organism: Trametes sp.

substrate_name: D-glucose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T166A/E539K to reconstruct the assayed variant sequence.

substrate: D-glucose


enzyme_display_name: pyranose oxidase

source_db: brenda

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

data_origin: experimental

enzyme: pyranose oxidase

status: unverified

source: brenda


sequence_variant_note: Mutation signature E359K could not be applied safely because the resolved sequence does not match the expected reference residue(s).

mutation_type: substitution


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K312E/E539K to reconstruct the assayed variant sequence.


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


enzyme_display_name: cholesterol oxidase

organism: Brevibacterium sterolicum

substrate_name: cholesterol

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

sequence_source: multiple

assay_conditions_summary: pH 7.5; buffer product formation followed

proof_lines: assay relies on spectroscopic detection of 4-cholesten-3-one formation, decreasing length of C17 chain affects turnover negatively

proof_lines: substrate cholesterol, polarographic determination of the rate of oxygen consumption. 1% thesit (polyoxyethylene(9)-lauryl-ether), 10% propan-2-ol and 50 mM phosphate, 25°C and pH 7.5

source_databases_merged: brenda skid

enzyme: cholesterol oxidase

substrate: cholesterol


assay_conditions_summary: pH 7.5; buffer H2O2 production assayed

proof_lines: assay relies on detection of H2O2 formation

proof_lines: product formation followed at 240 nm in the presence of 0.02 ml H2O2, substrate dissolved in Triton X-100, 100 mM phosphate buffer

proof_lines: H2O2 production assayed, 100 mM phosphate buffer


substrate_name: pregnenolone

assay_conditions_summary: pH 7.5; buffer substrate pregnenolone

proof_lines: assay relies on spectroscopic detection of 4-cholesten-3-one formation

proof_lines: substrate pregnenolone, detection of product formation at 240 nm. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5

substrate: pregnenolone


substrate_name: cholestanol

assay_conditions_summary: pH 7.5; buffer substrate cholestanol

proof_lines: substrate cholestanol, rate of H2O2 formation detected with o-dianisidine and horseradish peroxidase. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5

substrate: cholestanol


organism: Trametes ochracea

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N593C with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N593C, with O2 as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme N593C, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme N593C, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q448H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q448H, with O2 as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme Q448H, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme Q448H, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L547R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L547R, with O2 as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme L547R, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme L547R, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L545C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L545C, with O2 as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme L545C, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme L545C, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T166R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T166R, with O2 as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme T166R, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme T166R, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C


organism: Streptomyces sp.

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

assay_conditions_summary: pH 7

proof_lines: mutant enzyme N485D, determined by H2O2 detection

proof_lines: mutant enzyme N485D, determined by cholest-4-en-3-one detection

proof_lines: apparent value, mutant enzyme N485D, pH 7.0, temperature not specified in the publication


proof_lines: mutant enzyme G347N, determined by H2O2 detection

proof_lines: mutant enzyme G347N, determined by cholest-4-en-3-one detection


proof_lines: mutant enzyme F359W, determined by cholest-4-en-3-one detection

proof_lines: mutant enzyme F359W, determined by H2O2 detection


kcat_display: Not reported

kcat_over_km_display: Not reported

smiles: O=O


enzyme_display_name: aryl-alcohol oxidase

organism: Aspergillus terreus

substrate_name: benzyl alcohol

assay_conditions_summary: pH 6

proof_lines:
recombinant enzyme, at pH 6.0 and 30°C
pH 8.0, 30°C

enzyme: aryl-alcohol oxidase

substrate: benzyl alcohol


substrate_name: 3,4-dimethoxybenzyl alcohol

verification_status: corrected

assay_conditions_summary: pH 6; buffer 0.1 M sodium phosphate

column_label: Table 2 row Veratryl alcohol columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); explicit required kcat/Km cell does not match expected value.

raw_value_unit_evidence: Expected substrate 3,4-dimethoxybenzyl alcohol maps to paper row Veratryl alcohol: Km 4.91 mM, kcat 6925.42 min^-1, kcat/Km 1410.47 min^-1 mM^-1. The expected values instead match paper row m-anisyl alcohol / 3-methoxybenzyl alcohol.

row_label: Veratryl alcohol

table_label: Table 2. Steady-state kinetic parameters of in-vitro refolded recombinant alcohol oxidase from E. coli.

substrate: 3,4-dimethoxybenzyl alcohol

status: corrected


substrate_name: 3-Methoxybenzyl alcohol

column_label: Table 2 row m-anisyl alcohol reports Km 2.88 mM, kcat 6341.70 min^-1, and kcat/Km 2201.98 min^-1 mM^-1; the expected values instead align with the Veratryl alcohol row.

raw_value_unit_evidence: m-anisyl alcohol row: Km raw_value=2.88 raw_unit=mM; kcat raw_value=6341.70 raw_unit=min^-1; kcat/Km raw_value=2201.98 raw_unit=min^-1 mM^-1. Veratryl alcohol row: Km raw_value=4.91 raw_unit=mM; kcat raw_value=6925.42 raw_unit=min^-1; kcat/Km raw_value=1410.47 raw_unit=min^-1 mM^-1.

row_label: m-anisyl alcohol / 3-methoxybenzyl alcohol

table_label: PMC3994049 Table 2

substrate: 3-Methoxybenzyl alcohol


substrate_name: 4-methoxybenzyl alcohol

column_label: Table 2 row p-anisyl alcohol, columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1), raw cells 1.08, 8455.86, and 7829.50, normalized to 1.08 mM, 140.931 s^(-1), and 130.4916666667 s^(-1)*mM^(-1)

normalized_value_unit_evidence: Km normalized_value=1.08 normalized_unit=mM; kcat normalized_value=140.931 normalized_unit=s^(-1); kcat/Km normalized_value=130.4916666667 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Km raw_value=1.08 mM raw_unit=mM raw_cell=1.08; kcat raw_value=8455.86 min^-1 raw_unit=min^-1 raw_cell=8455.86; kcat/Km raw_value=7829.50 min^-1 mM^-1 raw_unit=min^-1 mM^-1 raw_cell=7829.50

row_label: p-anisyl alcohol

substrate: 4-methoxybenzyl alcohol


km_display: Not reported

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H167A/H548R to reconstruct the assayed variant sequence.

proof_lines:
pH 6.0, 25°C, mutant H167A/H548R
pH 7.0, 25°C, mutant H167A/H548R
pH 8.0, 25°C, mutant H167A/H548R


substrate_name: D-galactose

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

assay_conditions_summary: pH 7; buffer 50 mM KH2PO4

proof_lines: pH 7.0, 25°C, reductive half-reaction, wild-type enzyme

proof_lines: wild type enzyme, in 50 mM sodium phosphate (pH 7.0), at 25°C

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

substrate: D-galactose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T169S to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 25°C, reductive half-reaction, mutant T169S

proof_lines: T169S, mutant, substrate D-galactose, 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: mutant enzyme T169S, in 50 mM sodium phosphate (pH 7.0), at 25°C


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

proof_lines: pH 7.0, 25°C, reductive half-reaction, mutant T169N

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

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


proof_lines: mutant enzyme T169G, pH and temperature not specified in the publication

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

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


proof_lines: mutant enzyme T196G/V546C, pH and temperature not specified in the publication


proof_lines: mutant enzyme H167A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q286R to reconstruct the assayed variant sequence.


enzyme_display_name: Cholesterol oxidase

organism: Streptomyces sp. (strain SA-COO)

source_db: uniprot

proof_lines: kcat is 44 sec(-1) for the oxidation of cholesterol. kcat is 64 sec(-1) for the isomerization of cholest-5-en-3-one.

enzyme: Cholesterol oxidase

source: uniprot


assay_conditions_summary: pH 6.5; buffer 50 mM phosphate

proof_lines: mutant enzyme H450G/E542K/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C


proof_lines: mutant enzyme H450G, in 50 mM phosphate buffer (pH 6.5) at 60°C

proof_lines: mutant enzyme H450G, pH and temperature not specified in the publication


proof_lines: mutant enzyme H450G/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C

proof_lines: mutant enzyme H450G/V546C, pH and temperature not specified in the publication


proof_lines: mutant enzyme T169A, in 50 mM sodium phosphate (pH 7.0), at 4°C

proof_lines: mutant enzyme T169A, in 50 mM sodium phosphate (pH 7.0), at 25°C


proof_lines: wild type enzyme, using D-galactose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 25°C

proof_lines: wild type enzyme, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C

source_databases_merged: brenda oed

source_db: oed


proof_lines: mutant enzyme T169S, using D-galactose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 25°C

proof_lines: mutant enzyme T169S, using D-glucose as cosubstrate ,in 50 mM sodium phosphate (pH 7.0), at 4°C

proof_lines: mutant enzyme T169S, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C


proof_lines: mutant enzyme T169A, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C

proof_lines: mutant enzyme T169A, using D-galactose as cosubstrate,in 50 mM sodium phosphate (pH 7.0), at 25°C


proof_lines: mutant enzyme T169N, using D-galactose as cosubstrate,in 50 mM sodium phosphate (pH 7.0), at 25°C

proof_lines: mutant enzyme T169N, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C


proof_lines: mutant enzyme T169G, using D-galactose as cosubstrate,in 50 mM sodium phosphate (pH 7.0), at 25°C

proof_lines: mutant enzyme T169G, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H447E/E361Q with inferred residue-numbering offset +37 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H447Q/E361Q with inferred residue-numbering offset +37 to reconstruct the assayed variant sequence.


organism: Lyophyllum shimeji

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

column_label: LsP2Ox row DCIP; columns Km [mM], kcat [s^-1], and kcat/Km [mM^-1 s^-1] report Km 0.187 mM; kcat 67.3 s^-1; kcat/Km 361 mM^-1 s^-1.

row_label: LsP2Ox row DCIP

table_label: Table 4. Apparent kinetic constants for electron acceptor substrates


column_label: LsP2Ox row BQ; columns Km [mM], kcat [s^-1], and kcat/Km [mM^-1 s^-1] report Km 0.033 mM; kcat 92.3 s^-1; kcat/Km 2760 mM^-1 s^-1.

row_label: LsP2Ox row BQ


assay_conditions_summary: pH 7.5; buffer 50 mM phosphate

proof_lines: H69A mutant enzyme, steady state, 50 mM phosphate buffer, 1% thesit, 1% 2-propanol

proof_lines: H69A mutant enzyme, cholesterol oxidation, 50 mM phosphate buffer, 1% thesit, 1% 2-propanol

proof_lines: H69A mutant enzyme, 50 mM phosphate buffer, pH 7.5, 1% thesit, 1% 2-propanol


assay_conditions_summary: buffer 50 mM phosphate

proof_lines: H69A mutant enzyme, 5-cholesten-3-one isomerization, 50 mM phosphate buffer, 1% thesit, 1% 2-propanol


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V191A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N485L with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines: apparent value, mutant enzyme N485L, pH 5.1, temperature not specified in the publication

proof_lines: apparent value, mutant enzyme N485L, pH 7.0, temperature not specified in the publication


organism: Phanerodontia chrysosporium

verification_status: verified

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

assay_conditions_summary: pH 8

column_label: Table 5, row 2-Deoxy-D-glucose, Km (mM) column: 55.0 +/- 1.4.

raw_value_unit_evidence: Table 5 row 2-Deoxy-D-glucose, Km=55.0 +/- 1.4 mM.

table_label: Table 5, PDF page 5 / printed page 512

source_databases_merged: brenda uniprot

status: verified


substrate_name: maltose

column_label: Table 5, row Maltose, Km (mM) column: 257.0 +/- 10.0.

raw_value_unit_evidence: Table 5 row Maltose, Km=257.0 +/- 10.0 mM. Kinetic-properties prose qualification: the maltose result must be interpreted with care because the substrate contained trace glucose as measured by HPLC; TLC detection of the corresponding oxidation product was negative; the authors state that the trace glucose could not account for the high H2O2-production rate.

row_label: Maltose

substrate: maltose


organism: Mycolicibacterium neoaurum

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


mutation_signature: stopped-flow measurement / stopped-flow measurement

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

mutation_type: truncation

proof_lines: isomerization to 4-cholesten-3-one, rapid reaction, stopped-flow measurement, 500 mM phosphate buffer, pH 7.5, in the presence of 1% thesit and 1.25% 2-propanol


organism: Bacillus sp. (in: firmicutes)

proof_lines:
pH 7, 30°C, enzyme CO2
pH 7, 30°C, enzyme CO1


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F454A with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


organism: Brevibacterium sp.

proof_lines: non-tagged recombinant enzyme, pH 7.2, 37°C

proof_lines: N-terminally His-tagged recombinant enzyme , pH 7.2, 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T169G/E542K/V546C to reconstruct the assayed variant sequence.

proof_lines: T169G/E542K/V546C, mutant, 30°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay

proof_lines: T169G/E542K/V546C, mutant, 30°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay

proof_lines: T169G/E542K/V546C, mutant, 50°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) assay


assay_conditions_summary: pH 5

proof_lines: soluble enzyme, 500 mM glucose used as electron acceptor, pH 5.0


proof_lines: pH 5.5, substrate D-glucose, measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C

proof_lines: pH 7.5, substrate D-glucose, measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C

proof_lines: pH 6.5, substrate D-glucose, measuring oxygen consumption (computer-interfaced Oxy-32 oxygen-monitoring system), 30°C


proof_lines: substrate 1,4-benzoquinone (100 mM D-glucose), pH 4.5

proof_lines: substrate D-glucose (air saturated), pH 6.5


substrate_name: trans-androsterone

assay_conditions_summary: pH 7.5; buffer o-dianisidine/horseradish peroxidase under phosphate

proof_lines: substrate trans-androsterone, rate of H2O2 formation detected with o-dianisidine and horseradish peroxidase. 0.1 M potassium phosphate, 1% Triton X-100, 1.25% propan-2-ol, 25°C and pH 7.5

substrate: trans-androsterone


substrate_name: ferrocenium hexafluorophosphate

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).

substrate: ferrocenium hexafluorophosphate

source: oed


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.


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


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


column_label: Table 4; row label Wild-type | Fc+/Glc; column label relevant Km, kcat, and kcat/Km columns; raw value cells K m[Fc+] 400 ± 110 μM, kcat[Fc+/Glc] 210 ± 30 s^-1, kcat[Fc+/Glc]/Km[Fc+] 0.51 × 10^6 M^-1 s^-1

normalized_value_unit_evidence: Paper central values normalize to kcat 210.0 s^-1, Km 0.4 mM, and explicit kcat/Km 510.0 s^-1 mM^-1. Explicit paper kcat/Km is 510 s^-1 mM^-1; export carries 525.0 from central-cell division, so not strict exact.

raw_value_unit_evidence: Table 4, row Wild-type | Fc+/Glc; columns: K m[Fc+] 400 ± 110 μM; kcat[Fc+/Glc] 210 ± 30 s^-1; kcat[Fc+/Glc]/Km[Fc+] 0.51 × 10^6 M^-1 s^-1.

row_label: Wild-type | Fc+/Glc

table_label: Table 4


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.


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).


organism: Coprinopsis cinerea

substrate_name: 4-anisyl alcohol

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A2Z5WP81 and applied mutation signature L416W to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; buffer 50 mM potassium phosphate

column_label: Table 2 (Steady-state kinetic constants of rCcAAO and the mutants), body row 'p-Anisyl alcohol' with enzyme-form cell 'L416W'; column 'Km (uM)' = 7.56; column 'kcat (s-1)' = 3.49; column 'kcat/Km (s-1 uM-1)' = 0.461. The value printed after each ± in the same cell is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.49 in a column headed kcat (s-1); s-1 is the canonical s^(-1), so no unit conversion applies and the value is 3.49 s^(-1). Km: printed Table 2 cell 7.56 in a column headed Km (uM); 7.56 / 1000 = 0.00756 mM. kcat/Km: printed Table 2 cell 0.461 in a column headed kcat/Km (s-1 uM-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.461 x 1000 = 461 s^-1 mM^-1. The exported values are kcat 3.49 s^(-1), Km 0.0076 mM and kcat_over_km 459.2105263157895 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'p-Anisyl alcohol', enzyme-form cell 'L416W': Km = 7.56 uM; kcat = 3.49 s-1; printed kcat/Km = 0.461 in a column headed (s-1 uM-1), that is 0.461 s^(-1)*uM^(-1).

row_label: Table 2, row p-Anisyl alcohol / L416W

table_label: Table 2: Steady-state kinetic constants of rCcAAO and the mutants (Biotechnology Letters 2018, 40(7):1077-1086). Printed column heads: Substrate; enzyme form; Km (uM); kcat (s-1); kcat/Km (s-1 uM-1)

substrate: 4-anisyl alcohol


column_label: Official Springer Table 2 row p-Anisyl alcohol / rCcAAO: Km column 11.6 +/- 1.0 uM, kcat column 12.5 +/- 0.3 s^-1, kcat/Km column 1.08 +/- 0.09 s^-1 uM^-1.

normalized_value_unit_evidence: Km normalized_value=0.0116 normalized_unit=mM; kcat normalized_value=12.5 normalized_unit=s^-1; kcat/Km normalized_value=1080 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=11.6 +/- 1.0 raw_unit=uM; kcat raw_value=12.5 +/- 0.3 raw_unit=s^-1; kcat/Km raw_value=1.08 +/- 0.09 raw_unit=s^-1 uM^-1

row_label: p-Anisyl alcohol / rCcAAO

table_label: Table 2


substrate_name: 4-Hydroxybenzyl alcohol

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A2Z5WP81 and applied mutation signature L416F to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic constants of rCcAAO and the mutants), body row '4-Hydroxybenzyl alcohol' with enzyme-form cell 'L416F'; column 'Km (uM)' = 163; column 'kcat (s-1)' = 8.77; column 'kcat/Km (s-1 uM-1)' = 0.0539. The value printed after each ± in the same cell is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 8.77 in a column headed kcat (s-1); s-1 is the canonical s^(-1), so no unit conversion applies and the value is 8.77 s^(-1). Km: printed Table 2 cell 163 in a column headed Km (uM); 163 / 1000 = 0.163 mM. kcat/Km: printed Table 2 cell 0.0539 in a column headed kcat/Km (s-1 uM-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.0539 x 1000 = 53.9 s^-1 mM^-1. The exported values are kcat 8.77 s^(-1), Km 0.163 mM and kcat_over_km 53.803680981595086 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row '4-Hydroxybenzyl alcohol', enzyme-form cell 'L416F': Km = 163 uM; kcat = 8.77 s-1; printed kcat/Km = 0.0539 in a column headed (s-1 uM-1), that is 0.0539 s^(-1)*uM^(-1).

row_label: Table 2, row 4-Hydroxybenzyl alcohol / L416F

substrate: 4-Hydroxybenzyl alcohol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L416W to reconstruct the assayed variant sequence.

column_label: Official Springer Table 2 row 4-Hydroxybenzyl alcohol / L416W: Km column 466 +/- 74 uM, kcat column 0.539 +/- 0.051 s^-1, kcat/Km column 0.00119 +/- 0.00007 s^-1 uM^-1.

normalized_value_unit_evidence: Km normalized_value=0.466 normalized_unit=mM; kcat normalized_value=0.539 normalized_unit=s^-1; kcat/Km normalized_value=1.19 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=466 +/- 74 raw_unit=uM; kcat raw_value=0.539 +/- 0.051 raw_unit=s^-1; kcat/Km raw_value=0.00119 +/- 0.00007 raw_unit=s^-1 uM^-1

row_label: 4-Hydroxybenzyl alcohol / L416W


column_label: Official Springer Table 2 row 4-Hydroxybenzyl alcohol / rCcAAO: Km column 56.3 +/- 7.6 uM, kcat column 4.81 +/- 0.06 s^-1, kcat/Km column 0.0855 +/- 0.0120 s^-1 uM^-1.

normalized_value_unit_evidence: Km normalized_value=0.0563 normalized_unit=mM; kcat normalized_value=4.81 normalized_unit=s^-1; kcat/Km normalized_value=85.5 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=56.3 +/- 7.6 raw_unit=uM; kcat raw_value=4.81 +/- 0.06 raw_unit=s^-1; kcat/Km raw_value=0.0855 +/- 0.0120 raw_unit=s^-1 uM^-1

row_label: 4-Hydroxybenzyl alcohol / rCcAAO


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L416F to reconstruct the assayed variant sequence.


column_label: Table 2 (Steady-state kinetic constants of rCcAAO and the mutants), body row 'Benzyl alcohol' with enzyme-form cell 'L416W'; column 'Km (uM)' = 5.87; column 'kcat (s-1)' = 3.84; column 'kcat/Km (s-1 uM-1)' = 0.665. The value printed after each ± in the same cell is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.84 in a column headed kcat (s-1); s-1 is the canonical s^(-1), so no unit conversion applies and the value is 3.84 s^(-1). Km: printed Table 2 cell 5.87 in a column headed Km (uM); 5.87 / 1000 = 0.00587 mM. kcat/Km: printed Table 2 cell 0.665 in a column headed kcat/Km (s-1 uM-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.665 x 1000 = 665 s^-1 mM^-1. The exported values are kcat 3.84 s^(-1), Km 0.0059 mM and kcat_over_km 650.8474576271186 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'Benzyl alcohol', enzyme-form cell 'L416W': Km = 5.87 uM; kcat = 3.84 s-1; printed kcat/Km = 0.665 in a column headed (s-1 uM-1), that is 0.665 s^(-1)*uM^(-1).

row_label: Table 2, row Benzyl alcohol / L416W


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

column_label: Official Springer Table 2 row Benzyl alcohol / rCcAAO: Km column 1.21 +/- 0.27 uM, kcat column 6.13 +/- 0.12 s^-1, kcat/Km column 5.06 +/- 1.08 s^-1 uM^-1.

normalized_value_unit_evidence: Km normalized_value=0.00121 normalized_unit=mM; kcat normalized_value=6.13 normalized_unit=s^-1; kcat/Km normalized_value=5060 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=1.21 +/- 0.27 raw_unit=uM; kcat raw_value=6.13 +/- 0.12 raw_unit=s^-1; kcat/Km raw_value=5.06 +/- 1.08 raw_unit=s^-1 uM^-1

row_label: Benzyl alcohol / rCcAAO


substrate_name: isovanillyl alcohol

column_label: Official Springer Table 2 row Isovanillyl alcohol / L416F: Km column 318 +/- 19 uM, kcat column 8.67 +/- 0.55 s^-1, kcat/Km column 0.0273 +/- 0.0001 s^-1 uM^-1.

normalized_value_unit_evidence: Km normalized_value=0.318 normalized_unit=mM; kcat normalized_value=8.67 normalized_unit=s^-1; kcat/Km normalized_value=27.3 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=318 +/- 19 raw_unit=uM; kcat raw_value=8.67 +/- 0.55 raw_unit=s^-1; kcat/Km raw_value=0.0273 +/- 0.0001 raw_unit=s^-1 uM^-1

row_label: Isovanillyl alcohol / L416F

substrate: isovanillyl alcohol


column_label: Official Springer Table 2 row Isovanillyl alcohol / L416W: Km column 154 +/- 2 uM, kcat column 2.05 +/- 0.05 s^-1, kcat/Km column 0.0133 +/- 0.0005 s^-1 uM^-1.

normalized_value_unit_evidence: Km normalized_value=0.154 normalized_unit=mM; kcat normalized_value=2.05 normalized_unit=s^-1; kcat/Km normalized_value=13.3 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=154 +/- 2 raw_unit=uM; kcat raw_value=2.05 +/- 0.05 raw_unit=s^-1; kcat/Km raw_value=0.0133 +/- 0.0005 raw_unit=s^-1 uM^-1

row_label: Isovanillyl alcohol / L416W


enzyme_display_name: galactose oxidase

organism: Gibberella zeae

substrate_name: D-Galactose

sequence_variant_note: Mutation signature C383A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

enzyme: galactose oxidase

substrate: D-Galactose


sequence_variant_note: Mutation signature C383S could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -39, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature C383S/Y436A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +20, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature C383S/Y436H/V494A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -15, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature Y436A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y436A/V494A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y436H could not be applied safely because the resolved sequence does not match the expected reference residue(s).


proof_lines:
rCcAAO
aryl-alcohol oxidase
aromatic alcohols


substrate_name: Vanillyl alcohol

column_label: Table 2 (Steady-state kinetic constants of rCcAAO and the mutants), body row 'Vanillyl alcohol' with enzyme-form cell 'L416F'; column 'Km (uM)' = 980; column 'kcat (s-1)' = 21.3; column 'kcat/Km (s-1 uM-1)' = 0.0218. The value printed after each ± in the same cell is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 21.3 in a column headed kcat (s-1); s-1 is the canonical s^(-1), so no unit conversion applies and the value is 21.3 s^(-1). Km: printed Table 2 cell 980 in a column headed Km (uM); 980 / 1000 = 0.98 mM. kcat/Km: printed Table 2 cell 0.0218 in a column headed kcat/Km (s-1 uM-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.0218 x 1000 = 21.8 s^-1 mM^-1. The exported values are kcat 21.3 s^(-1), Km 0.98 mM and kcat_over_km 21.73469387755102 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'Vanillyl alcohol', enzyme-form cell 'L416F': Km = 980 uM; kcat = 21.3 s-1; printed kcat/Km = 0.0218 in a column headed (s-1 uM-1), that is 0.0218 s^(-1)*uM^(-1).

row_label: Table 2, row Vanillyl alcohol / L416F

substrate: Vanillyl alcohol


column_label: Table 2 (Steady-state kinetic constants of rCcAAO and the mutants), body row 'Vanillyl alcohol' with enzyme-form cell 'L416W'; column 'Km (uM)' = 419; column 'kcat (s-1)' = 0.811; column 'kcat/Km (s-1 uM-1)' = 0.00194. The value printed after each ± in the same cell is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.811 in a column headed kcat (s-1); s-1 is the canonical s^(-1), so no unit conversion applies and the value is 0.811 s^(-1). Km: printed Table 2 cell 419 in a column headed Km (uM); 419 / 1000 = 0.419 mM. kcat/Km: printed Table 2 cell 0.00194 in a column headed kcat/Km (s-1 uM-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.00194 x 1000 = 1.94 s^-1 mM^-1. The exported values are kcat 0.81 s^(-1), Km 0.419 mM and kcat_over_km 1.9331742243436756 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'Vanillyl alcohol', enzyme-form cell 'L416W': Km = 419 uM; kcat = 0.811 s-1; printed kcat/Km = 0.00194 in a column headed (s-1 uM-1), that is 0.00194 s^(-1)*uM^(-1).

row_label: Table 2, row Vanillyl alcohol / L416W


column_label: Table 2 (Steady-state kinetic constants of rCcAAO and the mutants), body row 'Vanillyl alcohol' with enzyme-form cell 'rCcAAO'; column 'Km (uM)' = 6.27; column 'kcat (s-1)' = 14.7; column 'kcat/Km (s-1 uM-1)' = 2.35. The value printed after each ± in the same cell is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 14.7 in a column headed kcat (s-1); s-1 is the canonical s^(-1), so no unit conversion applies and the value is 14.7 s^(-1). Km: printed Table 2 cell 6.27 in a column headed Km (uM); 6.27 / 1000 = 0.00627 mM. kcat/Km: printed Table 2 cell 2.35 in a column headed kcat/Km (s-1 uM-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.35 x 1000 = 2350 s^-1 mM^-1. The exported values are kcat 14.7 s^(-1), Km 0.0063 mM and kcat_over_km 2333.333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'Vanillyl alcohol', enzyme-form cell 'rCcAAO': Km = 6.27 uM; kcat = 14.7 s-1; printed kcat/Km = 2.35 in a column headed (s-1 uM-1), that is 2.35 s^(-1)*uM^(-1).

row_label: Table 2, row Vanillyl alcohol / rCcAAO


substrate_name: veratryl alcohol

column_label: Table 2 (Steady-state kinetic constants of rCcAAO and the mutants), body row 'Veratryl alcohol' with enzyme-form cell 'L416F'; column 'Km (uM)' = 424; column 'kcat (s-1)' = 12.4; column 'kcat/Km (s-1 uM-1)' = 0.0293. The value printed after each ± in the same cell is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 12.4 in a column headed kcat (s-1); s-1 is the canonical s^(-1), so no unit conversion applies and the value is 12.4 s^(-1). Km: printed Table 2 cell 424 in a column headed Km (uM); 424 / 1000 = 0.424 mM. kcat/Km: printed Table 2 cell 0.0293 in a column headed kcat/Km (s-1 uM-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.0293 x 1000 = 29.3 s^-1 mM^-1. The exported values are kcat 12.4 s^(-1), Km 0.424 mM and kcat_over_km 29.245283018867926 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'Veratryl alcohol', enzyme-form cell 'L416F': Km = 424 uM; kcat = 12.4 s-1; printed kcat/Km = 0.0293 in a column headed (s-1 uM-1), that is 0.0293 s^(-1)*uM^(-1).

row_label: Table 2, row Veratryl alcohol / L416F

substrate: veratryl alcohol


column_label: Table 2 (Steady-state kinetic constants of rCcAAO and the mutants), body row 'Veratryl alcohol' with enzyme-form cell 'L416W'; column 'Km (uM)' = 686; column 'kcat (s-1)' = 2.96; column 'kcat/Km (s-1 uM-1)' = 0.00432. The value printed after each ± in the same cell is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.96 in a column headed kcat (s-1); s-1 is the canonical s^(-1), so no unit conversion applies and the value is 2.96 s^(-1). Km: printed Table 2 cell 686 in a column headed Km (uM); 686 / 1000 = 0.686 mM. kcat/Km: printed Table 2 cell 0.00432 in a column headed kcat/Km (s-1 uM-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.00432 x 1000 = 4.32 s^-1 mM^-1. The exported values are kcat 2.96 s^(-1), Km 0.686 mM and kcat_over_km 4.314868804664723 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'Veratryl alcohol', enzyme-form cell 'L416W': Km = 686 uM; kcat = 2.96 s-1; printed kcat/Km = 0.00432 in a column headed (s-1 uM-1), that is 0.00432 s^(-1)*uM^(-1).

row_label: Table 2, row Veratryl alcohol / L416W


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


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.


substrate_name: Methyl alpha-D-galactopyranoside

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CS93 and applied mutation signature Y436A/V494A with inferred residue-numbering offset +41 to reconstruct the assayed variant sequence.

column_label: Official OUP publisher PDF, Table II, row Y436A/V494A under 1-methyl-alpha-D-galactopyranoside, columns KM (mM), kcat (s^-1), and kcat/KM (M^-1 s^-1): 46 +/- 3; 1548 +/- 95; 33600 +/- 3000.

normalized_value_unit_evidence: KM 46 mM; kcat 1548 s^-1; printed kcat/KM 33.6 s^-1 mM^-1 after exact /1000 unit normalization.

raw_value_unit_evidence: Table II Y436A/V494A, 1-methyl-alpha-D-galactopyranoside: KM 46 +/- 3 mM; kcat 1548 +/- 95 s^-1; kcat/KM 33600 +/- 3000 M^-1 s^-1.

table_label: Table II

substrate: Methyl alpha-D-galactopyranoside


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CS93 and applied mutation signature Y436H with inferred residue-numbering offset +41 to reconstruct the assayed variant sequence.

column_label: Official OUP publisher PDF, Table II, row Y436H under 1-methyl-alpha-D-galactopyranoside, columns KM (mM), kcat (s^-1), and kcat/KM (M^-1 s^-1): 55 +/- 5; 1267 +/- 97; 23000 +/- 2700.

normalized_value_unit_evidence: KM 55 mM; kcat 1267 s^-1; printed kcat/KM 23.0 s^-1 mM^-1 after exact /1000 unit normalization.

raw_value_unit_evidence: Table II Y436H, 1-methyl-alpha-D-galactopyranoside: KM 55 +/- 5 mM; kcat 1267 +/- 97 s^-1; kcat/KM 23000 +/- 2700 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CS93 and applied mutation signature Y436H/V494A with inferred residue-numbering offset +41 to reconstruct the assayed variant sequence.

column_label: Official OUP publisher PDF, Table II, row Y436H/V494A under 1-methyl-alpha-D-galactopyranoside, columns KM (mM), kcat (s^-1), and kcat/KM (M^-1 s^-1): 45 +/- 7; 851 +/- 91; 18900 +/- 3600.

normalized_value_unit_evidence: KM 45 mM; kcat 851 s^-1; printed kcat/KM 18.9 s^-1 mM^-1 after exact /1000 unit normalization.

raw_value_unit_evidence: Table II Y436H/V494A, 1-methyl-alpha-D-galactopyranoside: KM 45 +/- 7 mM; kcat 851 +/- 91 s^-1; kcat/KM 18900 +/- 3600 M^-1 s^-1.


enzyme_display_name: Galactose oxidase

substrate_name: D-fructose

enzyme: Galactose oxidase

substrate: D-fructose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A2Z5WP81 and applied mutation signature L416F to reconstruct the assayed variant sequence.

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

column_label: Table 2 (Steady-state kinetic constants of rCcAAO and the mutants), body row 'trans,trans-2,4-Hexadien-1-ol' with enzyme-form cell 'L416F'; column 'Km (uM)' = 16.4; column 'kcat (s-1)' = 68.4; column 'kcat/Km (s-1 uM-1)' = 4.18. The value printed after each ± in the same cell is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 68.4 in a column headed kcat (s-1); s-1 is the canonical s^(-1), so no unit conversion applies and the value is 68.4 s^(-1). Km: printed Table 2 cell 16.4 in a column headed Km (uM); 16.4 / 1000 = 0.0164 mM. kcat/Km: printed Table 2 cell 4.18 in a column headed kcat/Km (s-1 uM-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 4.18 x 1000 = 4180 s^-1 mM^-1. The exported values are kcat 68.4 s^(-1), Km 0.0164 mM and kcat_over_km 4170.731707317073 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'trans,trans-2,4-Hexadien-1-ol', enzyme-form cell 'L416F': Km = 16.4 uM; kcat = 68.4 s-1; printed kcat/Km = 4.18 in a column headed (s-1 uM-1), that is 4.18 s^(-1)*uM^(-1).

row_label: Table 2, row trans,trans-2,4-Hexadien-1-ol / L416F


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A2Z5WP81 and applied mutation signature L416W to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic constants of rCcAAO and the mutants), body row 'trans,trans-2,4-Hexadien-1-ol' with enzyme-form cell 'L416W'; column 'Km (uM)' = 7.04; column 'kcat (s-1)' = 17.3; column 'kcat/Km (s-1 uM-1)' = 2.46. The value printed after each ± in the same cell is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 17.3 in a column headed kcat (s-1); s-1 is the canonical s^(-1), so no unit conversion applies and the value is 17.3 s^(-1). Km: printed Table 2 cell 7.04 in a column headed Km (uM); 7.04 / 1000 = 0.00704 mM. kcat/Km: printed Table 2 cell 2.46 in a column headed kcat/Km (s-1 uM-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.46 x 1000 = 2460 s^-1 mM^-1. The exported values are kcat 17.3 s^(-1), Km 0.007 mM and kcat_over_km 2471.4285714285716 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'trans,trans-2,4-Hexadien-1-ol', enzyme-form cell 'L416W': Km = 7.04 uM; kcat = 17.3 s-1; printed kcat/Km = 2.46 in a column headed (s-1 uM-1), that is 2.46 s^(-1)*uM^(-1).

row_label: Table 2, row trans,trans-2,4-Hexadien-1-ol / L416W


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

column_label: Official Springer Table 2 row trans,trans-2,4-Hexadien-1-ol / rCcAAO: Km column 15.6 +/- 0.8 uM, kcat column 48.3 +/- 1.4 s^-1, kcat/Km column 3.10 +/- 0.23 s^-1 uM^-1.

normalized_value_unit_evidence: Km normalized_value=0.0156 normalized_unit=mM; kcat normalized_value=48.3 normalized_unit=s^-1; kcat/Km normalized_value=3100 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=15.6 +/- 0.8 raw_unit=uM; kcat raw_value=48.3 +/- 1.4 raw_unit=s^-1; kcat/Km raw_value=3.10 +/- 0.23 raw_unit=s^-1 uM^-1

row_label: trans,trans-2,4-Hexadien-1-ol / rCcAAO


substrate_name: 3-anisyl alcohol

column_label: Table 2 (Steady-state kinetic constants of rCcAAO and the mutants), body row 'm-Anisyl alcohol' with enzyme-form cell 'L416F'; column 'Km (uM)' = 34.2; column 'kcat (s-1)' = 12.4; column 'kcat/Km (s-1 uM-1)' = 0.361. The value printed after each ± in the same cell is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 12.4 in a column headed kcat (s-1); s-1 is the canonical s^(-1), so no unit conversion applies and the value is 12.4 s^(-1). Km: printed Table 2 cell 34.2 in a column headed Km (uM); 34.2 / 1000 = 0.0342 mM. kcat/Km: printed Table 2 cell 0.361 in a column headed kcat/Km (s-1 uM-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.361 x 1000 = 361 s^-1 mM^-1. The exported values are kcat 12.4 s^(-1), Km 0.034 mM and kcat_over_km 364.70588235294116 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'm-Anisyl alcohol', enzyme-form cell 'L416F': Km = 34.2 uM; kcat = 12.4 s-1; printed kcat/Km = 0.361 in a column headed (s-1 uM-1), that is 0.361 s^(-1)*uM^(-1).

row_label: Table 2, row m-Anisyl alcohol / L416F

substrate: 3-anisyl alcohol


column_label: Table 2 (Steady-state kinetic constants of rCcAAO and the mutants), body row 'm-Anisyl alcohol' with enzyme-form cell 'L416W'; column 'Km (uM)' = 30.8; column 'kcat (s-1)' = 11.3; column 'kcat/Km (s-1 uM-1)' = 0.367. The value printed after each ± in the same cell is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 11.3 in a column headed kcat (s-1); s-1 is the canonical s^(-1), so no unit conversion applies and the value is 11.3 s^(-1). Km: printed Table 2 cell 30.8 in a column headed Km (uM); 30.8 / 1000 = 0.0308 mM. kcat/Km: printed Table 2 cell 0.367 in a column headed kcat/Km (s-1 uM-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.367 x 1000 = 367 s^-1 mM^-1. The exported values are kcat 11.3 s^(-1), Km 0.031 mM and kcat_over_km 364.5161290322581 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'm-Anisyl alcohol', enzyme-form cell 'L416W': Km = 30.8 uM; kcat = 11.3 s-1; printed kcat/Km = 0.367 in a column headed (s-1 uM-1), that is 0.367 s^(-1)*uM^(-1).

row_label: Table 2, row m-Anisyl alcohol / L416W


column_label: Official Springer Table 2 row m-Anisyl alcohol / rCcAAO: Km column 3.96 +/- 1.14 uM, kcat column 7.66 +/- 0.25 s^-1, kcat/Km column 1.94 +/- 0.59 s^-1 uM^-1.

normalized_value_unit_evidence: Km normalized_value=0.00396 normalized_unit=mM; kcat normalized_value=7.66 normalized_unit=s^-1; kcat/Km normalized_value=1940 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=3.96 +/- 1.14 raw_unit=uM; kcat raw_value=7.66 +/- 0.25 raw_unit=s^-1; kcat/Km raw_value=1.94 +/- 0.59 raw_unit=s^-1 uM^-1

row_label: m-Anisyl alcohol / rCcAAO


substrate_name: 3-Hydroxybenzyl alcohol

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L416F to reconstruct the assayed variant sequence.

substrate: 3-Hydroxybenzyl alcohol


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -9, so it is treated as a source-provided variant sequence.


column_label: Official Springer Table 2 row 3-Hydroxybenzyl alcohol / rCcAAO: Km column 5.68 +/- 0.1 uM, kcat column 9.91 +/- 0.12 s^-1, kcat/Km column 1.75 +/- 0.06 s^-1 uM^-1.

normalized_value_unit_evidence: Km normalized_value=0.00568 normalized_unit=mM; kcat normalized_value=9.91 normalized_unit=s^-1; kcat/Km normalized_value=1750 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=5.68 +/- 0.1 raw_unit=uM; kcat raw_value=9.91 +/- 0.12 raw_unit=s^-1; kcat/Km raw_value=1.75 +/- 0.06 raw_unit=s^-1 uM^-1

row_label: 3-Hydroxybenzyl alcohol / rCcAAO


column_label: Table 2 (Steady-state kinetic constants of rCcAAO and the mutants), body row 'p-Anisyl alcohol' with enzyme-form cell 'L416F'; column 'Km (uM)' = 19.2; column 'kcat (s-1)' = 14.2; column 'kcat/Km (s-1 uM-1)' = 0.740. The value printed after each ± in the same cell is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 14.2 in a column headed kcat (s-1); s-1 is the canonical s^(-1), so no unit conversion applies and the value is 14.2 s^(-1). Km: printed Table 2 cell 19.2 in a column headed Km (uM); 19.2 / 1000 = 0.0192 mM. kcat/Km: printed Table 2 cell 0.740 in a column headed kcat/Km (s-1 uM-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.740 x 1000 = 740 s^-1 mM^-1. The exported values are kcat 14.2 s^(-1), Km 0.019 mM and kcat_over_km 747.3684210526316 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'p-Anisyl alcohol', enzyme-form cell 'L416F': Km = 19.2 uM; kcat = 14.2 s-1; printed kcat/Km = 0.740 in a column headed (s-1 uM-1), that is 0.740 s^(-1)*uM^(-1).

row_label: Table 2, row p-Anisyl alcohol / L416F


enzyme_display_name: alcohol oxidase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F101N with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

smiles: CCCO

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.

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

enzyme: alcohol oxidase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F101S with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

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_accession and applied mutation signature M103S to reconstruct the assayed variant sequence.

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

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


substrate_name: ethanol

smiles: CCO

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.

row_label: ethanol

substrate: ethanol


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 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.


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: methanol

smiles: CO

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.

row_label: methanol

substrate: methanol


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.


substrate_name: L-sorbose

column_label: Table 3; row l-Sorbose; column K m (mM)

normalized_value_unit_evidence: km paper=38 mM

raw_value_unit_evidence: Table 3, row l-Sorbose: K m (mM) 38

row_label: l-Sorbose

table_label: Table 3

substrate: L-sorbose


substrate_name: D-gluconolactone

column_label: Table 3; row d-Glucono-1,5-lactone; column K m (mM)

raw_value_unit_evidence: Table 3, row d-Glucono-1,5-lactone: K m (mM) 38

substrate: D-gluconolactone


substrate_name: D-mannoheptose

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

column_label: Table 3; row d-Mannoheptose; column K m (mM)

normalized_value_unit_evidence: km paper=110 mM

raw_value_unit_evidence: Table 3, row d-Mannoheptose: K m (mM) 110

row_label: d-Mannoheptose

substrate: D-mannoheptose


column_label: Table 4; row DCIP (pH 4.5); column k cat (s^-1); Table 4; row DCIP (pH 4.5); column k cat / K m (mM^-1 s^-1); Table 4; row DCIP (pH 4.5); column K m (mM)

normalized_value_unit_evidence: kcat paper=150 s^-1; kcat_over_km paper=1600 s^-1*mM^-1; km paper=0.094 mM

row_label: DCIP (pH 4.5)


column_label: Table 4; row DCIP; column k cat (s^-1); Table 4; row DCIP; column k cat / K m (mM^-1 s^-1); Table 4; row DCIP; column K m (mM)

normalized_value_unit_evidence: kcat paper=20 s^-1; kcat_over_km paper=300 s^-1*mM^-1; km paper=0.065 mM

row_label: DCIP


column_label: Table 4; row 2,6-Dimethyl-1,4-benzoquinone (pH 4.5); column k cat (s^-1); Table 4; row 2,6-Dimethyl-1,4-benzoquinone (pH 4.5); column k cat / K m (mM^-1 s^-1); Table 4; row 2,6-Dimethyl-1,4-benzoquinone (pH 4.5); column K m (mM)

normalized_value_unit_evidence: kcat paper=210 s^-1; kcat_over_km paper=250 s^-1*mM^-1; km paper=0.83 mM

raw_value_unit_evidence: Table 4, row 2,6-Dimethyl-1,4-benzoquinone (pH 4.5): k cat (s^-1) 210; k cat / K m (mM^-1 s^-1) 250; K m (mM) 0.83

row_label: 2,6-Dimethyl-1,4-benzoquinone (pH 4.5)


column_label: Table 3; row 5-Thio-d-glucose; column k cat (s^-1); Table 3; row 5-Thio-d-glucose; column k cat / K m (mM^-1 s^-1); Table 3; row 5-Thio-d-glucose; column K m (mM)

normalized_value_unit_evidence: kcat paper=13 s^-1; kcat_over_km paper=3.3 s^-1*mM^-1; km paper=3.9 mM

raw_value_unit_evidence: Table 3, row 5-Thio-d-glucose: k cat (s^-1) 13; k cat / K m (mM^-1 s^-1) 3.3; K m (mM) 3.9


substrate_name: D-Allose

column_label: Table 3; row d-Allose; column k cat (s^-1); Table 3; row d-Allose; column k cat / K m (mM^-1 s^-1); Table 3; row d-Allose; column K m (mM)

normalized_value_unit_evidence: kcat paper=20 s^-1; kcat_over_km paper=0.57 s^-1*mM^-1; km paper=36 mM

raw_value_unit_evidence: Table 3, row d-Allose: k cat (s^-1) 20; k cat / K m (mM^-1 s^-1) 0.57; K m (mM) 36

row_label: d-Allose

substrate: D-Allose


substrate_name: D-Gentiobiose

column_label: Table 3; row Gentiobiose; column k cat (s^-1); Table 3; row Gentiobiose; column k cat / K m (mM^-1 s^-1); Table 3; row Gentiobiose; column K m (mM)

normalized_value_unit_evidence: kcat paper=12 s^-1; kcat_over_km paper=0.19 s^-1*mM^-1; km paper=62 mM

raw_value_unit_evidence: Table 3, row Gentiobiose: k cat (s^-1) 12; k cat / K m (mM^-1 s^-1) 0.19; K m (mM) 62

row_label: Gentiobiose

substrate: D-Gentiobiose


substrate_name: D-Mannoheptose

column_label: Table 3. Apparent kinetic constants of P2O from T. multicolor for several electron donors; row d-Mannoheptose; column Km (mM) raw value 110; column kcat (s^-1) raw value 4.4; column kcat/Km (mM^-1 s^-1) raw value 0.042

normalized_value_unit_evidence: kcat normalized_value=4.4 normalized_unit=s^-1; Km normalized_value=110 normalized_unit=mM; kcat/Km normalized_value=0.042 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=4.4 raw_unit=s^-1; Km raw_value=110 raw_unit=mM; kcat/Km raw_value=0.042 raw_unit=mM^-1*s^-1

substrate: D-Mannoheptose


substrate_name: D-Xylose

column_label: Table 3. Apparent kinetic constants of P2O from T. multicolor for several electron donors; row d-Xylose; column Km (mM) raw value 30; column kcat (s^-1) raw value 30; column kcat/Km (mM^-1 s^-1) raw value 1.0

normalized_value_unit_evidence: kcat normalized_value=30 normalized_unit=s^-1; Km normalized_value=30 normalized_unit=mM; kcat/Km normalized_value=1.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=30 raw_unit=s^-1; Km raw_value=30 raw_unit=mM; kcat/Km raw_value=1.0 raw_unit=mM^-1*s^-1

row_label: d-Xylose

substrate: D-Xylose


substrate_name: L-Arabinose

column_label: Table 3. Apparent kinetic constants of P2O from T. multicolor for several electron donors; row l-Arabinose; column Km (mM) raw value 97; column kcat (s^-1) raw value 0.81; column kcat/Km (mM^-1 s^-1) raw value 0.008

normalized_value_unit_evidence: kcat normalized_value=0.81 normalized_unit=s^-1; Km normalized_value=97 normalized_unit=mM; kcat/Km normalized_value=0.008 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.81 raw_unit=s^-1; Km raw_value=97 raw_unit=mM; kcat/Km raw_value=0.008 raw_unit=mM^-1*s^-1

row_label: l-Arabinose

substrate: L-Arabinose


substrate_name: L-Sorbose

column_label: Table 3. Apparent kinetic constants of P2O from T. multicolor for several electron donors; row l-Sorbose; column Km (mM) raw value 38; column kcat (s^-1) raw value 53; column kcat/Km (mM^-1 s^-1) raw value 1.4

normalized_value_unit_evidence: kcat normalized_value=53 normalized_unit=s^-1; Km normalized_value=38 normalized_unit=mM; kcat/Km normalized_value=1.4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=53 raw_unit=s^-1; Km raw_value=38 raw_unit=mM; kcat/Km raw_value=1.4 raw_unit=mM^-1*s^-1

substrate: L-Sorbose


column_label: Table 4. Apparent kinetic constants of P2O from T. multicolor for several electron acceptors; row ABTS cation radical; column Km (mM) raw value 0.070; column kcat (s^-1) raw value 21; column kcat/Km (mM^-1 s^-1) raw value 310

normalized_value_unit_evidence: kcat normalized_value=21 normalized_unit=s^-1; Km normalized_value=0.070 normalized_unit=mM; kcat/Km normalized_value=310 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=21 raw_unit=s^-1; Km raw_value=0.070 raw_unit=mM; kcat/Km raw_value=310 raw_unit=mM^-1*s^-1

row_label: ABTS cation radical


column_label: Table 4. Apparent kinetic constants of P2O from T. multicolor for several electron acceptors; row Tetrabromo-1,4-benzoquinone; column Km (mM) raw value 0.090; column kcat (s^-1) raw value 280; column kcat/Km (mM^-1 s^-1) raw value 3100

normalized_value_unit_evidence: kcat normalized_value=280 normalized_unit=s^-1; Km normalized_value=0.090 normalized_unit=mM; kcat/Km normalized_value=3100 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=280 raw_unit=s^-1; Km raw_value=0.090 raw_unit=mM; kcat/Km raw_value=3100 raw_unit=mM^-1*s^-1


column_label: Table 4. Apparent kinetic constants of P2O from T. multicolor for several electron acceptors; row Methyl-1,4-benzoquinone (pH 4.5); column Km (mM) raw value 0.35; column kcat (s^-1) raw value 230; column kcat/Km (mM^-1 s^-1) raw value 670

normalized_value_unit_evidence: kcat normalized_value=230 normalized_unit=s^-1; Km normalized_value=0.35 normalized_unit=mM; kcat/Km normalized_value=670 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=230 raw_unit=s^-1; Km raw_value=0.35 raw_unit=mM; kcat/Km raw_value=670 raw_unit=mM^-1*s^-1

row_label: Methyl-1,4-benzoquinone (pH 4.5)


column_label: LsP2Ox row D-xylose; columns Km [mM], kcat [s^-1], and kcat/Km [mM^-1 s^-1] report Km 6.3 mM; kcat 5.48 s^-1; kcat/Km 0.867 mM^-1 s^-1.

row_label: LsP2Ox row D-xylose

table_label: Table 3. Apparent kinetic constants for electron donor substrates


column_label: LsP2Ox row BQ; columns Km [mM], kcat [s^-1], and kcat/Km [mM^-1 s^-1] report Km 0.033 mM; kcat 92.3 s^-1; kcat/Km 2760 mM^-1 s^-1.

row_label: LsP2Ox row BQ


organism: Pleurotus eryngii

smiles: CC=CC=CC=O

assay_conditions_summary: pH 6; 297.15 K; buffer pH 6

column_label: Table 2 columns Aldehyde, Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); row matched by 2,4-Hexadienal.

raw_value_unit_evidence: Table 2 row 2,4-Hexadienal: Km 13.0 mM; kcat 20 min^-1; kcat/Km 1.5 min^-1 mM^-1.

table_label: Table 2, steady-state kinetic constants for AAO oxidation of different aldehydes


assay_conditions_summary: pH 6; 297.15 K; Assay condition: 0.1 M sodium phosphate

column_label: Columns Aldehyde, Km (mM), kcat (min^-1), kcat/Km (min^-1 mM^-1); row 3,4-Difluorobenzaldehyde.

raw_value_unit_evidence: Table 2 row 3,4-Difluorobenzaldehyde: Km 3.0 mM; kcat 52 min^-1; kcat/Km 16.9 min^-1 mM^-1.


column_label: Table 2 columns Aldehyde, Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); row matched by 3-Chloro-p-anisaldehyde.

raw_value_unit_evidence: Table 2 row 3-Chloro-p-anisaldehyde: Km 0.7 mM; kcat 3.4 min^-1; kcat/Km 5.1 min^-1 mM^-1.


column_label: Table 2 columns Aldehyde, Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); row matched by m-Chlorobenzaldehyde.

raw_value_unit_evidence: Table 2 row m-Chlorobenzaldehyde: Km 1.5 mM; kcat 51 min^-1; kcat/Km 38.6 min^-1 mM^-1.

row_label: m-Chlorobenzaldehyde


column_label: Table 2 columns Aldehyde, Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); row matched by m-Fluorobenzaldehyde.

raw_value_unit_evidence: Table 2 row m-Fluorobenzaldehyde: Km 2.2 mM; kcat 53 min^-1; kcat/Km 24.4 min^-1 mM^-1.

row_label: m-Fluorobenzaldehyde


column_label: Table 2 columns Aldehyde, Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); row matched by p-Anisaldehyde.

raw_value_unit_evidence: Table 2 row p-Anisaldehyde: Km 0.7 mM; kcat 3.0 min^-1; kcat/Km 5.2 min^-1 mM^-1.

row_label: p-Anisaldehyde


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -6, so it is treated as a source-provided variant sequence.


column_label: Table 2 columns Aldehyde, Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); row matched by p-Chlorobenzaldehyde.

raw_value_unit_evidence: Table 2 row p-Chlorobenzaldehyde: Km 4.7 mM; kcat 63 min^-1; kcat/Km 13.4 min^-1 mM^-1.

row_label: p-Chlorobenzaldehyde


column_label: Table 2 columns Aldehyde, Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); row matched by p-Fluorobenzaldehyde.

raw_value_unit_evidence: Table 2 row p-Fluorobenzaldehyde: Km 4.9 mM; kcat 22.0 min^-1; kcat/Km 4.5 min^-1 mM^-1.

row_label: p-Fluorobenzaldehyde


column_label: Table 2 columns Aldehyde, Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); row matched by p-Nitrobenzaldehyde.

raw_value_unit_evidence: Table 2 row p-Nitrobenzaldehyde: Km 5.0 mM; kcat 98 min^-1; kcat/Km 18.9 min^-1 mM^-1.

row_label: p-Nitrobenzaldehyde


substrate_name: D-Galactose

column_label: Official OUP publisher PDF, Table II, row Y436H/V494A under D-galactose, columns KM (mM), kcat (s^-1), and kcat/KM (M^-1 s^-1): 68 +/- 4; 1181 +/- 36; 17400 +/- 1200.

normalized_value_unit_evidence: KM 68 mM; kcat 1181 s^-1; printed kcat/KM 17.4 s^-1 mM^-1 after exact /1000 unit normalization.

row_label: Y436H/V494A — D-galactose

substrate: D-Galactose


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CS93 and applied mutation signature C383A with inferred residue-numbering offset +41 to reconstruct the assayed variant sequence.

column_label: Official OUP publisher PDF, Table II, row C383A under 1-methyl-alpha-D-galactopyranoside, columns KM (mM), kcat (s^-1), and kcat/KM (M^-1 s^-1): 47 +/- 6; 457 +/- 34; 9700 +/- 1400.

normalized_value_unit_evidence: KM 47 mM; kcat 457 s^-1; printed kcat/KM 9.7 s^-1 mM^-1 after exact /1000 unit normalization.

raw_value_unit_evidence: Table II C383A, 1-methyl-alpha-D-galactopyranoside: KM 47 +/- 6 mM; kcat 457 +/- 34 s^-1; kcat/KM 9700 +/- 1400 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CS93 and applied mutation signature C383S with inferred residue-numbering offset +41 to reconstruct the assayed variant sequence.

column_label: Official OUP publisher PDF, Table II, row C383S under 1-methyl-alpha-D-galactopyranoside, columns KM (mM), kcat (s^-1), and kcat/KM (M^-1 s^-1): 16 +/- 3; 839 +/- 63; 52400 +/- 11000.

normalized_value_unit_evidence: KM 16 mM; kcat 839 s^-1; printed kcat/KM 52.4 s^-1 mM^-1 after exact /1000 unit normalization.

raw_value_unit_evidence: Table II C383S, 1-methyl-alpha-D-galactopyranoside: KM 16 +/- 3 mM; kcat 839 +/- 63 s^-1; kcat/KM 52400 +/- 11000 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CS93 and applied mutation signature C383S/V494A with inferred residue-numbering offset +41 to reconstruct the assayed variant sequence.

column_label: Official OUP publisher PDF, Table II, row C383S/V494A under 1-methyl-alpha-D-galactopyranoside, columns KM (mM), kcat (s^-1), and kcat/KM (M^-1 s^-1): 17 +/- 3; 1495 +/- 114; 87900 +/- 17000.

normalized_value_unit_evidence: KM 17 mM; kcat 1495 s^-1; printed kcat/KM 87.9 s^-1 mM^-1 after exact /1000 unit normalization.

raw_value_unit_evidence: Table II C383S/V494A, 1-methyl-alpha-D-galactopyranoside: KM 17 +/- 3 mM; kcat 1495 +/- 114 s^-1; kcat/KM 87900 +/- 17000 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CS93 and applied mutation signature C383S/Y436A with inferred residue-numbering offset +41 to reconstruct the assayed variant sequence.

column_label: Official OUP publisher PDF, Table II, row C383S/Y436A under 1-methyl-alpha-D-galactopyranoside, columns KM (mM), kcat (s^-1), and kcat/KM (M^-1 s^-1): 25 +/- 3; 811 +/- 63; 32400 +/- 4600.

normalized_value_unit_evidence: KM 25 mM; kcat 811 s^-1; printed kcat/KM 32.4 s^-1 mM^-1 after exact /1000 unit normalization.

raw_value_unit_evidence: Table II C383S/Y436A, 1-methyl-alpha-D-galactopyranoside: KM 25 +/- 3 mM; kcat 811 +/- 63 s^-1; kcat/KM 32400 +/- 4600 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CS93 and applied mutation signature C383S/Y436H with inferred residue-numbering offset +41 to reconstruct the assayed variant sequence.

column_label: Official OUP publisher PDF, Table II, row C383S/Y436H under 1-methyl-alpha-D-galactopyranoside, columns KM (mM), kcat (s^-1), and kcat/KM (M^-1 s^-1): 17 +/- 3; 1091 +/- 69; 64200 +/- 12000.

normalized_value_unit_evidence: KM 17 mM; kcat 1091 s^-1; printed kcat/KM 64.2 s^-1 mM^-1 after exact /1000 unit normalization.

raw_value_unit_evidence: Table II C383S/Y436H, 1-methyl-alpha-D-galactopyranoside: KM 17 +/- 3 mM; kcat 1091 +/- 69 s^-1; kcat/KM 64200 +/- 12000 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CS93 and applied mutation signature C383S/Y436H/V494A with inferred residue-numbering offset +41 to reconstruct the assayed variant sequence.

column_label: Official OUP publisher PDF, Table II, row C383S/Y436H/V494A under 1-methyl-alpha-D-galactopyranoside, columns KM (mM), kcat (s^-1), and kcat/KM (M^-1 s^-1): 18 +/- 2; 1067 +/- 40; 59300 +/- 7000.

normalized_value_unit_evidence: KM 18 mM; kcat 1067 s^-1; printed kcat/KM 59.3 s^-1 mM^-1 after exact /1000 unit normalization.

raw_value_unit_evidence: Table II C383S/Y436H/V494A, 1-methyl-alpha-D-galactopyranoside: KM 18 +/- 2 mM; kcat 1067 +/- 40 s^-1; kcat/KM 59300 +/- 7000 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0CS93 and applied mutation signature V494A with inferred residue-numbering offset +41 to reconstruct the assayed variant sequence.

column_label: Official OUP publisher PDF, Table II, row V494A under 1-methyl-alpha-D-galactopyranoside, columns KM (mM), kcat (s^-1), and kcat/KM (M^-1 s^-1): 46 +/- 4; 1444 +/- 86; 31400 +/- 3300.

normalized_value_unit_evidence: KM 46 mM; kcat 1444 s^-1; printed kcat/KM 31.4 s^-1 mM^-1 after exact /1000 unit normalization.

raw_value_unit_evidence: Table II V494A, 1-methyl-alpha-D-galactopyranoside: KM 46 +/- 4 mM; kcat 1444 +/- 86 s^-1; kcat/KM 31400 +/- 3300 M^-1 s^-1.


column_label: Table II reports the wild-type proGO row under kinetic properties of GO mutants with D-galactose and 1-methyl-alpha-D-galactose as substrates.

normalized_value_unit_evidence: kcat normalized_value=995 normalized_unit=s^-1; Km normalized_value=56 normalized_unit=mM; kcat/Km normalized_value=17.8 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Table II row Wild-type proGO, 1-methyl-alpha-D-galactopyranoside: KM 56 +/- 5 mM; kcat 995 +/- 34 s^-1; kcat/KM 17 800 +/- 1700 M^-1 s^-1

row_label: Wild-type proGO / 1-methyl-alpha-D-galactopyranoside

table_label: OUP/ISU full text Table II


sequence_variant_note: Mutation signature Y436A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: melibiose

column_label: LsP2Ox row melibiose; columns Km [mM], kcat [s^-1], and kcat/Km [mM^-1 s^-1] report Km 72.8 mM; kcat 0.839 s^-1; kcat/Km 0.0115 mM^-1 s^-1.

row_label: LsP2Ox row melibiose

substrate: melibiose


substrate_name: D-galactose

substrate: D-galactose


substrate_name: D-xylose

column_label: LsP2Ox row D-xylose; columns Km [mM], kcat [s^-1], and kcat/Km [mM^-1 s^-1] report Km 6.3 mM; kcat 5.48 s^-1; kcat/Km 0.867 mM^-1 s^-1.

substrate: D-xylose


column_label: LsP2Ox row L-sorbose; columns Km [mM], kcat [s^-1], and kcat/Km [mM^-1 s^-1] report Km 14.7 mM; kcat 7.7 s^-1; kcat/Km 0.524 mM^-1 s^-1.

row_label: LsP2Ox row L-sorbose


column_label: LsP2Ox row DCIP; columns Km [mM], kcat [s^-1], and kcat/Km [mM^-1 s^-1] report Km 0.187 mM; kcat 67.3 s^-1; kcat/Km 361 mM^-1 s^-1.

row_label: LsP2Ox row DCIP


column_label: LsP2Ox row D-galactose; columns Km [mM], kcat [s^-1], and kcat/Km [mM^-1 s^-1] report Km 3.84 mM; kcat 1.02 s^-1; kcat/Km 0.265 mM^-1 s^-1.

row_label: LsP2Ox row D-galactose


substrate_name: D-glucose

column_label: LsP2Ox row D-glucose; columns Km [mM], kcat [s^-1], and kcat/Km [mM^-1 s^-1] report Km 0.314 mM; kcat 6.92 s^-1; kcat/Km 22.1 mM^-1 s^-1.

row_label: LsP2Ox row D-glucose

substrate: D-glucose


substrate_name: ferrocenium ion

column_label: LsP2Ox row Fc+; columns Km [mM], kcat [s^-1], and kcat/Km [mM^-1 s^-1] report Km 0.187 mM; kcat 39.9 s^-1; kcat/Km 213 mM^-1 s^-1.

row_label: LsP2Ox row Fc+

substrate: ferrocenium ion


substrate_name: 3-Chloro-4-methoxybenzyl alcohol

assay_conditions_summary: pH 6; 297.15 K; buffer 100 mM sodium phosphate

column_label: PMID 15813702 / PMCID PMC1180723 official PMC HTML Table 1 row 3-Chloro-p-anisyl alcohol columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 14+/-1, 46+/-1, and 4086+/-200 respectively.

normalized_value_unit_evidence: Km=0.014 mM; kcat=46.0 s^-1; queued kcat_over_km=3285.714285714286 s^-1 mM^-1 from 46.0 / 0.014; explicit paper kcat/Km cell normalizes to 4086.0 s^-1 mM^-1, outside the queued quotient by 800.2857142857142.

raw_value_unit_evidence: Table 1 row 3-Chloro-p-anisyl alcohol: Km=14+/-1 uM; kcat=46+/-1 s^-1; kcat/Km=4086+/-200 s^-1 mM^-1.

row_label: 3-Chloro-p-anisyl alcohol

table_label: Table 1. Steady-state kinetic constants for AAO oxidation of different substrates

substrate: 3-Chloro-4-methoxybenzyl alcohol


substrate_name: 3-Chlorobenzyl alcohol

column_label: PMID 15813702 / PMCID PMC1180723 official PMC HTML Table 1 row m-Chlorobenzyl alcohol columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 107+/-2, 22+/-1, and 203+/-4 respectively.

normalized_value_unit_evidence: Km=0.107 mM; kcat=22.0 s^-1; queued kcat_over_km=205.60747663551402 s^-1 mM^-1 computed from table kcat/Km input cells (22.0 / 0.107); explicit kcat/Km cell prints 203+/-4 s^-1 mM^-1 and is compatible with the quotient within the reported uncertainty.

raw_value_unit_evidence: Table 1 row m-Chlorobenzyl alcohol: Km=107+/-2 uM; kcat=22+/-1 s^-1; kcat/Km=203+/-4 s^-1 mM^-1.

row_label: m-Chlorobenzyl alcohol

substrate: 3-Chlorobenzyl alcohol


substrate_name: 3-Methoxybenzyl alcohol

column_label: PMID 15813702 / PMCID PMC1180723 official PMC HTML Table 1 row m-Anisyl alcohol (3-methoxybenzyl alcohol) columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 227+/-105, 15+/-2, and 65+/-24 respectively.

normalized_value_unit_evidence: Km=0.227 mM; kcat=15.0 s^-1; queued kcat_over_km=66.07929515418502 s^-1 mM^-1 computed from table kcat/Km input cells (15.0 / 0.227); explicit kcat/Km cell prints 65+/-24 s^-1 mM^-1 and is compatible with the quotient within the reported uncertainty.

raw_value_unit_evidence: Table 1 row m-Anisyl alcohol (3-methoxybenzyl alcohol): Km=227+/-105 uM; kcat=15+/-2 s^-1; kcat/Km=65+/-24 s^-1 mM^-1.

substrate: 3-Methoxybenzyl alcohol


substrate_name: 4-Hydroxymethylbenzoic acid

column_label: Table 1 p-(Hydroxymethyl) benzoic acid row, Km and kcat columns and same-row quotient.

row_label: p-(Hydroxymethyl) benzoic acid

substrate: 4-Hydroxymethylbenzoic acid


substrate_name: 4-Methoxybenzyl alcohol

substrate: 4-Methoxybenzyl alcohol


substrate_name: Isovanillyl alcohol

column_label: PMID 15813702 / PMCID PMC1180723 official PMC HTML Table 1 row Isovanillyl alcohol columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 831+/-58, 127+/-3, and 152+/-5 respectively.

normalized_value_unit_evidence: Km=0.831 mM; kcat=127.0 s^-1; queued kcat_over_km=152.82791817087846 s^-1 mM^-1 computed from table kcat/Km input cells (127.0 / 0.831); explicit kcat/Km cell prints 152+/-5 s^-1 mM^-1 and is compatible with the quotient within the reported uncertainty.

raw_value_unit_evidence: Table 1 row Isovanillyl alcohol: Km=831+/-58 uM; kcat=127+/-3 s^-1; kcat/Km=152+/-5 s^-1 mM^-1.

row_label: Isovanillyl alcohol

substrate: Isovanillyl alcohol


substrate_name: m-Fluorobenzyl alcohol

column_label: PMID 15813702 / PMCID PMC1180723 official PMC HTML Table 1 row m-Fluorobenzyl alcohol columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 554+/-30, 6+/-1, and 13+/-1 respectively.

normalized_value_unit_evidence: Km=0.554 mM; kcat=6.0 s^-1; queued kcat_over_km=10.830324909747292 s^-1 mM^-1 from 6.0 / 0.554; explicit paper kcat/Km cell normalizes to 13.0 s^-1 mM^-1, outside the queued quotient by 2.169675090252708.

raw_value_unit_evidence: Table 1 row m-Fluorobenzyl alcohol: Km=554+/-30 uM; kcat=6+/-1 s^-1; kcat/Km=13+/-1 s^-1 mM^-1.

row_label: m-Fluorobenzyl alcohol

substrate: m-Fluorobenzyl alcohol


substrate_name: p-Chlorobenzyl alcohol

column_label: PMID 15813702 / PMCID PMC1180723 official PMC HTML Table 1 row p-Chlorobenzyl alcohol columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 132+/-6, 51+/-1, and 398+/-32 respectively.

normalized_value_unit_evidence: Km=0.132 mM; kcat=51.0 s^-1; queued kcat_over_km=386.3636363636363 s^-1 mM^-1 computed from table kcat/Km input cells (51.0 / 0.132); explicit kcat/Km cell prints 398+/-32 s^-1 mM^-1 and is compatible with the quotient within the reported uncertainty.

raw_value_unit_evidence: Table 1 row p-Chlorobenzyl alcohol: Km=132+/-6 uM; kcat=51+/-1 s^-1; kcat/Km=398+/-32 s^-1 mM^-1.

row_label: p-Chlorobenzyl alcohol

substrate: p-Chlorobenzyl alcohol


substrate_name: p-Fluorobenzyl alcohol

column_label: PMID 15813702 / PMCID PMC1180723 official PMC HTML Table 1 row p-Fluorobenzyl alcohol columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 553+/-38, 32+/-1, and 59+/-6 respectively.

normalized_value_unit_evidence: Km=0.553 mM; kcat=32.0 s^-1; queued kcat_over_km=57.866184448462924 s^-1 mM^-1 computed from table kcat/Km input cells (32.0 / 0.553); explicit kcat/Km cell prints 59+/-6 s^-1 mM^-1 and is compatible with the quotient within the reported uncertainty.

raw_value_unit_evidence: Table 1 row p-Fluorobenzyl alcohol: Km=553+/-38 uM; kcat=32+/-1 s^-1; kcat/Km=59+/-6 s^-1 mM^-1.

row_label: p-Fluorobenzyl alcohol

substrate: p-Fluorobenzyl alcohol


substrate_name: cinnamyl alcohol

column_label: PMID 15813702 / PMCID PMC1180723 official PMC HTML Table 1 row Cinnamyl alcohol columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 708+/-85, 65+/-3, and 78+/-11 respectively.

normalized_value_unit_evidence: Km=0.708 mM; kcat=65.0 s^-1; queued kcat_over_km=91.80790960451978 s^-1 mM^-1 from 65.0 / 0.708; explicit paper kcat/Km cell normalizes to 78.0 s^-1 mM^-1, outside the queued quotient by 13.807909604519779.

raw_value_unit_evidence: Table 1 row Cinnamyl alcohol: Km=708+/-85 uM; kcat=65+/-3 s^-1; kcat/Km=78+/-11 s^-1 mM^-1.

row_label: Cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: benzaldehyde

column_label: Table 2 columns Aldehyde, Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); row matched by Benzaldehyde.

raw_value_unit_evidence: Table 2 row Benzaldehyde: Km 7.0 mM; kcat 30 min^-1; kcat/Km 4.4 min^-1 mM^-1.

row_label: Benzaldehyde

substrate: benzaldehyde


substrate_name: veratraldehyde

column_label: Table 2 columns Aldehyde, Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); row matched by Veratraldehyde.

raw_value_unit_evidence: Table 2 row Veratraldehyde: Km 8.0 mM; kcat 8.0 min^-1; kcat/Km 1.0 min^-1 mM^-1.

row_label: Veratraldehyde

substrate: veratraldehyde


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


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: 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: 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.


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.


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


substrate_name: D-galactose

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

substrate: D-galactose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H450G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H450G/E542K/V546C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H450G/V546C to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q7ZA32 and applied mutation signature H450G/E542K/V546C to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 333.15 K; buffer 50 mM KH2PO4

column_label: Table 1: Kinetic Properties and Substrate Selectivity of His-Tagged Recombinant Wild-Type P2Ox from Trametes multicolor and Mutational Variants with Either D-Glucose or D-Galactose as Substrate and O2 (Air) as Electron Acceptor (J. Agric. Food Chem. 2010, 58(6):3465-3471), row 'H450G/E542K/V546C', D-glucose block; column 'KM (mM)' = 0.770; column 'kcat (s^-1)' = 6.81; column 'kcat/KM (mM^-1 s^-1)' = 8.83.

normalized_value_unit_evidence: kcat: printed Table 1 cell 6.81 s^-1; the printed unit is already the export unit, no conversion, so the normalized value is 6.81 s^-1. KM: printed Table 1 cell 0.770 mM; already the export unit, no conversion, so the normalized value is 0.770 mM. kcat/KM: printed Table 1 cell 8.83 mM^-1 s^-1; mM^-1 s^-1 is the export unit s^(-1)*mM^(-1), no conversion, so the normalized value is 8.83 s^-1 mM^-1. This paper prints no min^-1, uM or M^-1 s^-1 kinetic cell in Table 1.

raw_value_unit_evidence: Table 1, row H450G/E542K/V546C, D-glucose block: KM = 0.770 mM; kcat = 6.81 s^-1; printed kcat/KM = 8.83 mM^-1 s^-1.

row_label: Table 1, row H450G/E542K/V546C, D-glucose columns


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


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.


substrate_name: D-melibiose

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).

substrate: D-melibiose


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).


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.


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


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


substrate_name: ferrocenium hexafluorophosphate

substrate: ferrocenium hexafluorophosphate


organism: Streptomyces sp. SA-COO

substrate_name: cholesterol

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.

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 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.

substrate: cholesterol


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


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.

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.


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 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'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12676 and applied mutation signature L80C 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 1, L80C'; column 'kcat (s^-1)' prints 89; column 'Km (uM)' prints 11; column 'kcat/Km (M^-1 s^-1)' prints 8.4 x 10^6; column 'lambda-max Trp (nm)' prints 330.

normalized_value_unit_evidence: kcat: printed Table 1 cell 89 s^-1; already in s^-1, no conversion; the exported value is 89.0 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 8.4 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.4 x 10^6 / 1000 = 8400.0 s^-1 mM^-1. The exported ratio is 8090.909090909091 s^(-1)*mM^(-1), which is the quotient 89.0 / 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 8400.0 and kcat and Km are unchanged.

row_label: Table 1, row 'mutant 1, L80C'


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 T168C/A276C 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 5, T168C/A276C'; column 'kcat (s^-1)' prints 46; column 'Km (uM)' prints 14; column 'kcat/Km (M^-1 s^-1)' prints 3.4 x 10^6; column 'lambda-max Trp (nm)' prints 328.

normalized_value_unit_evidence: kcat: printed Table 1 cell 46 s^-1; already in s^-1, no conversion; the exported value is 46.0 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 14 uM; 14 / 1000 = 0.014 mM; the exported value is 0.014 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 3.4 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.4 x 10^6 / 1000 = 3400.0 s^-1 mM^-1. The exported ratio is 3285.714285714286 s^(-1)*mM^(-1), which is the quotient 46.0 / 0.014 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 3400.0 and kcat and Km are unchanged.

row_label: Table 1, row 'mutant 5, T168C/A276C'


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 'wild type'; column 'kcat (s^-1)' prints 67; column 'Km (uM)' prints 13; column 'kcat/Km (M^-1 s^-1)' prints 5.1 x 10^6; column 'lambda-max Trp (nm)' prints 329.

normalized_value_unit_evidence: kcat: printed Table 1 cell 67 s^-1; already in s^-1, no conversion; the exported value is 67.0 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 13 uM; 13 / 1000 = 0.013 mM; the exported value is 0.013 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 5.1 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.1 x 10^6 / 1000 = 5100.0 s^-1 mM^-1. The exported ratio is 5153.846153846154 s^(-1)*mM^(-1), which is the quotient 67.0 / 0.013 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 5100.0 and kcat and Km are unchanged.

row_label: Table 1, row 'wild type'


organism: Fusarium graminearum

assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM sodium phosphate

column_label: Table 1; enzyme column group FgrAAO; row_label: 3-Methoxybenzyl (m-anisyl) alcohol; columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1)

normalized_value_unit_evidence: normalized: kcat=52 s^-1; km=6.5 mM; kcat_over_km=8 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for FgrAAO / 3-Methoxybenzyl (m-anisyl) alcohol: KM=6.5 +/- 1.5 mM; kcat=52 +/- 1.5 s^-1; kcat/KM=8000 M^-1 s^-1

row_label: 3-Methoxybenzyl (m-anisyl) alcohol

table_label: Table 1


column_label: Table 1; enzyme column group FgrAAO; row_label: DFF; columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1)

normalized_value_unit_evidence: normalized: kcat=3.6 s^-1; km=10 mM; kcat_over_km=0.36 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for FgrAAO / DFF: KM=10 +/- 2.9 mM; kcat=3.6 +/- 0.27 s^-1; kcat/KM=360 M^-1 s^-1

row_label: DFF


column_label: Table 1. Substrate specificity of FgrAAO and FoxAAO; row FgrAAO / HMFCA; FgrAAO columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1); cells KM=4.4 +/- 0.90; kcat=3.8 +/- 0.33; kcat/KM=860

normalized_value_unit_evidence: kcat normalized_value=3.8 s^-1; Km normalized_value=4.4 mM; kcat/Km normalized_value=0.8636363636363635 s^-1*mM^-1 (printed table efficiency normalized=0.86 s^-1*mM^-1)

raw_value_unit_evidence: kcat raw_value=3.8 +/- 0.33 s^-1; Km raw_value=4.4 +/- 0.90 mM; kcat/Km raw_value=860 M^-1 s^-1; source/export central value derived from same-row kcat/Km = 0.8636363636363635 s^-1*mM^-1

row_label: FgrAAO / HMFCA


column_label: Table 1. Substrate specificity of FgrAAO and FoxAAO; row FgrAAO / HMF; FgrAAO columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1); cells KM=14 +/- 2.6; kcat=29 +/- 1.7; kcat/KM=2100

normalized_value_unit_evidence: kcat normalized_value=29.0 s^-1; Km normalized_value=14.0 mM; kcat/Km normalized_value=2.0714285714285716 s^-1*mM^-1 (printed table efficiency normalized=2.1 s^-1*mM^-1)

raw_value_unit_evidence: kcat raw_value=29 +/- 1.7 s^-1; Km raw_value=14 +/- 2.6 mM; kcat/Km raw_value=2100 M^-1 s^-1; source/export central value derived from same-row kcat/Km = 2.0714285714285716 s^-1*mM^-1

row_label: FgrAAO / HMF


substrate_name: benzyl alcohol

column_label: Table 1. Substrate specificity of FgrAAO and FoxAAO; row FgrAAO / Benzyl alcohol; FgrAAO columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1); cells KM=86 +/- 12; kcat=37 +/- 2.8; kcat/KM=430

normalized_value_unit_evidence: kcat normalized_value=37.0 s^-1; Km normalized_value=86.0 mM; kcat/Km normalized_value=0.43023255813953487 s^-1*mM^-1 (printed table efficiency normalized=0.43 s^-1*mM^-1)

raw_value_unit_evidence: kcat raw_value=37 +/- 2.8 s^-1; Km raw_value=86 +/- 12 mM; kcat/Km raw_value=430 M^-1 s^-1; source/export central value derived from same-row kcat/Km = 0.43023255813953487 s^-1*mM^-1

row_label: FgrAAO / Benzyl alcohol

substrate: benzyl alcohol


substrate_name: veratryl alcohol

column_label: Table 1. Substrate specificity of FgrAAO and FoxAAO; row FgrAAO / 3,4-Dimethoxybenzyl (veratryl) alcohol; FgrAAO columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1); cells KM=3.7 +/- 0.75; kcat=41 +/- 4.0; kcat/KM=11000

normalized_value_unit_evidence: kcat normalized_value=41.0 s^-1; Km normalized_value=3.7 mM; kcat/Km normalized_value=11.08108108108108 s^-1*mM^-1 (printed table efficiency normalized=11.0 s^-1*mM^-1)

raw_value_unit_evidence: kcat raw_value=41 +/- 4.0 s^-1; Km raw_value=3.7 +/- 0.75 mM; kcat/Km raw_value=11000 M^-1 s^-1; source/export central value derived from same-row kcat/Km = 11.08108108108108 s^-1*mM^-1

substrate: veratryl alcohol


column_label: Table 1. Substrate specificity of FgrAAO and FoxAAO; row FgrAAO / 4-Methoxybenzyl (p-anisyl) alcohol; FgrAAO columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1); cells KM=59 +/- 7.2; kcat=32 +/- 1.8; kcat/KM=540

normalized_value_unit_evidence: kcat normalized_value=32.0 s^-1; Km normalized_value=59.0 mM; kcat/Km normalized_value=0.5423728813559322 s^-1*mM^-1 (printed table efficiency normalized=0.54 s^-1*mM^-1)

raw_value_unit_evidence: kcat raw_value=32 +/- 1.8 s^-1; Km raw_value=59 +/- 7.2 mM; kcat/Km raw_value=540 M^-1 s^-1; source/export central value derived from same-row kcat/Km = 0.5423728813559322 s^-1*mM^-1


organism: Fusarium oxysporum f. sp. lycopersici

column_label: Table 1. Substrate specificity of FgrAAO and FoxAAO; row FoxAAO / DFF; FoxAAO columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1); cells KM=3.7 +/- 1.0; kcat=1.4 +/- 0.13; kcat/KM=380

normalized_value_unit_evidence: kcat normalized_value=1.4 s^-1; Km normalized_value=3.7 mM; kcat/Km normalized_value=0.37837837837837834 s^-1*mM^-1 (printed table efficiency normalized=0.38 s^-1*mM^-1)

raw_value_unit_evidence: kcat raw_value=1.4 +/- 0.13 s^-1; Km raw_value=3.7 +/- 1.0 mM; kcat/Km raw_value=380 M^-1 s^-1; source/export central value derived from same-row kcat/Km = 0.37837837837837834 s^-1*mM^-1

row_label: FoxAAO / DFF


substrate_name: 3-Methoxybenzyl alcohol

column_label: Table 1. Substrate specificity of FgrAAO and FoxAAO; row FoxAAO / 3-Methoxybenzyl (m-anisyl) alcohol; FoxAAO columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1); cells KM=6.7 +/- 0.59; kcat=34 +/- 1.7; kcat/KM=5100

normalized_value_unit_evidence: kcat normalized_value=34.0 s^-1; Km normalized_value=6.7 mM; kcat/Km normalized_value=5.074626865671641 s^-1*mM^-1 (printed table efficiency normalized=5.1 s^-1*mM^-1)

raw_value_unit_evidence: kcat raw_value=34 +/- 1.7 s^-1; Km raw_value=6.7 +/- 0.59 mM; kcat/Km raw_value=5100 M^-1 s^-1; source/export central value derived from same-row kcat/Km = 5.074626865671641 s^-1*mM^-1

substrate: 3-Methoxybenzyl alcohol


column_label: Table 1. Substrate specificity of FgrAAO and FoxAAO; row FoxAAO / HMFCA; FoxAAO columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1); cells KM=3.1 +/- 0.31; kcat=5.2 +/- 0.14; kcat/KM=1700

normalized_value_unit_evidence: kcat normalized_value=5.2 s^-1; Km normalized_value=3.1 mM; kcat/Km normalized_value=1.6774193548387097 s^-1*mM^-1 (printed table efficiency normalized=1.7 s^-1*mM^-1)

raw_value_unit_evidence: kcat raw_value=5.2 +/- 0.14 s^-1; Km raw_value=3.1 +/- 0.31 mM; kcat/Km raw_value=1700 M^-1 s^-1; source/export central value derived from same-row kcat/Km = 1.6774193548387097 s^-1*mM^-1

row_label: FoxAAO / HMFCA


column_label: Table 1. Substrate specificity of FgrAAO and FoxAAO; row FoxAAO / HMF; FoxAAO columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1); cells KM=17 +/- 4.9; kcat=26 +/- 2.6; kcat/KM=1500

normalized_value_unit_evidence: kcat normalized_value=26.0 s^-1; Km normalized_value=17.0 mM; kcat/Km normalized_value=1.5294117647058822 s^-1*mM^-1 (printed table efficiency normalized=1.5 s^-1*mM^-1)

raw_value_unit_evidence: kcat raw_value=26 +/- 2.6 s^-1; Km raw_value=17 +/- 4.9 mM; kcat/Km raw_value=1500 M^-1 s^-1; source/export central value derived from same-row kcat/Km = 1.5294117647058822 s^-1*mM^-1

row_label: FoxAAO / HMF