H548I, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V546G to reconstruct the assayed variant sequence.

proof_lines: V546G, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: V546G, mutant, substrate D-glucose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V546C to reconstruct the assayed variant sequence.

proof_lines: V546C, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: mutant enzyme V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C

proof_lines: mutant enzyme V546C, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M103S to reconstruct the assayed variant sequence.

smiles: CC(CO)O

column_label: Table 3 row (R)-1,2-Propanediol; column group M103S; metric columns KM, kcat, kcat/KM.

normalized_value_unit_evidence: kcat=0.4 s^-1; KM=110 mM; kcat_over_km=0.0036363636363636364 s^-1 mM^-1 from Table 3 kcat/KM; printed table cell 4 M^-1 s^-1 (= 0.004 s^-1 mM^-1) is rounded

raw_value_unit_evidence: Table 3 row (R)-1,2-Propanediol; M103S columns: KM=110 mM, kcat=0.4 s^-1, kcat/KM=4 M^-1 s^-1.

table_label: Table 3 - Apparent Steady-State Kinetic Parameters for PcAOX


substrate_name: methanol

column_label: Table 3 row methanol; column group M103S; metric columns KM, kcat, kcat/KM.

normalized_value_unit_evidence: kcat=1 s^-1; KM=2 mM; kcat_over_km=0.5 s^-1 mM^-1 from Table 3 kcat/KM; printed table cell 500 M^-1 s^-1 (= 0.5 s^-1 mM^-1) is rounded

raw_value_unit_evidence: Table 3 row methanol; M103S columns: KM=2 mM, kcat=1 s^-1, kcat/KM=500 M^-1 s^-1.

row_label: methanol

substrate: methanol


substrate_name: ethanol

column_label: Table 3 row ethanol; column group M103S; metric columns KM, kcat, kcat/KM.

normalized_value_unit_evidence: kcat=1 s^-1; KM=1 mM; kcat_over_km=1.0 s^-1 mM^-1 from Table 3 kcat/KM; printed table cell 1000 M^-1 s^-1 (= 1.0 s^-1 mM^-1) is rounded

raw_value_unit_evidence: Table 3 row ethanol; M103S columns: KM=1 mM, kcat=1 s^-1, kcat/KM=1000 M^-1 s^-1.

row_label: ethanol

substrate: ethanol


column_label: Table 3 row 1-propanol; column group M103S; metric columns KM, kcat, kcat/KM.

raw_value_unit_evidence: Table 3 row 1-propanol; M103S columns: KM=2 mM, kcat=1 s^-1, kcat/KM=500 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F101S to reconstruct the assayed variant sequence.

column_label: Table 3 row methanol; column group F101S; metric columns KM, kcat, kcat/KM.

normalized_value_unit_evidence: kcat=4 s^-1; KM=2 mM; kcat_over_km=2.0 s^-1 mM^-1 from Table 3 kcat/KM; printed table cell 2000 M^-1 s^-1 (= 2.0 s^-1 mM^-1) is rounded

raw_value_unit_evidence: Table 3 row methanol; F101S columns: KM=2 mM, kcat=4 s^-1, kcat/KM=2000 M^-1 s^-1.


column_label: Table 3 row (R)-1,2-Propanediol; column group F101S; metric columns KM, kcat, kcat/KM.

normalized_value_unit_evidence: kcat=4 s^-1; KM=110 mM; kcat_over_km=0.03636363636363636 s^-1 mM^-1 from Table 3 kcat/KM; printed table cell 36 M^-1 s^-1 (= 0.036 s^-1 mM^-1) is rounded

raw_value_unit_evidence: Table 3 row (R)-1,2-Propanediol; F101S columns: KM=110 mM, kcat=4 s^-1, kcat/KM=36 M^-1 s^-1.


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

column_label: PMID 30272958 Table 3; row (R)-1,2-Propanediol; column group wild-type; KM/kcat/kcat/KM cells: KM >1600 mM; kcat >5 s^-1; kcat/KM >3 M^-1 s^-1.

normalized_value_unit_evidence: KM >1600 mM; kcat >5 s^-1; kcat/KM >0.003 s^-1 mM^-1 (inequality/lower-bound cells)

row_label: (R)-1,2-Propanediol / wild-type

table_label: PMID 30272958 Table 3. Apparent Steady-State Kinetic Parameters for PcAOX


column_label: Table 3 row ethanol; column group F101S; metric columns KM, kcat, kcat/KM.

normalized_value_unit_evidence: kcat=5 s^-1; KM=1 mM; kcat_over_km=5.0 s^-1 mM^-1 from Table 3 kcat/KM; printed table cell 5000 M^-1 s^-1 (= 5.0 s^-1 mM^-1) is rounded

raw_value_unit_evidence: Table 3 row ethanol; F101S columns: KM=1 mM, kcat=5 s^-1, kcat/KM=5000 M^-1 s^-1.


column_label: Table 3 row 1-propanol; column group F101S; metric columns KM, kcat, kcat/KM.

normalized_value_unit_evidence: kcat=7 s^-1; KM=4 mM; kcat_over_km=1.75 s^-1 mM^-1 from Table 3 kcat/KM; printed table cell 1800 M^-1 s^-1 (= 1.8 s^-1 mM^-1) is rounded

raw_value_unit_evidence: Table 3 row 1-propanol; F101S columns: KM=4 mM, kcat=7 s^-1, kcat/KM=1800 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F101N to reconstruct the assayed variant sequence.

column_label: Table 3 row methanol; column group F101N; metric columns KM, kcat, kcat/KM.

normalized_value_unit_evidence: kcat=10 s^-1; KM=14 mM; kcat_over_km=0.7142857142857143 s^-1 mM^-1 from Table 3 kcat/KM; printed table cell 710 M^-1 s^-1 (= 0.71 s^-1 mM^-1) is rounded

raw_value_unit_evidence: Table 3 row methanol; F101N columns: KM=14 mM, kcat=10 s^-1, kcat/KM=710 M^-1 s^-1.


column_label: Table 3 row ethanol; column group F101N; metric columns KM, kcat, kcat/KM.

normalized_value_unit_evidence: kcat=10 s^-1; KM=11 mM; kcat_over_km=0.9090909090909091 s^-1 mM^-1 from Table 3 kcat/KM; printed table cell 910 M^-1 s^-1 (= 0.91 s^-1 mM^-1) is rounded

raw_value_unit_evidence: Table 3 row ethanol; F101N columns: KM=11 mM, kcat=10 s^-1, kcat/KM=910 M^-1 s^-1.


column_label: PMID 30272958 Table 3; row 1-propanol; column group wild-type; KM/kcat/kcat/KM cells: KM 45 mM; kcat 11 s^-1; kcat/KM 240 M^-1 s^-1.

row_label: 1-propanol / wild-type


column_label: Table 3 row 1-propanol; column group F101N; metric columns KM, kcat, kcat/KM.

normalized_value_unit_evidence: kcat=12 s^-1; KM=11 mM; kcat_over_km=1.0909090909090908 s^-1 mM^-1 from Table 3 kcat/KM; printed table cell 1100 M^-1 s^-1 (= 1.1 s^-1 mM^-1) is rounded

raw_value_unit_evidence: Table 3 row 1-propanol; F101N columns: KM=11 mM, kcat=12 s^-1, kcat/KM=1100 M^-1 s^-1.


column_label: Table 3 row (R)-1,2-Propanediol; column group F101N; metric columns KM, kcat, kcat/KM.

normalized_value_unit_evidence: kcat=13 s^-1; KM=1200 mM; kcat_over_km=0.010833333333333334 s^-1 mM^-1 from Table 3 kcat/KM; printed table cell 11 M^-1 s^-1 (= 0.011 s^-1 mM^-1) is rounded

raw_value_unit_evidence: Table 3 row (R)-1,2-Propanediol; F101N columns: KM=1200 mM, kcat=13 s^-1, kcat/KM=11 M^-1 s^-1.


column_label: PMID 30272958 Table 3; row methanol; column group wild-type; KM/kcat/kcat/KM cells: KM 2 mM; kcat 18 s^-1; kcat/KM 9000 M^-1 s^-1.

normalized_value_unit_evidence: KM 2 mM; kcat 18 s^-1; kcat/KM 9 s^-1 mM^-1

row_label: methanol / wild-type


column_label: PMID 30272958 Table 3; row ethanol; column group wild-type; KM/kcat/kcat/KM cells: KM 15 mM; kcat 19 s^-1; kcat/KM 1300 M^-1 s^-1.

row_label: ethanol / wild-type


substrate_name: D-cellobiose

substrate: D-cellobiose


substrate_name: D-maltoheptaose

substrate: D-maltoheptaose


substrate_name: D-maltopentaose

substrate: D-maltopentaose


substrate_name: D-fucose

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

substrate: D-fucose


substrate_name: D-maltotriose

substrate: D-maltotriose


substrate_name: D-trehalose

substrate: D-trehalose


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

smiles: CCCCCCO

column_label: Table 2 columns Substrate/KM/KI/kcat/kcat/KM, row Compound 9; table footnote [a] says HRP-coupled assay in 50 mM potassium phosphate pH 7.5 and units KM=mM, kcat=s^-1, kcat/KM=M^-1 s^-1.

raw_value_unit_evidence: Table 2 Compound 9: Km=3.0 mM; kcat=0.56 s^-1; kcat/KM=187 M^-1 s^-1.

row_label: Compound 9

table_label: Table 2: Apparent steady-state kinetic parameters for AOX*


substrate_name: diethylene glycol

smiles: C(COCCO)O

column_label: Table 2 columns Substrate/KM/KI/kcat/kcat/KM, row Compound 4; table footnote [a] says HRP-coupled assay in 50 mM potassium phosphate pH 7.5 and units KM=mM, kcat=s^-1, kcat/KM=M^-1 s^-1.

row_label: Compound 4

substrate: diethylene glycol


smiles: CC(CCCO)O

column_label: Table 2 columns Substrate/KM/KI/kcat/kcat/KM, row Compound 2; table footnote [a] says HRP-coupled assay in 50 mM potassium phosphate pH 7.5 and units KM=mM, kcat=s^-1, kcat/KM=M^-1 s^-1.

row_label: Compound 2


smiles: C(CCO)CCO

column_label: Table 2 columns Substrate/KM/KI/kcat/kcat/KM, row Compound 3; table footnote [a] says HRP-coupled assay in 50 mM potassium phosphate pH 7.5 and units KM=mM, kcat=s^-1, kcat/KM=M^-1 s^-1.

row_label: Compound 3


smiles: C(CSCCO)O

column_label: Table 2 columns Substrate/KM/KI/kcat/kcat/KM, row Compound 5; table footnote [a] says HRP-coupled assay in 50 mM potassium phosphate pH 7.5 and units KM=mM, kcat=s^-1, kcat/KM=M^-1 s^-1.

raw_value_unit_evidence: Table 2 Compound 5: Km=119 mM; kcat=3.56 s^-1; kcat/KM=29.9 M^-1 s^-1.

row_label: Compound 5


smiles: C(CCCO)CCO

column_label: Table 2 columns Substrate/KM/KI/kcat/kcat/KM, row Compound 6; table footnote [a] says HRP-coupled assay in 50 mM potassium phosphate pH 7.5 and units KM=mM, kcat=s^-1, kcat/KM=M^-1 s^-1.

raw_value_unit_evidence: Table 2 Compound 6: Km=12.9 mM; kcat=4.07 s^-1; kcat/KM=316 M^-1 s^-1.

row_label: Compound 6


smiles: C(CCO)CO

column_label: Table 2 columns Substrate/KM/KI/kcat/kcat/KM, row Compound 1; table footnote [a] says HRP-coupled assay in 50 mM potassium phosphate pH 7.5 and units KM=mM, kcat=s^-1, kcat/KM=M^-1 s^-1.

raw_value_unit_evidence: Table 2 Compound 1: Km=198 mM; kcat=6.74 s^-1; kcat/KM=34.1 M^-1 s^-1.

row_label: Compound 1


proof_lines:
pH 6.5, substrate: D-glucose
at pH 6.5 and 30°C
pH 4.5, substrate: D-glucose


proof_lines:
pH 6.5, substrate: D-glucose
at pH 6.5 and 30°C


proof_lines:
pH 4.5, substrate: D-glucose
at pH 4.5 and 30°C
pH 6.5, substrate: D-glucose


proof_lines:
pH 4.5, substrate: D-glucose
pH 6.5, substrate: D-glucose


substrate_name: L-arabinose

assay_conditions_summary: pH 10.5; buffer the publication 100 mM ethanolamine

proof_lines: pH and temperature not specified in the publication

substrate: L-arabinose


organism: Fusarium sp.

substrate_name: guar

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

assay_conditions_summary: pH 7

substrate: guar


proof_lines:
mutant Y436H/v494A, pH 7.0, 25°C
mutant Y436H, pH 7.0, 25°C


substrate_name: D-galactose

proof_lines:
mutant Y436H, pH 7.0, 25°C
mutant Y436H/v494A, pH 7.0, 25°C

substrate: D-galactose


organism: Streptomyces sp. SA-COO

substrate_name: cholesterol

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12676 and applied mutation signature A32C/S129C/T371C/A423C with inferred residue-numbering offset +37 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 310.15 K; buffer 50 mM sodium phosphate

column_label: Table 1: Michaelis-Menten Constants and Tryptophan Fluorescence Emission Maxima for Wild-Type ChoA and ChoA Mutants (Biochemistry 2018, 57(36):5370-5378); Table 1, row 'mutant 3, A32C/S129C/T371C/A423C'; column 'kcat (s^-1)' prints 23; column 'Km (uM)' prints 11; column 'kcat/Km (M^-1 s^-1)' prints 2.0 x 10^6; column 'lambda-max Trp (nm)' prints 332.

normalized_value_unit_evidence: kcat: printed Table 1 cell 23 s^-1; already in s^-1, no conversion; the exported value is 23.0 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 11 uM; 11 / 1000 = 0.011 mM; the exported value is 0.011 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 2.0 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.0 x 10^6 / 1000 = 2000.0 s^-1 mM^-1. The exported ratio is 2090.909090909091 s^(-1)*mM^(-1), which is the quotient 23.0 / 0.011 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 2000.0 and kcat and Km are unchanged.

substrate: cholesterol


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12676 and applied mutation signature A32C/T168C/S312C/A465C with inferred residue-numbering offset +37 to reconstruct the assayed variant sequence.

column_label: Table 1: Michaelis-Menten Constants and Tryptophan Fluorescence Emission Maxima for Wild-Type ChoA and ChoA Mutants (Biochemistry 2018, 57(36):5370-5378); Table 1, row 'mutant 7, A32C/T168C/S312C/A465C'; column 'kcat (s^-1)' prints 30; column 'Km (uM)' prints 12; column 'kcat/Km (M^-1 s^-1)' prints 2.4 x 10^6; column 'lambda-max Trp (nm)' prints 328.

normalized_value_unit_evidence: kcat: printed Table 1 cell 30 s^-1; already in s^-1, no conversion; the exported value is 30.0 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 12 uM; 12 / 1000 = 0.012 mM; the exported value is 0.012 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 2.4 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.4 x 10^6 / 1000 = 2400.0 s^-1 mM^-1. The exported ratio is 2500.0 s^(-1)*mM^(-1), which is the quotient 30.0 / 0.012 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 2400.0 and kcat and Km are unchanged.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12676 and applied mutation signature A184C/A301C/T394C with inferred residue-numbering offset +37 to reconstruct the assayed variant sequence.

column_label: Table 1: Michaelis-Menten Constants and Tryptophan Fluorescence Emission Maxima for Wild-Type ChoA and ChoA Mutants (Biochemistry 2018, 57(36):5370-5378); Table 1, row 'mutant 8, A184C/A301C/T394C'; column 'kcat (s^-1)' prints 57; column 'Km (uM)' prints 11; column 'kcat/Km (M^-1 s^-1)' prints 5.0 x 10^6; column 'lambda-max Trp (nm)' prints 329.

normalized_value_unit_evidence: kcat: printed Table 1 cell 57 s^-1; already in s^-1, no conversion; the exported value is 57.0 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 11 uM; 11 / 1000 = 0.011 mM; the exported value is 0.011 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 5.0 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.0 x 10^6 / 1000 = 5000.0 s^-1 mM^-1. The exported ratio is 5181.818181818182 s^(-1)*mM^(-1), which is the quotient 57.0 / 0.011 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 5000.0 and kcat and Km are unchanged.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A184C/T239C/A407C/A465C with inferred residue-numbering offset +37 to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 37°C, mutant enzyme A184C/T239C/A407C/A465C, cholesterol solubilized in detergent micelles as a substrate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12676 and applied mutation signature S153C/A205C/S312C/T435C with inferred residue-numbering offset +37 to reconstruct the assayed variant sequence.

column_label: Table 1: Michaelis-Menten Constants and Tryptophan Fluorescence Emission Maxima for Wild-Type ChoA and ChoA Mutants (Biochemistry 2018, 57(36):5370-5378); Table 1, row 'mutant 4, S153C/A205C/S312C/T435C'; column 'kcat (s^-1)' prints 68; column 'Km (uM)' prints 10; column 'kcat/Km (M^-1 s^-1)' prints 7.0 x 10^6; column 'lambda-max Trp (nm)' prints 328.

normalized_value_unit_evidence: kcat: printed Table 1 cell 68 s^-1; already in s^-1, no conversion; the exported value is 68.0 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 10 uM; 10 / 1000 = 0.01 mM; the exported value is 0.01 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 7.0 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.0 x 10^6 / 1000 = 7000.0 s^-1 mM^-1. The exported ratio is 6800.0 s^(-1)*mM^(-1), which is the quotient 68.0 / 0.01 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 7000.0 and kcat and Km are unchanged.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12676 and applied mutation signature L274C with inferred residue-numbering offset +37 to reconstruct the assayed variant sequence.

column_label: Table 1: Michaelis-Menten Constants and Tryptophan Fluorescence Emission Maxima for Wild-Type ChoA and ChoA Mutants (Biochemistry 2018, 57(36):5370-5378); Table 1, row 'mutant 2, L274C'; column 'kcat (s^-1)' prints 75; column 'Km (uM)' prints 17; column 'kcat/Km (M^-1 s^-1)' prints 4.5 x 10^6; column 'lambda-max Trp (nm)' prints 328.

normalized_value_unit_evidence: kcat: printed Table 1 cell 75 s^-1; already in s^-1, no conversion; the exported value is 75.0 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 17 uM; 17 / 1000 = 0.017 mM; the exported value is 0.017 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 4.5 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.5 x 10^6 / 1000 = 4500.0 s^-1 mM^-1. The exported ratio is 4411.764705882352 s^(-1)*mM^(-1), which is the quotient 75.0 / 0.017 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 4500.0 and kcat and Km are unchanged.

row_label: Table 1, row 'mutant 2, L274C'