column_label: Table 1. Substrate specificity of FgrAAO and FoxAAO; row FoxAAO / Benzyl alcohol; FoxAAO columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1); cells KM=30 +/- 19; kcat=31 +/- 4.2; kcat/KM=1000 (350 +/- 20)a

normalized_value_unit_evidence: kcat normalized_value=31.0 s^-1; Km normalized_value=30.0 mM; kcat/Km normalized_value=1.0333333333333334 s^-1*mM^-1 (printed table efficiency normalized=1.0 s^-1*mM^-1)

raw_value_unit_evidence: kcat raw_value=31 +/- 4.2 s^-1; Km raw_value=30 +/- 19 mM; kcat/Km raw_value=1000 (350 +/- 20)a M^-1 s^-1; source/export central value derived from same-row kcat/Km = 1.0333333333333334 s^-1*mM^-1

row_label: FoxAAO / Benzyl alcohol


enzyme_display_name: aryl-alcohol oxidase

organism: Fusarium oxysporum f. sp. lycopersici

substrate_name: veratryl alcohol

source_db: oed

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

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.

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

column_label: Table 1. Substrate specificity of FgrAAO and FoxAAO; row FoxAAO / 3,4-Dimethoxybenzyl (veratryl) alcohol; FoxAAO columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1); cells KM=3.0 +/- 0.24; kcat=25 +/- 1.2; kcat/KM=8300

normalized_value_unit_evidence: kcat normalized_value=25.0 s^-1; Km normalized_value=3.0 mM; kcat/Km normalized_value=8.333333333333334 s^-1*mM^-1 (printed table efficiency normalized=8.3 s^-1*mM^-1)

raw_value_unit_evidence: kcat raw_value=25 +/- 1.2 s^-1; Km raw_value=3.0 +/- 0.24 mM; kcat/Km raw_value=8300 M^-1 s^-1; source/export central value derived from same-row kcat/Km = 8.333333333333334 s^-1*mM^-1

data_origin: experimental

enzyme: aryl-alcohol oxidase

substrate: veratryl alcohol

status: verified

source: oed


substrate_name: 4-Methoxybenzyl alcohol

verification_status: unverified

substrate: 4-Methoxybenzyl alcohol

status: unverified


enzyme_display_name: pyranose oxidase

organism: Phanerochaete chrysosporium

verification_status: corrected

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

enzyme: pyranose oxidase

status: corrected


substrate_name: alpha-D-Glucose

column_label: Table 5, alpha-D(+)-Glucose row, kcat, Km, and independently printed kcat/Km columns.

row_label: alpha-D(+)-Glucose

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

substrate: alpha-D-Glucose


substrate_name: beta-D-Glucose

column_label: Table 5, beta-D(+)-Glucose row, kcat, Km, and independently printed kcat/Km columns.

row_label: beta-D(+)-Glucose

substrate: beta-D-Glucose


substrate_name: D-Glucose

substrate: D-Glucose


substrate_name: D-Xylose

row_label: D-Xylose

substrate: D-Xylose


substrate_name: L-Sorbose

row_label: L-Sorbose

substrate: L-Sorbose


substrate_name: Maltose

row_label: Maltose

substrate: Maltose


smiles: O=O

column_label: PMID 9210340 / DOI 10.1007/s002530050964, abstract/prose: P2O reaction at pH 8.0 gives kcat 111.0 s^-1 and affinity constant Km 83.2 uM for oxygen.

raw_value_unit_evidence: kcat = 111.0 s^-1; Km = 83.2 uM for oxygen

row_label: oxygen

table_label: Springer abstract prose


organism: Tricholoma matsutake

substrate_name: D-arabinose

source_db: brenda

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

assay_conditions_summary: pH 7

column_label: PMID 14730138 Table 2 row D(-)-arabinose, columns Km, kcat, and kcat/Km; raw cells Km 174 mM, kcat 7.79 s^-1, kcat/Km 0.045 s^-1 mM^-1.

row_label: D(-)-arabinose / T. matsutake pyranose oxidase

table_label: PMID 14730138 Table 2, apparent kinetic constants for several sugars

source_databases_merged: brenda uniprot

substrate: D-arabinose

source: brenda


substrate_name: D-galactose

substrate: D-galactose


substrate_name: D-xylose

column_label: PMID 14730138 Table 2 row D(+)-xylose, columns Km, kcat, and kcat/Km; raw cells Km 45.8 mM, kcat 55.8 s^-1, kcat/Km 1.2 s^-1 mM^-1.

row_label: D(+)-xylose / T. matsutake pyranose oxidase

substrate: D-xylose


substrate_name: trehalose

column_label: PMID 14730138 Table 2 row trehalose, columns Km, kcat, and kcat/Km; raw cells Km 192 mM, kcat 59.6 s^-1, kcat/Km 0.31 s^-1 mM^-1.

row_label: trehalose / T. matsutake pyranose oxidase

substrate: trehalose


substrate_name: D-maltose

column_label: PMID 14730138 Table 2 row maltose, columns Km, kcat, and kcat/Km; raw cells Km 329 mM, kcat 62.9 s^-1, kcat/Km 0.19 s^-1 mM^-1.

row_label: maltose / T. matsutake pyranose oxidase

substrate: D-maltose


substrate_name: L-sorbose

column_label: PMID 14730138 Table 2 row L(-)-sorbose, columns Km, kcat, and kcat/Km; raw cells Km 26.4 mM, kcat 74.6 s^-1, kcat/Km 2.8 s^-1 mM^-1.

row_label: L(-)-sorbose / T. matsutake pyranose oxidase

substrate: L-sorbose


column_label: PMID 14730138 Table 2 row 1,5-anhydro-D-glucitol, columns Km, kcat, and kcat/Km; raw cells Km 10.7 mM, kcat 76.7 s^-1, kcat/Km 7.2 s^-1 mM^-1.

row_label: 1,5-anhydro-D-glucitol / T. matsutake pyranose oxidase


organism: Pleurotus sapidus

substrate_name: benzyl alcohol

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

assay_conditions_summary: pH 6

column_label: Table 4, row group Benzyl alcohol, metric rows Km [uM], kcat [s^-1], and kcat Km^-1 [s^-1 mM^-1], column P. sapidus AAO expressed in C. cinerea

raw_value_unit_evidence: P. sapidus AAO expressed in C. cinerea column: Km 784 uM; kcat 38 s^-1; kcat Km^-1 48 s^-1 mM^-1 printed rounded

row_label: Benzyl alcohol

table_label: Table 4 Kinetic parameters of recombinant P. sapidus AAO with different substrates in comparison to other native and recombinant Pleurotus AAOs

substrate: benzyl alcohol


column_label: Table 4, row group Veratryl alcohol, metric rows Km [uM], kcat [s^-1], and kcat Km^-1 [s^-1 mM^-1], column P. sapidus AAO expressed in C. cinerea

raw_value_unit_evidence: P. sapidus AAO expressed in C. cinerea column: Km 529 uM; kcat 70 s^-1; kcat Km^-1 132 s^-1 mM^-1 printed rounded

row_label: Veratryl alcohol


substrate_name: anisyl alcohol

column_label: Table 4, row group Anisyl alcohol, metric rows Km [uM], kcat [s^-1], and kcat Km^-1 [s^-1 mM^-1], column P. sapidus AAO expressed in C. cinerea

raw_value_unit_evidence: P. sapidus AAO expressed in C. cinerea column: Km 59 uM; kcat 203 s^-1; kcat Km^-1 3466 s^-1 mM^-1

row_label: Anisyl alcohol

substrate: anisyl alcohol


enzyme_display_name: alcohol oxidase

organism: Ogataea thermomethanolica (nom. inval.)

substrate_name: methanol

smiles: CO

column_label: Table 3 row Methanol: Vmax 0.24 nmole/min; Km 0.27 mM; kcat 3628.76 min^-1; kcat/Km 13,638.37 min^-1 mM^-1; note says kcat calculated for octameric enzyme.

raw_value_unit_evidence: Vmax raw_value=0.24 nmole/min; Km raw_value=0.27 mM; kcat raw_value=3628.76 min^-1; kcat/Km raw_value=13,638.37 min^-1 mM^-1.

row_label: Methanol

table_label: Primary article PDF page 5 / printed page 30, Table 3

enzyme: alcohol oxidase

substrate: methanol


smiles: CCCO


substrate_name: ethanol

smiles: CCO

substrate: ethanol


organism: Trametes sp.

substrate_name: D-glucose

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

mutation_type: substitution

column_label: Table 1 columns 'kcat (s^-1)', 'Km (mM)', and 'kcat/Km (M^-1 s^-1)' for TsPOx/E539K with substrate D-glucose under assay conditions pH 6.5 and 30 C (Methods: 1-50 mM D-glucose; activity assay at pH 6.5 and 30 C).

table_label: Table 1 Biochemical properties of TsPOx, its mutants, and other pyranose oxidases

substrate: D-glucose


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

column_label: Table 1 columns 'kcat (s^-1)', 'Km (mM)', and 'kcat/Km (M^-1 s^-1)' for TsPOx/K312E with substrate D-glucose under assay conditions pH 6.5 and 30 C (Methods: 1-50 mM D-glucose; activity assay at pH 6.5 and 30 C).


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

column_label: Table 1 columns 'kcat (s^-1)', 'Km (mM)', and 'kcat/Km (M^-1 s^-1)' for TsPOx/K312E/E539K with substrate D-glucose under assay conditions pH 6.5 and 30 C (Methods: 1-50 mM D-glucose; activity assay at pH 6.5 and 30 C).


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

column_label: Table 1 columns 'kcat (s^-1)', 'Km (mM)', and 'kcat/Km (M^-1 s^-1)' for TsPOx/T166A/E539K with substrate D-glucose under assay conditions pH 6.5 and 30 C (Methods: 1-50 mM D-glucose; activity assay at pH 6.5 and 30 C).


column_label: Table 1 columns 'kcat (s^-1)', 'Km (mM)', and 'kcat/Km (M^-1 s^-1)' for TsPOx/TsPOx with substrate D-glucose under assay conditions pH 6.5 and 30 C (Methods: 1-50 mM D-glucose; activity assay at pH 6.5 and 30 C).

raw_value_unit_evidence: Table 1 row TsPOx: kcat 6.1 ± 0.2 s^-1; Km 1.2 ± 0.1 mM; kcat/Km 5083 M^-1 s^-1

row_label: TsPOx


organism: Arthrobacter chlorophenolicus

sequence_variant_note: Resolved canonical sequence from UniProtKB:B8H740 and applied mutation signature M359R to reconstruct the assayed variant sequence.

smiles: CCCCCCO

assay_conditions_summary: pH 8; 303.15 K; buffer air-saturated 100 mM potassium phosphate

table_label: Table 2: Kinetic parameters of choline oxidase variants with hexan-1-ol


sequence_variant_note: Resolved canonical sequence from UniProtKB:B8H740 and applied mutation signature S101A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:B8H740 and applied mutation signature S101A/D250G/F253R/V355T/F357R/M359R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:B8H740 and applied mutation signature S101A/V355T/F357R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:B8H740 and applied mutation signature S101A/V355T/F357R/M359R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:B8H740 and applied mutation signature V355T/F357R to reconstruct the assayed variant sequence.


row_label: WT


organism: Trametes ochracea

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


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


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


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


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


organism: Aspergillus terreus

substrate_name: 3,4-dimethoxybenzyl alcohol

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

assay_conditions_summary: pH 6; 303.15 K; 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); expected value tuple belongs to a different substrate row.

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.

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

substrate: 3,4-dimethoxybenzyl alcohol


substrate_name: 3-Methoxybenzyl alcohol

substrate: 3-Methoxybenzyl alcohol


column_label: Table 2 row Benzyl alcohol columns kcat and kcat/Km; kcat rounds toward the export but the explicit kcat/Km cell does not equal the exported computed ratio.

normalized_value_unit_evidence: Benzyl alcohol normalized Km=10.80 mM, kcat=2.1563333 s^-1, kcat/Km=0.1996667 s^-1*mM^-1; expected kcat=2.2 s^-1 and expected kcat_over_km=0.20370370370370372 s^-1*mM^-1.

raw_value_unit_evidence: Table 2 Benzyl alcohol row reports Km 10.80 mM, kcat 129.38 min^-1, and kcat/Km 11.98 min^-1 mM^-1.


substrate_name: 4-Methoxybenzyl alcohol

substrate: 4-Methoxybenzyl alcohol


organism: Phanerodontia chrysosporium

kcat_display: Not reported

kcat_over_km_display: Not reported

column_label: Visible primary ScienceDirect Table 1, row Methanol, column Km [mM], reports 36.6.

normalized_value_unit_evidence: Km normalized_value=36.6 mM.

raw_value_unit_evidence: Methanol Km = 36.6 mM.

table_label: Table 1. Substrate specificity and kinetic parameters of AOX from P. chrysosporium


substrate_name: glycerol

smiles: C(C(CO)O)O

column_label: ScienceDirect Table 1 row Glycerol, column Km [mM], reports 1.9.

normalized_value_unit_evidence: Km normalized 1.9 mM.

raw_value_unit_evidence: Km raw 1.9 mM for glycerol.

row_label: Glycerol

table_label: Table 1. Substrate specificity and kinetic parameters of AOX from P. chrysosporium.

substrate: glycerol


column_label: Visible primary ScienceDirect Table 1, row Ethanol, column Km [mM], reports 22.5.

normalized_value_unit_evidence: Km normalized_value=22.5 mM.

raw_value_unit_evidence: Ethanol Km = 22.5 mM.

row_label: Ethanol


substrate_name: n-Pentanol

smiles: CCCCCO

column_label: ScienceDirect Table 1 row n-Pentanol, column Km [mM], reports 10.9.

normalized_value_unit_evidence: Km normalized 10.9 mM.

raw_value_unit_evidence: Km raw 10.9 mM for n-Pentanol.

row_label: n-Pentanol

substrate: n-Pentanol


substrate_name: n-Propanol

substrate: n-Propanol


enzyme_display_name: Pyranose 2-oxidase

organism: Phlebiopsis gigantea

source_db: uniprot

column_label: The abstract reports Km values for D-glucose, L-sorbose, D-xylose and oxygen were 1.1 mM, 50.0 mM, 29.4 mM and 0.65 mM, respectively.

raw_value_unit_evidence: Km raw_value=0.65 mM raw_unit=mM

row_label: Prose segment: oxygen Km

table_label: PubMed PMID 8319689 abstract

enzyme: Pyranose 2-oxidase

source: uniprot


raw_value_unit_evidence: Km raw_value=1.1 mM raw_unit=mM

row_label: Prose segment: D-glucose Km


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


raw_value_unit_evidence: Km raw_value=29.4 mM raw_unit=mM

row_label: Prose segment: D-xylose Km


raw_value_unit_evidence: Km raw_value=50.0 mM raw_unit=mM

row_label: Prose segment: L-sorbose Km


organism: Pleurotus eryngii

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H502A with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -11, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H546A with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H546S with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


organism: Thermothelomyces thermophilus

assay_conditions_summary: pH 6; 303.15 K; buffer pH 6

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

normalized_value_unit_evidence: KM paper=13.02 mM; kcat paper=0.0008666666666666667 s^-1; export kcat=0.0008; export row is a source-tuple split/demote target.

table_label: Table 1. MtAAOx substrate specificity and kinetic parameters


column_label: Table 1 row anisyl alcohol lists KM 1.03 +/- 0.07 mM, kcat 0.451 +/- 0.019 min^-1, and kcat/KM 0.450 +/- 0.019 min^-1 mM^-1.

normalized_value_unit_evidence: Km normalized_value=1.03 mM; kcat normalized_value=0.0075 s^-1; explicit kcat/KM normalized_value=0.0075 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=1.03 mM; kcat raw_value=0.451 min^-1; kcat/KM raw_value=0.450 min^-1 mM^-1

row_label: anisyl alcohol

table_label: Table 1. MtAAOx substrate specificity and kinetic parameters.


substrate_name: cinnamyl alcohol

column_label: Table 1 row cinnamyl alcohol lists KM 0.49 +/- 0.01 mM, kcat 0.414 +/- 0.016 min^-1, and kcat/KM 0.838 +/- 0.032 min^-1 mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.49 mM; kcat normalized_value=0.0069 s^-1; explicit kcat/KM normalized_value=0.0139666666666667 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.49 mM; kcat raw_value=0.414 min^-1; kcat/KM raw_value=0.838 min^-1 mM^-1

row_label: cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: veratryl alcohol

column_label: Table 1 row veratryl alcohol lists KM 0.47 +/- 0.15 mM, kcat 0.317 +/- 0.019 min^-1, and kcat/KM 0.676 +/- 0.041 min^-1 mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.47 mM; kcat normalized_value=0.0053 s^-1; explicit kcat/KM normalized_value=0.0112666666666667 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.47 mM; kcat raw_value=0.317 min^-1; kcat/KM raw_value=0.676 min^-1 mM^-1

row_label: veratryl alcohol

substrate: veratryl alcohol


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.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -12, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -4, so it is treated as a source-provided variant sequence.


organism: Trametes pubescens

substrate_name: L-arabinose (at pH 6.5 and 30 degrees Celsius)

proof_lines:
Pyranose 2-oxidase
L-arabinose
Trametes pubescens


substrate_name: D-galactose (at pH 6.5 and 30 degrees Celsius)

proof_lines:
Pyranose 2-oxidase
D-galactose
Trametes pubescens


substrate_name: melibiose (at pH 6.5 and 30 degrees Celsius)

proof_lines:
Pyranose 2-oxidase
melibiose
Trametes pubescens


substrate_name: L-sorbose (at pH 6.5 and 30 degrees Celsius)

proof_lines:
Pyranose 2-oxidase
L-sorbose
Trametes pubescens


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F501A with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F501Y with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


enzyme_display_name: pyridoxine 4-oxidase

organism: Microbacterium luteolum

sequence_source: multiple

column_label: Page 1026, Results subsection 'Substrate and cofactor specificity'; 2,6-dichloroindophenol metric-labeled Km prose.

normalized_value_unit_evidence: 9.71 +/- 1.65 uM = 0.00971 +/- 0.00165 mM; stored 0.0097 mM is within printed uncertainty/rounding.

raw_value_unit_evidence: 2,6-dichloroindophenol (Km, 9.71 +/- 1.65 uM).

table_label: Results prose: Substrate and cofactor specificity (page 1026)

enzyme: pyridoxine 4-oxidase


substrate_name: vitamin K3

column_label: Page 1026, Results subsection 'Substrate and cofactor specificity'; vitamin K3 metric-labeled Km prose.

normalized_value_unit_evidence: 50.16 +/- 14.6 uM = 0.05016 +/- 0.0146 mM; stored 0.05 mM is within printed uncertainty/rounding.

row_label: vitamin K3

substrate: vitamin K3


substrate_name: pyridoxine

column_label: Page 1026, Results subsection 'Substrate and cofactor specificity'; pyridoxine metric-labeled Km prose.

normalized_value_unit_evidence: 54.5 +/- 5.7 uM = 0.0545 +/- 0.0057 mM; stored 0.054 mM is within printed uncertainty/rounding.

raw_value_unit_evidence: PN showed reactivity only toward PN (Km, 54.5 +/- 5.7 uM; kcat, 28.1 s^-1).

row_label: pyridoxine (PN)

substrate: pyridoxine


organism: Peniophora sp.

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

source_databases_merged: brenda skid


substrate_name: D-xylose

substrate: D-xylose


substrate_name: L-sorbose

substrate: L-sorbose


organism: Mesorhizobium loti

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H462A to reconstruct the assayed variant sequence.


organism: Pleurotus pulmonarius

substrate_name: m-anisyl alcohol

substrate: m-anisyl alcohol


substrate_name: 3,4-dimethoxybenzyl alcohol


substrate_name: p-anisyl alcohol

km_display: Not reported

assay_conditions_summary: pH 6; buffer Chrome Assay condition: Kinetic constants calculated in 100 mM phosphate

column_label: ScienceDirect Table 2, row p-Anisyl alcohol, column Kcat (s-1), reports 48.46.

normalized_value_unit_evidence: Kcat normalized_value=48.46 normalized_unit=s-1; queued value 48.5 s-1 matches by rounding.

raw_value_unit_evidence: Kcat raw_value=48.46 raw_unit=s-1

row_label: p-Anisyl alcohol

table_label: Table 2. Kinetic constants of AAO from P. pulmonarius

substrate: p-anisyl alcohol


enzyme_display_name: UniProt P0CS93

organism: Fusarium graminearum

source_db: skid

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

smiles: C=C(CO)CO

proof_lines: oxidizes a range of primary alcohols to aldehydes

source_databases_merged: skid uniprot

enzyme: UniProt P0CS93

source: skid


substrate_name: D-galactose

substrate: D-galactose


organism: Methylovorus sp. MP688

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

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


column_label: Table 3 lists MetspHMFO DFF row columns kcat / Km / kcat/Km as 6.1+/-0.2 min^-1 / 6.8+/-0.6 mM / 0.9+/-0.1 mM^-1 min^-1

row_label: MetspHMFO row / DFF substrate

table_label: PMC7414962 Table 3


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H91N/L170M with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H91N/L170M/F501W with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


organism: [Candida] methanosorbosa

substrate_name: methanol

substrate: methanol


substrate_name: ethanol

substrate: ethanol


substrate_name: benzyl alcohol

substrate: benzyl alcohol


enzyme_display_name: cholesterol oxidase

organism: Castellaniella sp.

substrate_name: cholesterol

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

assay_conditions_summary: pH 8

enzyme: cholesterol oxidase

substrate: cholesterol


organism: Brevibacterium sterolicum


organism: Pseudomonas aeruginosa

column_label: Abstract reports the Km value and Vmax value for cholesterol were 92.6 microM and 15.9 micromol/min/mg of protein, respectively.

raw_value_unit_evidence: Km raw_value=92.6 microM raw_unit=microM

row_label: Pseudomonas aeruginosa PA157 cholesterol oxidase / cholesterol

table_label: PubMed XML abstract PMID 25573142


enzyme_display_name: galactose oxidase

enzyme: galactose oxidase


substrate_name: galactoglucomannan

column_label: Downloaded ScienceDirect/BBA PDF Table 1 lists the GaO / Galacto-glucomannan row with kcat=195 +/- 28 min^-1, Km=0.16 +/- 0.07 mM, and kcat/Km=1200 +/- 500 min^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=3.25 normalized_unit=s^-1 from 195 min^-1; Km normalized_value=0.16 normalized_unit=mM; kcat/Km normalized_value=20 normalized_unit=s^-1*mM^-1 from 1200 min^-1*mM^-1.

raw_value_unit_evidence: Table 1 GaO row for Galacto-glucomannan reports kcat raw_value=195 +/- 28 raw_unit=min^-1, Km raw_value=0.16 +/- 0.07 raw_unit=mM, and kcat/Km raw_value=1200 +/- 500 raw_unit=min^-1*mM^-1.

row_label: GaO / Galacto-glucomannan

table_label: PDF Table 1

substrate: galactoglucomannan


organism: Chryseobacterium gleum

substrate_name: taurocholate

substrate: taurocholate


organism: Chrysomela tremula

substrate_name: 2-hydroxybenzyl alcohol

proof_lines:
2-hydroxybenzyl alcohol
pH 6.0

substrate: 2-hydroxybenzyl alcohol


organism: Trametes ochracea

proof_lines: Pyranose 2-oxidase from Trametes multicolor


substrate_name: D-glucose

substrate: D-glucose


organism: Chrysomela populi


organism: Gloeophyllum trabeum


organism: Gibberella zeae

raw_value_unit_evidence: Table 2 wild type row for 2-methylene-1,3-propanediol reports Km = 57 +/- 4.1 mM, kcat = 283 +/- 7.0 s^-1, and kcat/Km = 4965 +/- 377 M^-1 s^-1.

row_label: wild type / 2-methylene-1,3-propanediol

table_label: Table 2. Kinetic parameters for 2-methylene-1,3-propanediol


organism: Fusarium sp.

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


organism: Streptomyces sp.


substrate_name: pregnenolone

substrate: pregnenolone


proof_lines:
pH 7.0, 37°C, mutant enzyme V145E
V145E mutant


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


proof_lines: wild-type enzyme, determined by cholest-4-en-3-one detection


substrate_name: guar

substrate: guar


organism: Pleurotus eryngii

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

smiles: CC=CC=CCO


organism: Streptomyces virginiae

substrate_name: diosgenin

substrate: diosgenin


substrate_name: dehydroepiandrosterone

substrate: dehydroepiandrosterone


substrate_name: sitosterol

substrate: sitosterol


enzyme_display_name: 2-oxoglutarate reductase

organism: Escherichia coli

enzyme: 2-oxoglutarate reductase


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


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


enzyme_display_name: L-lactate dehydrogenase (cytochrome)

organism: Saccharomyces cerevisiae

substrate_name: Fluoropyruvate

enzyme: L-lactate dehydrogenase (cytochrome)

substrate: Fluoropyruvate


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: L-lactate

substrate: L-lactate


substrate_name: L-Mandelate

proof_lines: wild type enzyme with ferricyanide as electron acceptor

substrate: L-Mandelate


proof_lines: A198G/L230G mutant enzyme with ferricyanide as electron acceptor


enzyme_display_name: alcohol dehydrogenase (cytochrome c)

organism: Pseudomonas putida

substrate_name: ethanol

proof_lines: pH 9.0, temperature not specified in the publication, in presence of ethylamine

proof_lines: pH 9.0, temperature not specified in the publication, in presence of pentylamine

enzyme: alcohol dehydrogenase (cytochrome c)

substrate: ethanol


substrate_name: Propanol

assay_conditions_summary: pH 9

substrate: Propanol


proof_lines: pH 9.0, temperature not specified in the publication


enzyme_display_name: D-lactate dehydrogenase (cytochrome)

substrate_name: D-lactate

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

enzyme: D-lactate dehydrogenase (cytochrome)

substrate: D-lactate


smiles: CCCC(C(=O)[O-])O


enzyme_display_name: glucose oxidase

organism: Aspergillus niger

substrate_name: phenazine methosulfate

enzyme: glucose oxidase

substrate: phenazine methosulfate


substrate_name: cholesterol

substrate: cholesterol


organism: Streptomyces sp. SA-COO

proof_lines: pH 7.0, 37°C, mutant enzyme T168C/A276C, cholesterol solubilized in detergent micelles as a substrate


proof_lines: pH 7.0, 37°C, wild-type enzyme, cholesterol solubilized in detergent micelles as a substrate


proof_lines: pH 7.0, 37°C, mutant enzyme L80C, cholesterol solubilized in detergent micelles as a substrate


enzyme_display_name: ketol-acid reductoisomerase [NAD(P)+]

organism: Ignisphaera aggregans

substrate_name: NADH

assay_conditions_summary: pH 7; cofactor NADH

proof_lines: pH 7, temperature not specified in the publication, cosubstrate: (2S)-2-hydroxy-2-methyl-3-oxobutanoate

enzyme: ketol-acid reductoisomerase [NAD(P)+]

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 7; cofactor NADPH

substrate: NADPH


substrate_name: ferricytochrome c

proof_lines: pH 7.5, 25°C, Tris-HCl buffer, mutant Y143F

proof_lines: pH 7.0, 5°C, phosphate buffer, mutant Y143F

proof_lines: pH 7.0, 30°C, phosphate buffer, mutant Y143F

substrate: ferricytochrome c


proof_lines: pH 7.5, 25°C, Tris-HCl buffer, wild-type enzyme

proof_lines: pH 7.0, 5°C, phosphate buffer, wild-type enzyme


assay_conditions_summary: pH 7.5; 298.15 K; cofactor FMN

proof_lines: Y143F mutant with cytochrome c as electron acceptor

proof_lines: native enzyme and Y143F mutant with ferricyanide as electron acceptor


proof_lines: native enzyme mutant with ferricyanide as electron acceptor


enzyme_display_name: UniProt Q9UJM8

organism: Homo sapiens

source_license: CC BY-NC-ND 4.0

smiles: CCCCCCC(=O)C(=O)[O-]

enzyme: UniProt Q9UJM8


proof_lines:
Raw SKiD Env: Temp=30°C, pH=9
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=7


enzyme_display_name: long-chain-alcohol oxidase

organism: Simmondsia chinensis

substrate_name: Dodecanol

smiles: CCCCCCCCCCCCO

enzyme: long-chain-alcohol oxidase

substrate: Dodecanol


organism: Rhodopseudomonas palustris


proof_lines: mutant enzyme R91D/E408P/N410K, pH and temperature not specified in the publication


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


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


organism: Staphylococcus aureus

assay_conditions_summary: cofactor NADPH


substrate_name: ribulose 5-phosphate

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

substrate: ribulose 5-phosphate


enzyme_display_name: (S)-2-hydroxy-acid oxidase

organism: Rattus sp.

substrate_name: L-leucine

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

proof_lines:
isozymes beta1 and beta2
isozyme beta2
pH 7.5

enzyme: (S)-2-hydroxy-acid oxidase

substrate: L-leucine


proof_lines:
isozyme beta1
isozyme beta2
pH 7.0


substrate_name: L-Phenyllactate

proof_lines:
isozyme beta1
isozyme beta2
pH 7.0 and 7.5

substrate: L-Phenyllactate


proof_lines:
isozyme beta1
isozyme beta2
pH 7.5


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


organism: Aerococcus viridans

smiles: O=O

assay_conditions_summary: cofactor FMN


substrate_name: (S)-lactate

substrate: (S)-lactate


enzyme_display_name: choline oxidase

organism: Cylindrocarpon didymum

substrate_name: choline

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

enzyme: choline oxidase

substrate: choline


substrate_name: Betaine aldehyde

substrate: Betaine aldehyde


substrate_name: N,N-Dimethylaminoethanol

smiles: CN(C)CCO

substrate: N,N-Dimethylaminoethanol


organism: Tanacetum vulgare


substrate_name: n-Octanol

smiles: CCCCCCCCO

substrate: n-Octanol


substrate_name: geraniol

smiles: CC(=CCCC(=CCO)C)C

substrate: geraniol


proof_lines:
25°C, wild-type enzyme
35°C, wild-type enzyme
wild-type


proof_lines:
25°C, mutant enzyme E160G/V198I
35°C, mutant enzyme E160G/V198I


proof_lines: 25°C, mutant enzyme E160G/V198I/G36S/T103S/A232S/F277Y

proof_lines: 35°C, mutant enzyme E160G/V198I/G36S/T103S/A232S/F277Y


organism: Mesostigma viride

substrate_name: glycolate

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

substrate: glycolate


substrate_name: L-lactate

substrate: L-lactate


organism: Mycolicibacterium smegmatis


proof_lines:
4°C, pH 7
25°C, pH 7


proof_lines:
4°C, pH 7
25°C, pH 7
at pH 7


enzyme_display_name: ecdysone oxidase

organism: Calliphora vicina

substrate_name: oxidized 2,6-dichloroindophenol

enzyme: ecdysone oxidase

substrate: oxidized 2,6-dichloroindophenol


substrate_name: ecdysone

proof_lines:
optical assay
radio assay

substrate: ecdysone


organism: Rattus norvegicus


substrate_name: betaine aldehyde

proof_lines: oxidation of choline is competitively inhibited

substrate: betaine aldehyde


enzyme_display_name: N-acylhexosamine oxidase

organism: Pseudomonas sp.

substrate_name: N-acetyl-D-galactosamine

enzyme: N-acylhexosamine oxidase

substrate: N-acetyl-D-galactosamine


substrate_name: N-Glycolyl-D-glucosamine

substrate: N-Glycolyl-D-glucosamine


substrate_name: D-galactosamine

substrate: D-galactosamine


substrate_name: N,N-diacetylchitobiose

substrate: N,N-diacetylchitobiose


substrate_name: N-acetyl muramic acid

substrate: N-acetyl muramic acid


substrate_name: D-mannose

substrate: D-mannose


substrate_name: L-Mandelate

substrate: L-Mandelate


substrate_name: DL-glycerate

proof_lines:
at pH 6.0
at pH 7.0

substrate: DL-glycerate


substrate_name: (S)-lactate

substrate: (S)-lactate


substrate_name: DL-alpha-hydroxy-n-valerate

substrate: DL-alpha-hydroxy-n-valerate


organism: Fusarium oxysporum

substrate_name: choline

substrate: choline


substrate_name: Betaine aldehyde

substrate: Betaine aldehyde


substrate_name: glycolate

proof_lines: pH 7.0, 30°C, recombinant enzyme, first order

proof_lines: pH 7.5, 30°C, recombinant enzyme, first order

proof_lines: pH 9.0, 30°C, recombinant enzyme, first order

substrate: glycolate


smiles: CCCCCCC(C(=O)[O-])O


organism: Amaranthus retroflexus

proof_lines:
pH 7.5, mesophyll cell isozyme
pH 7.5, bundle sheath cell isozyme


enzyme_display_name: secondary-alcohol oxidase

substrate_name: polyvinyl alcohol

enzyme: secondary-alcohol oxidase

substrate: polyvinyl alcohol


smiles: CCCC(CCC)O


organism: Geotrichum candidum


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


enzyme_display_name: thiamine oxidase

organism: unidentified soil bacterium

substrate_name: thiamine

enzyme: thiamine oxidase

substrate: thiamine


organism: Pseudomonas putida


organism: Manduca sexta

substrate_name: ecdysone

substrate: ecdysone


enzyme_display_name: Glycolate oxidase

organism: Spinacia oleracea

substrate_name: L-lactate

proof_lines: kcat is 20 sec(-1) with glycolate as substrate. kcat is 11 sec(-1) with L-lactate as substrate. kcat is 13.2 sec(-1) with L-2-hydroxbyutanoate as substrate. kcat is 0.09 sec(-1) with L-mandelate as substrate.

enzyme: Glycolate oxidase

substrate: L-lactate


substrate_name: L-mandelate

substrate: L-mandelate


enzyme_display_name: nucleoside oxidase

organism: Stenotrophomonas maltophilia

substrate_name: Inosine

enzyme: nucleoside oxidase

substrate: Inosine


smiles: OO


enzyme_display_name: hydroxyphytanate oxidase

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

enzyme: hydroxyphytanate oxidase


enzyme_display_name: UniProt P56216

organism: Penicillium simplicissimum

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=25°C, pH=10

enzyme: UniProt P56216


enzyme_display_name: alditol oxidase

organism: Streptomyces coelicolor

smiles: CCCC(CO)N

assay_conditions_summary: pH 7.5; 303.15 K; buffer 50 mM sodium phosphate

proof_lines: in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C

enzyme: alditol oxidase


smiles: C=CCCO


smiles: CCC(CO)O


smiles: C=CC(CO)O


smiles: CCCC(CO)O


substrate_name: L-arabinose

substrate: L-arabinose


smiles: CCCCC(CO)O


smiles: C(CO)C(CO)O


organism: Ralstonia solanacearum

substrate_name: N-acetyl-beta-D-glucosamine

raw_value_unit_evidence: Table 1 row GlcNAc (N-acetyl-D-glucosamine), K_M [mM] / A3RXB7 column = 0.26; adjacent specific activity / A3RXB7 column = 6.08 umol min^-1 mg^-1.

row_label: A3RXB7 / GlcNAc

table_label: Table 1

substrate: N-acetyl-beta-D-glucosamine


substrate_name: D-galactosamine

column_label: PMID 34709726 / DOI 10.1002/cbic.202100510, Table 1, row D-galactosamine, column K_M [mM] / A3RXB7 = 1.4, which does not exactly match the exported 1.35 mM.

normalized_value_unit_evidence: Km=1.4 mM in the accessible primary table; export expects 1.35 mM.

raw_value_unit_evidence: Table 1 row D-galactosamine, K_M [mM] / A3RXB7 column = 1.4; adjacent specific activity / A3RXB7 column = 0.67 umol min^-1 mg^-1.

row_label: A3RXB7 / D-galactosamine

substrate: D-galactosamine


substrate_name: D-galactose

column_label: PMID 34709726 / DOI 10.1002/cbic.202100510, Table 1, row D-galactose, column K_M [mM] / A3RXB7 = 102.

raw_value_unit_evidence: Table 1 row D-galactose, K_M [mM] / A3RXB7 column = 102; adjacent specific activity / A3RXB7 column = 0.21 umol min^-1 mg^-1.

row_label: A3RXB7 / D-galactose

substrate: D-galactose


enzyme_display_name: 2-Hydroxyacid oxidase 2

substrate_name: L-2-hydroxybutanoate (with DCIP as electron acceptor)

proof_lines: kcat is 0.99 sec(-1) for the oxidation of L-2-hydroxyoctanoate with DCIP instead of O2 as electron acceptor. kcat is 0.34 sec(-1) for the oxidation of L-2-hydroxyhexadecanoate with DCIP instead of O2 as electron acceptor (PubMed:15683236).

enzyme: 2-Hydroxyacid oxidase 2


substrate_name: L-mandelate (with DCIP as electron acceptor)


enzyme_display_name: 2-Hydroxyacid oxidase 1

organism: Homo sapiens

substrate_name: L-lactate (at pH 7.0 and 37 degrees Celsius, with DCIP as electron acceptor)

proof_lines: kcat is 3.6 sec(-1) for the oxidation of glycolate with DCIP as electron acceptor (at pH 7.0 and 37 degrees Celsius) (PubMed:17669354). kcat is 4.1 sec(-1) for the oxidation of glycolate with DCIP as electron acceptor (at pH 7.5 and 37 degr

enzyme: 2-Hydroxyacid oxidase 1


substrate_name: L-mandelate (at pH 7.0 and 37 degrees Celsius, with DCIP as electron acceptor)


enzyme_display_name: Glycolate oxidase 2

organism: Arabidopsis thaliana

substrate_name: (S)-lactate

proof_lines: kcat is 30.10 sec(-1) with glycolate as substrate (at pH 8 and 30 degrees Celsius).

enzyme: Glycolate oxidase 2


substrate_name: glyoxylate

assay_conditions_summary: pH 7; cofactor FMN

substrate: glyoxylate


enzyme_display_name: nucleoside oxidase (H2O2-forming)

organism: Elizabethkingia meningoseptica

enzyme: nucleoside oxidase (H2O2-forming)


substrate_name: guanosine

substrate: guanosine


substrate_name: 6-mercaptopurine arabinoside

substrate: 6-mercaptopurine arabinoside


substrate_name: thymidine

substrate: thymidine


substrate_name: tubercidin

substrate: tubercidin


substrate_name: uridine

substrate: uridine


substrate_name: cytidine

substrate: cytidine


enzyme_display_name: Choline oxidase

organism: Arthrobacter globiformis

substrate_name: choline

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

proof_lines: kcat is 13.4 sec(-1) with choline as substrate and 11.6 sec(-1) with betaine aldehyde as substrate.

enzyme: Choline oxidase

substrate: choline


substrate_name: betaine aldehyde

substrate: betaine aldehyde


enzyme_display_name: D-mannitol oxidase

organism: Cornu aspersum

smiles: O=O

enzyme: D-mannitol oxidase


substrate_name: D-mannitol

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

substrate: D-mannitol


organism: Limacus flavus


substrate_name: D-arabinitol

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

substrate: D-arabinitol


organism: Arion ater


enzyme_display_name: vanillyl-alcohol oxidase

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D170S to reconstruct the assayed variant sequence.

enzyme: vanillyl-alcohol oxidase


substrate_name: p-Cresol

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D170E to reconstruct the assayed variant sequence.

substrate: p-Cresol


substrate_name: propylphenol

substrate: propylphenol


substrate_name: Vanillyl alcohol

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P56216 and applied mutation signature Y108F to reconstruct the assayed variant sequence.

column_label: Table 1, Vanillyl alcohol substrate group, VAO variant row 'Y108F': column kcat (s^-1) = 0.042; column Km (uM) = 1750; column kcat/Km (s^-1 mM^-1) = 0.024.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.042 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 0.042 s^(-1). Km: printed Table 1 cell 1750 uM; 1 uM is 0.001 mM, so 1750 / 1000 = 1.75 mM, which is the exported value. kcat/Km: printed Table 1 cell 0.024 s^-1 mM^-1; the column head already prints s^-1 mM^-1, so no unit conversion applies. Quotient disclosure for this cell group: 0.042 / 1.75 = 0.024 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 1 uses.

raw_value_unit_evidence: Table 1, Vanillyl alcohol substrate group, VAO variant row 'Y108F': kcat = 0.042 s^-1; Km = 1750 uM; printed kcat/Km = 0.024 s^-1 mM^-1.

table_label: Table 1: Apparent steady-state kinetic parameters for the oxidation of vanillyl alcohol and chavicol by VAO variants (J. Biol. Chem. 2017, volume 292, number 35, pages 14668-14679); printed columns VAO variant, kcat (s^-1), Km (uM), kcat/Km (s^-1 mM^-1) and Ki (mM)

substrate: Vanillyl alcohol


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P56216 and applied mutation signature Y503F to reconstruct the assayed variant sequence.

column_label: Table 1, Vanillyl alcohol substrate group, VAO variant row 'Y503F': column kcat (s^-1) = 0.055; column Km (uM) = 990; column kcat/Km (s^-1 mM^-1) = 0.056.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.055 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 0.055 s^(-1). Km: printed Table 1 cell 990 uM; 1 uM is 0.001 mM, so 990 / 1000 = 0.99 mM, which is the exported value. kcat/Km: printed Table 1 cell 0.056 s^-1 mM^-1; the column head already prints s^-1 mM^-1, so no unit conversion applies. Quotient disclosure for this cell group: 0.055 / 0.99 = 0.05555555555555556 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 1 uses.

raw_value_unit_evidence: Table 1, Vanillyl alcohol substrate group, VAO variant row 'Y503F': kcat = 0.055 s^-1; Km = 990 uM; printed kcat/Km = 0.056 s^-1 mM^-1.


substrate_name: chavicol

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P56216 and applied mutation signature Y108F/Y503F to reconstruct the assayed variant sequence.

column_label: Table 1, Chavicol substrate group, VAO variant row 'Y108F/Y503F': column kcat (s^-1) = 0.13; column Km (uM) = 74; column kcat/Km (s^-1 mM^-1) = 1.8.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.13 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 0.13 s^(-1). Km: printed Table 1 cell 74 uM; 1 uM is 0.001 mM, so 74 / 1000 = 0.074 mM, which is the exported value. kcat/Km: printed Table 1 cell 1.8 s^-1 mM^-1; the column head already prints s^-1 mM^-1, so no unit conversion applies. Quotient disclosure for this cell group: 0.13 / 0.074 = 1.7567567567567568 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 1 uses.

raw_value_unit_evidence: Table 1, Chavicol substrate group, VAO variant row 'Y108F/Y503F': kcat = 0.13 s^-1; Km = 74 uM; printed kcat/Km = 1.8 s^-1 mM^-1.

substrate: chavicol


column_label: Table 1, Chavicol substrate group, VAO variant row 'Y503F': column kcat (s^-1) = 3.3; column Km (uM) = 21; column kcat/Km (s^-1 mM^-1) = 157.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.3 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 3.3 s^(-1). Km: printed Table 1 cell 21 uM; 1 uM is 0.001 mM, so 21 / 1000 = 0.021 mM, which is the exported value. kcat/Km: printed Table 1 cell 157 s^-1 mM^-1; the column head already prints s^-1 mM^-1, so no unit conversion applies. Quotient disclosure for this cell group: 3.3 / 0.021 = 157.14285714285714 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 1 uses.

raw_value_unit_evidence: Table 1, Chavicol substrate group, VAO variant row 'Y503F': kcat = 3.3 s^-1; Km = 21 uM; printed kcat/Km = 157 s^-1 mM^-1.


column_label: Table 1, Chavicol substrate group, VAO variant row 'Y108F': column kcat (s^-1) = 3.4; column Km (uM) = 67; column kcat/Km (s^-1 mM^-1) = 51.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.4 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 3.4 s^(-1). Km: printed Table 1 cell 67 uM; 1 uM is 0.001 mM, so 67 / 1000 = 0.067 mM, which is the exported value. kcat/Km: printed Table 1 cell 51 s^-1 mM^-1; the column head already prints s^-1 mM^-1, so no unit conversion applies. Quotient disclosure for this cell group: 3.4 / 0.067 = 50.74626865671642 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 1 uses.

raw_value_unit_evidence: Table 1, Chavicol substrate group, VAO variant row 'Y108F': kcat = 3.4 s^-1; Km = 67 uM; printed kcat/Km = 51 s^-1 mM^-1.


column_label: Table 1, Chavicol substrate group, VAO variant row 'Wild Type': column kcat (s^-1) = 7.4; column Km (uM) = 6.5; column kcat/Km (s^-1 mM^-1) = 1138.

normalized_value_unit_evidence: kcat: printed Table 1 cell 7.4 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 7.4 s^(-1). Km: printed Table 1 cell 6.5 uM; 1 uM is 0.001 mM, so 6.5 / 1000 = 0.0065 mM, which is the exported value. kcat/Km: printed Table 1 cell 1138 s^-1 mM^-1; the column head already prints s^-1 mM^-1, so no unit conversion applies. Quotient disclosure for this cell group: 7.4 / 0.0065 = 1138.4615384615386 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 1 uses.

raw_value_unit_evidence: Table 1, Chavicol substrate group, VAO variant row 'Wild Type': kcat = 7.4 s^-1; Km = 6.5 uM; printed kcat/Km = 1138 s^-1 mM^-1.


organism: Methylovorus sp. MP688

column_label: TABLE 3. Steady-state kinetic constants for the oxidation of vanillyl alcohol, HMF, DFF, and FDCA by HMFOs; row Vanillyl alcohol / MetspHMFO; columns kcat, Km, kcat/Km; kcat raw_value=1170 +/- 80 raw_unit=min^-1; Km raw_value=0.5 +/- 0.1 raw_unit=mM; kcat/Km raw_value=2170 +/- 330 raw_unit=mM^-1*min^-1

normalized_value_unit_evidence: kcat normalized_value=19.5 normalized_unit=s^-1; Km normalized_value=0.5 normalized_unit=mM; kcat/Km normalized_value=39.0 normalized_unit=s^-1*mM^-1

row_label: Vanillyl alcohol / MetspHMFO


assay_conditions_summary: pH 10

proof_lines:
pH 10, 25°C, wild-type enzyme
pH 7.5, 25°C, wild-type enzyme


substrate_name: creosol

proof_lines:
pH 8, 25°C, wild-type enzyme
pH 10, 25°C, wild-type enzyme
pH 7.5, 25°C, wild-type enzyme

substrate: creosol


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T505S to reconstruct the assayed variant sequence.

proof_lines:
pH 8, 25°C, mutant enzyme T505S
pH 10, 25°C, mutant enzyme T505S
pH 7.5, 25°C, mutant enzyme T505S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F454Y with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

proof_lines:
pH 10, 25°C, mutant enzyme F454Y
pH 8, 25°C, mutant enzyme F454Y
pH 7.5, 25°C, mutant enzyme F454Y


sequence_variant_note: Mutation signature I237T/M437L could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
pH 8, 25°C, mutant enzyme I237T/M437L
pH 10, 25°C, mutant enzyme I237T/M437L


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A429V to reconstruct the assayed variant sequence.

proof_lines:
pH 10, 25°C, mutant enzyme A429V
pH 8, 25°C, mutant enzyme A429V


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E502G with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

proof_lines:
pH 8, 25°C, mutant enzyme E502G
pH 10, 25°C, mutant enzyme E502G
pH 7.5, 25°C, mutant enzyme E502G


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F93Y/P189S/I238T to reconstruct the assayed variant sequence.

proof_lines: pH 10, 25°C, mutant enzyme F93Y/P189S/I238T


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I238T with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

proof_lines:
pH 10, 25°C, mutant enzyme I238T
pH 8, 25°C, mutant enzyme I238T
pH 7.5, 25°C, mutant enzyme I238T


proof_lines:
pH 10, 25°C, mutant enzyme T505S
pH 7.5, 25°C, mutant enzyme T505S


proof_lines:
pH 10, 25°C, mutant enzyme F454Y
pH 7.5, 25°C, mutant enzyme F454Y


proof_lines:
pH 10, 25°C, mutant enzyme E502G
pH 7.5, 25°C, mutant enzyme E502G


proof_lines:
pH 7.5, 25°C, mutant enzyme I238T
pH 10, 25°C, mutant enzyme I238T


substrate_name: eugenol

substrate: eugenol


proof_lines:
pH 7.5, 25°C, mutant enzyme T505S
pH 10, 25°C, mutant enzyme T505S


proof_lines:
pH 7.5, 25°C, mutant enzyme E502G
pH 10, 25°C, mutant enzyme E502G


proof_lines:
pH 7.5, 25°C, mutant enzyme F454Y
pH 10, 25°C, mutant enzyme F454Y


proof_lines:
pH 10, 25°C, mutant enzyme I238T
pH 7.5, 25°C, mutant enzyme I238T


proof_lines:
pH 7.5, 25°C, wild-type enzyme
pH 10, 25°C, wild-type enzyme
wild type enzyme, at pH 7.5 and 25°C


organism: Acidothermus cellulolyticus


column_label: Table 1. Steady-state kinetic parameters for recombinant HotAldO and AldO; row D-mannitol; HotAldO columns Km (mM), kcat (s^-1), kcat/Km (s^-1 M^-1); cells 5.5, 2.5, 450

normalized_value_unit_evidence: Km=5.5 mM; kcat=2.5 s^-1; kcat/Km=0.45 s^-1 mM^-1 (explicit table value / 1000)

raw_value_unit_evidence: HotAldO / D-mannitol: Km=5.5 mM; kcat=2.5 s^-1; kcat/Km=450 s^-1 M^-1

row_label: D-mannitol


substrate_name: D-sorbitol

column_label: Table 1. Steady-state kinetic parameters for recombinant HotAldO and AldO; row D-sorbitol; HotAldO columns Km (mM), kcat (s^-1), kcat/Km (s^-1 M^-1); cells 0.44, 1.2, 2700

normalized_value_unit_evidence: Km=0.44 mM; kcat=1.2 s^-1; kcat/Km=2.7 s^-1 mM^-1 (explicit table value / 1000)

raw_value_unit_evidence: HotAldO / D-sorbitol: Km=0.44 mM; kcat=1.2 s^-1; kcat/Km=2700 s^-1 M^-1

row_label: D-sorbitol

substrate: D-sorbitol


substrate_name: glycerol

smiles: C(C(CO)O)O

column_label: Table 1. Steady-state kinetic parameters for recombinant HotAldO and AldO; row Glycerol; HotAldO columns Km (mM), kcat (s^-1), kcat/Km (s^-1 M^-1); cells 270, 1.3, 4.8

normalized_value_unit_evidence: Km=270 mM; kcat=1.3 s^-1; kcat/Km=0.0048 s^-1 mM^-1 (explicit table value / 1000)

raw_value_unit_evidence: HotAldO / Glycerol: Km=270 mM; kcat=1.3 s^-1; kcat/Km=4.8 s^-1 M^-1

row_label: Glycerol

substrate: glycerol


substrate_name: xylitol

column_label: Table 1. Steady-state kinetic parameters for recombinant HotAldO and AldO; row Xylitol; HotAldO columns Km (mM), kcat (s^-1), kcat/Km (s^-1 M^-1); cells 0.07, 1.9, 27000

normalized_value_unit_evidence: Km=0.07 mM; kcat=1.9 s^-1; kcat/Km=27 s^-1 mM^-1 (explicit table value / 1000)

raw_value_unit_evidence: HotAldO / Xylitol: Km=0.07 mM; kcat=1.9 s^-1; kcat/Km=27000 s^-1 M^-1

row_label: Xylitol

substrate: xylitol


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D170N to reconstruct the assayed variant sequence.


proof_lines: in 50 mM sodium phosphate buffer, at pH 7.5 and 30°C


source_databases_merged: brenda skid uniprot


organism: Pseudomonas sp. 11/12A

protein_accession_database: NCBI Protein

sequence_source: NCBI RefSeq WP_047529632.1 cited in PMID 32503910

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H422A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H422T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H422C to reconstruct the assayed variant sequence.


enzyme_display_name: Glycerol 3-phosphate oxidase

organism: Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1)

substrate_name: sn-glycerol 3-phosphate (at pH 7 and 4 degrees Celsius)

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

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

proof_lines: kcat is 4.2 sec(-1) with sn-glycerol 3-phosphate as substrate (at pH 7 and 4 degrees Celsius). kcat is 60.1 sec(-1) with sn-glycerol 3-phosphate as substrate (at pH 7 and 25 degrees Celsius). kcat is 0.6 sec(-1) with sn-glycerol 3-phosphate

enzyme: Glycerol 3-phosphate oxidase


substrate_name: O2 (at pH 7 and 4 degrees Celsius)

substrate: O2 (at pH 7 and 4 degrees Celsius)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D170A/T457E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D170S/T457E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T457E to reconstruct the assayed variant sequence.


proof_lines:
pH 7.5, 25°C, wild-type enzyme
pH 7.5, 25?Cm wild-type enzyme
pH 10, 25°C, wild-type enzyme


organism: Rattus norvegicus

substrate_name: DL-2-hydroxybutanoate (with DCIP as electron acceptor)

proof_lines: kcat is 0.99 sec(-1) for the oxidation of L-2-hydroxyoctanoate with DCIP instead of O2 as electron acceptor. kcat is 0.34 sec(-1) for the oxidation of L-2-hydroxyhexadecanoate with DCIP instead of O2 as electron acceptor (PubMed:15683236).


proof_lines:
wild type enzyme, at pH 7.5 and 25°C
pH 7.5, 25°C, wild-type enzyme
pH 10, 25°C, wild-type enzyme


proof_lines: His-tagged recombinant enzyme, pH 7.5, 25°C


organism: Spinacia oleracea

substrate_name: glycolate (at 25 degrees Celsius)

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

proof_lines: kcat is 20 sec(-1) with glycolate as substrate. kcat is 11 sec(-1) with L-lactate as substrate. kcat is 13.2 sec(-1) with L-2-hydroxbyutanoate as substrate. kcat is 0.09 sec(-1) with L-mandelate as substrate.

substrate: glycolate (at 25 degrees Celsius)


enzyme_display_name: UniProt Q9UJM8

substrate_name: glycolate

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=9
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt Q9UJM8

substrate: glycolate


substrate_name: glycolate (at pH 7.0 and 37 degrees Celsius, with DCIP as electron acceptor)


enzyme_display_name: Glycolate oxidase 1

organism: Zea mays

substrate_name: glycolate (at pH 8 and 30 degrees Celsius)

proof_lines: kcat is 34.13 sec(-1) (at pH 8 and 30 degrees Celsius).

enzyme: Glycolate oxidase 1


enzyme_display_name: choline oxidase

organism: Alcaligenes sp.

substrate_name: choline

sequence: DNPNHSR

wild_type_sequence: DNPNHSR

proof_lines: enzyme immobilized in polyethylenimine-coated silica-monolith, apparent value, pH and temperature not specified in the publication

proof_lines: free enzyme, apparent value, pH and temperature not specified in the publication

enzyme: choline oxidase


organism: Penicillium simplicissimum

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H61T to reconstruct the assayed variant sequence.


organism: Streptomyces coelicolor

substrate_name: L-Threitol

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

assay_conditions_summary: pH 7.5; buffer 50 mM sodium phosphate

proof_lines: kcat is 13 sec(-1) with xylitol as substrate. kcat is 17 sec(-1) with D-sorbitol as substrate. kcat is 9.2 sec(-1) with D-mannitol as substrate. kcat is 6.3 sec(-1) with L-threitol as substrate.

substrate: L-Threitol


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

proof_lines: recombinant oxidase-peroxidase fusion mutant enzyme, pH 7.5, temperature not specified in the publication


enzyme_display_name: N-acetyl-D-hexosamine oxidase

organism: Ralstonia solanacearum (strain UW551)

substrate_name: diacetylchitobiose

proof_lines: kcat is 5.67 sec(-1) with N-acetyl-D-glucosamine as substrate. kcat is 4.46 sec(-1) with N-acetyl-D-glucosamine as substrate. kcat is 2.23 sec(-1) with N-acetyl-D-mannosamine as substrate. kcat is 0.84 sec(-1) with diacetylchitobiose as sub

enzyme: N-acetyl-D-hexosamine oxidase

substrate: diacetylchitobiose


organism: Arabidopsis thaliana

assay_conditions_summary: pH 8; buffer context

proof_lines: kcat is 29.86 sec(-1) (at pH 8 and 30 degrees Celsius).

substrate: glycolate (at pH 8 and 30 degrees Celsius)


proof_lines:
Raw SKiD Env: Temp=25°C, pH=10
Raw SKiD Env: Temp=25°C, pH=7.5


assay_conditions_summary: pH 7.5; buffer pH 7

column_label: Table 1 column Km (unit microM) for row 4-n-Heptylphenol gives 42

normalized_value_unit_evidence: Table 1 Km normalized_value=0.042 normalized_unit=mM

raw_value_unit_evidence: Table 1 Km raw_value=42 raw_unit=microM

table_label: Table 1: Steady-state kinetic parameters for vanillyl-alcohol oxidase from P. simplicissimum


organism: Rhodococcus jostii

proof_lines:
pH 7.5, 25°C
Raw SKiD Env: Temp=25°C, pH=7.5


substrate_name: vanillylamine

column_label: Table 1, row Vanillylamine, EUGO columns: Km = 76 uM; kcat = 0.26 s^-1; kcat/Km = 3.4 x 10^3 s^-1 M^-1.

raw_value_unit_evidence: Table 1 Vanillylamine / EUGO: Km 76 uM; kcat 0.26 s^-1; kcat/Km 3.4 x 10^3 s^-1 M^-1.

row_label: Vanillylamine / EUGO

substrate: vanillylamine


substrate_name: Vanillyl alcohol

column_label: Table 1, row Vanillyl alcohol, EUGO columns: Km = 40 uM; kcat = 12 s^-1; kcat/Km = 300 x 10^3 s^-1 M^-1.

raw_value_unit_evidence: Table 1 Vanillyl alcohol / EUGO: Km 40 uM; kcat 12 s^-1; kcat/Km 300 x 10^3 s^-1 M^-1.

row_label: Vanillyl alcohol / EUGO


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F454Y with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I238T with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T505S to reconstruct the assayed variant sequence.


column_label: table label: Table III Steady-state kinetic parameters for VAO and its mutants in 50 mm potassium phosphate (pH 7.5) at 25 °C; row label: 2-Methyl-p-cresol; column label: the Wild-type kcat cell and the Wild-type Km cell of this one table row; no cell is taken from any other enzyme column group of the table and no cell is taken from any other row or from any other table; raw value: kcat 0.031 s-1, Km 21 uM; raw unit: s-1 for kcat, uM for Km; normalized value: kcat 0.031 s^-1, Km 0.021 mM, kcat/Km 1.476190476190476 s^-1 mM^-1; normalized unit: s^-1, mM, s^-1 mM^-1; condition label: Steady-state kinetic parameters for VAO and its mutants in 50 mm potassium phosphate (pH 7.5) at 25 °C. Exported assay conditions: pH 7.5, 298.15 K.

normalized_value_unit_evidence: Km 21 uM divided by 1000 gives 0.021 mM at the export's stored precision; exported Km 0.021 mM. kcat 0.031 s-1 is already the export's unit, so the normalized value is 0.031 s^-1 with no conversion; exported kcat 0.031 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.031 s^-1 divided by 0.021 mM giving 1.476190476190476 s^-1 mM^-1, and of nothing else; exported kcat/Km 1.476190476190476 s^-1 mM^-1. This table prints no kcat/Km column, so no printed ratio cell is available or claimed.

raw_value_unit_evidence: Table III, row 2-Methyl-p-cresol, Wild-type column group: kcat 0.031 s-1; Km 21 uM.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E502G with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


substrate_name: Eugenol

substrate: Eugenol


substrate_name: creosol


column_label: table label: Table IV Steady-state kinetic parameters for VAO and its mutants in 50 mm glycine/potassium hydroxide (pH 10) at 25 °C; row label: Creosol; column label: the Wild-type kcat cell and the Wild-type Km cell of this one table row; no cell is taken from any other enzyme column group of the table and no cell is taken from any other row or from any other table; raw value: kcat 0.005 s-1, Km 2 uM; raw unit: s-1 for kcat, uM for Km; normalized value: kcat 0.005 s^-1, Km 0.002 mM, kcat/Km 2.5 s^-1 mM^-1; normalized unit: s^-1, mM, s^-1 mM^-1; condition label: Steady-state kinetic parameters for VAO and its mutants in 50 mm glycine/potassium hydroxide (pH 10) at 25 °C. Exported assay conditions: pH 10, 298.15 K.

normalized_value_unit_evidence: Km 2 uM divided by 1000 gives 0.002 mM at the export's stored precision; exported Km 0.002 mM. kcat 0.005 s-1 is already the export's unit, so the normalized value is 0.005 s^-1 with no conversion; exported kcat 0.005 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.005 s^-1 divided by 0.002 mM giving 2.5 s^-1 mM^-1, and of nothing else; exported kcat/Km 2.5 s^-1 mM^-1. This table prints no kcat/Km column, so no printed ratio cell is available or claimed.

raw_value_unit_evidence: Table IV, row Creosol, Wild-type column group: kcat 0.005 s-1; Km 2 uM.

row_label: Creosol


substrate_name: norepinephrine

column_label: Publication page 273, Table 1, row Norepinephrine; columns Km, kcat, and kcat/Km; caption states the assay used 10 mM ascorbate and supplies the shared temperature, buffer, pH, and racemic-mixture condition.

normalized_value_unit_evidence: Km 2.9 mM; kcat 0.3 s^-1; exact quotient kcat/Km 0.10344827586206896 s^-1 mM^-1, consistent with the table's rounded 0.1 cell.

raw_value_unit_evidence: Table 1 row Norepinephrine reports Km 2900 uM, kcat 0.3 s^-1, and rounded kcat/Km 0.1 x 10^3 s^-1 M^-1.

row_label: Norepinephrine

table_label: Table 1. Steady-state kinetic parameters for vanillyl-alcohol oxidase from P. simplicissimum

substrate: norepinephrine


substrate_name: normetanephrine

column_label: Publication page 273, Table 1, row Normetanephrine; columns Km, kcat, and kcat/Km; table caption supplies temperature, buffer, pH, and racemic-mixture condition.

raw_value_unit_evidence: Table 1 row Normetanephrine reports Km 1400 uM, kcat 0.7 s^-1, and kcat/Km 0.5 x 10^3 s^-1 M^-1.

row_label: Normetanephrine

substrate: normetanephrine


substrate_name: metanephrine

column_label: Publication page 273, Table 1, row Metanephrine; columns Km, kcat, and kcat/Km; table caption supplies temperature, buffer, pH, and racemic-mixture condition.

raw_value_unit_evidence: Table 1 row Metanephrine reports Km 1600 uM, kcat 0.8 s^-1, and kcat/Km 0.5 x 10^3 s^-1 M^-1.

row_label: Metanephrine

substrate: metanephrine


column_label: Publication page 273, Table 1, row 4-Hydroxy-3-methoxyphenylglycol, kcat column; table caption supplies temperature, buffer, pH, and racemic-mixture condition.

raw_value_unit_evidence: Table 1 row 4-Hydroxy-3-methoxyphenylglycol reports kcat 3.6 s^-1.


substrate_name: chavicol

substrate: chavicol


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P56216 and applied mutation signature F454Y to reconstruct the assayed variant sequence.

column_label: Table III has substrate row Eugenol, enzyme/variant column F454Y, kcat=0.5 s^-1 and Km=3 uM; condition 50 mM potassium phosphate (pH 7.5), 25 C.

normalized_value_unit_evidence: kcat 0.5 s^(-1); kcat_over_km 166.667 1/mM*1/s; km 0.003 mM matched primary table cells

raw_value_unit_evidence: Table III row Eugenol, enzyme F454Y: kcat 0.5 s^-1; Km 3 uM.

row_label: Eugenol / F454Y

table_label: Table III: Steady-state kinetic parameters for VAO and its mutants


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P56216 and applied mutation signature F454Y with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table IV has substrate row Eugenol, enzyme/variant column F454Y, kcat=0.23 s^-1 and Km=0.8 uM; condition 50 mM glycine/potassium hydroxide (pH 10), 25 C.

normalized_value_unit_evidence: kcat 0.23 s^(-1); kcat_over_km 287.5 1/mM*1/s; km 0.0008 mM matched primary table cells

raw_value_unit_evidence: Table IV row Eugenol, enzyme F454Y: kcat 0.23 s^-1; Km 0.8 uM.

table_label: Table IV: Steady-state kinetic parameters for VAO and its mutants


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P56216 and applied mutation signature I238T with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

column_label: Table III has substrate row Eugenol, enzyme/variant column I238T, kcat=0.8 s^-1 and Km=8 uM; condition 50 mM potassium phosphate (pH 7.5), 25 C.

normalized_value_unit_evidence: kcat 0.8 s^(-1); kcat_over_km 100.0 1/mM*1/s; km 0.008 mM matched primary table cells

raw_value_unit_evidence: Table III row Eugenol, enzyme I238T: kcat 0.8 s^-1; Km 8 uM.

row_label: Eugenol / I238T


column_label: Table IV has substrate row Eugenol, enzyme/variant column I238T, kcat=0.6 s^-1 and Km=0.2 uM; condition 50 mM glycine/potassium hydroxide (pH 10), 25 C.

normalized_value_unit_evidence: kcat 0.6 s^(-1); kcat_over_km 3000.0 1/mM*1/s; km 0.0002 mM matched primary table cells

raw_value_unit_evidence: Table IV row Eugenol, enzyme I238T: kcat 0.6 s^-1; Km 0.2 uM.


column_label: Table III has substrate row Eugenol, enzyme/variant column T505S, kcat=0.65 s^-1 and Km=0.8 uM; condition 50 mM potassium phosphate (pH 7.5), 25 C.

normalized_value_unit_evidence: kcat 0.65 s^(-1); kcat_over_km 812.5 s^(-1)*mM^(-1); km 0.0008 mM matched primary table cells

raw_value_unit_evidence: Table III row Eugenol, enzyme T505S: kcat 0.65 s^-1; Km 0.8 uM.

row_label: Eugenol / T505S


column_label: Table III has substrate row Eugenol, enzyme/variant column Wild-type, kcat=14 s^-1 and Km=2 uM; condition 50 mM potassium phosphate (pH 7.5), 25 C.

normalized_value_unit_evidence: kcat 14.0 s^(-1); kcat_over_km 7000.0 1/mM*1/s; km 0.002 mM matched primary table cells

raw_value_unit_evidence: Table III row Eugenol, enzyme Wild-type: kcat 14 s^-1; Km 2 uM.

row_label: Eugenol / Wild-type


column_label: Table IV has substrate row Eugenol, enzyme/variant column Wild-type, kcat=39 s^-1 and Km=19 uM; condition 50 mM glycine/potassium hydroxide (pH 10), 25 C.

normalized_value_unit_evidence: kcat 39.0 s^(-1); kcat_over_km 2052.632 1/mM*1/s; km 0.019 mM matched primary table cells

raw_value_unit_evidence: Table IV row Eugenol, enzyme Wild-type: kcat 39 s^-1; Km 19 uM.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P56216 and applied mutation signature E502G with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

column_label: Table III has substrate row 2-Amino-p-cresol, enzyme/variant column E502G, kcat=0.099 s^-1 and Km=200 uM; condition 50 mM potassium phosphate (pH 7.5), 25 C.

normalized_value_unit_evidence: kcat 0.099 s^(-1); kcat_over_km 0.495 1/mM*1/s; km 0.2 mM matched primary table cells

raw_value_unit_evidence: Table III row 2-Amino-p-cresol, enzyme E502G: kcat 0.099 s^-1; Km 200 uM.

row_label: 2-Amino-p-cresol / E502G


column_label: Table III has substrate row 2-Amino-p-cresol, enzyme/variant column F454Y, kcat=0.082 s^-1 and Km=167 uM; condition 50 mM potassium phosphate (pH 7.5), 25 C.

normalized_value_unit_evidence: kcat 0.082 s^(-1); kcat_over_km 0.491 1/mM*1/s; km 0.167 mM matched primary table cells

raw_value_unit_evidence: Table III row 2-Amino-p-cresol, enzyme F454Y: kcat 0.082 s^-1; Km 167 uM.

row_label: 2-Amino-p-cresol / F454Y


column_label: Table IV has substrate row 2-Amino-p-cresol, enzyme/variant column F454Y, kcat=0.047 s^-1 and Km=64 uM; condition 50 mM glycine/potassium hydroxide (pH 10), 25 C.

normalized_value_unit_evidence: kcat 0.047 s^(-1); kcat_over_km 0.734 1/mM*1/s; km 0.064 mM matched primary table cells

raw_value_unit_evidence: Table IV row 2-Amino-p-cresol, enzyme F454Y: kcat 0.047 s^-1; Km 64 uM.


column_label: Table IV has substrate row 2-Amino-p-cresol, enzyme/variant column I238T, kcat=0.086 s^-1 and Km=50 uM; condition 50 mM glycine/potassium hydroxide (pH 10), 25 C.

raw_value_unit_evidence: Table IV row 2-Amino-p-cresol, enzyme I238T: kcat 0.086 s^-1; Km 50 uM.

row_label: 2-Amino-p-cresol / I238T


column_label: Table III has substrate row 2-Amino-p-cresol, enzyme/variant column T505S, kcat=0.087 s^-1 and Km=254 uM; condition 50 mM potassium phosphate (pH 7.5), 25 C.

normalized_value_unit_evidence: kcat 0.087 s^(-1); kcat_over_km 0.343 1/mM*1/s; km 0.254 mM matched primary table cells

raw_value_unit_evidence: Table III row 2-Amino-p-cresol, enzyme T505S: kcat 0.087 s^-1; Km 254 uM.

row_label: 2-Amino-p-cresol / T505S


column_label: Table III has substrate row 2-Amino-p-cresol, enzyme/variant column Wild-type, kcat=0.017 s^-1 and Km=123 uM; condition 50 mM potassium phosphate (pH 7.5), 25 C.

raw_value_unit_evidence: Table III row 2-Amino-p-cresol, enzyme Wild-type: kcat 0.017 s^-1; Km 123 uM.

row_label: 2-Amino-p-cresol / Wild-type


smiles: CCCO


column_label: Table 1; 4-n-Pentylphenol; Km, kcat, kcat/Km columns

normalized_value_unit_evidence: not accepted: normalized kcat/Km explicit cell is 38 s^-1 mM^-1, export expects 37.5.

raw_value_unit_evidence: Table 1 reports Km 8 uM, kcat 0.3 s^-1, kcat/Km 38 x 10^3 s^-1 M^-1.


column_label: Table 1; 4-sec-Butylphenol; Km, kcat, kcat/Km columns

normalized_value_unit_evidence: not accepted: normalized kcat/Km explicit cell is 7 s^-1 mM^-1, export expects 6.944444444444445.

raw_value_unit_evidence: Table 1 reports Km 72 uM, kcat 0.5 s^-1, kcat/Km 7 x 10^3 s^-1 M^-1.


column_label: Table 1; 5-Indanol; Km, kcat, kcat/Km columns

normalized_value_unit_evidence: not accepted: normalized kcat/Km explicit cell is 7 s^-1 mM^-1, export expects 6.4935064935064934.

raw_value_unit_evidence: Table 1 reports Km 77 uM, kcat 0.5 s^-1, kcat/Km 7 x 10^3 s^-1 M^-1.


column_label: Table 1; 5,6,7,8-Tetrahydro-2-naphthol; Km, kcat, kcat/Km columns

normalized_value_unit_evidence: not accepted: normalized kcat/Km explicit cell is 7 s^-1 mM^-1, export expects 7.446808510638298.

raw_value_unit_evidence: Table 1 reports Km 94 uM, kcat 0.7 s^-1, kcat/Km 7 x 10^3 s^-1 M^-1.


column_label: Table 1; 4-n-Butylphenol; Km, kcat, kcat/Km columns

normalized_value_unit_evidence: normalized: Km=0.002 mM, kcat=1.2 s^-1, kcat/Km=600 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 reports Km 2 uM, kcat 1.2 s^-1, kcat/Km 600 x 10^3 s^-1 M^-1.


column_label: Table 1; 4-Isopropylphenol; Km, kcat, kcat/Km columns

normalized_value_unit_evidence: not accepted: normalized kcat/Km explicit cell is 81 s^-1 mM^-1, export expects 81.25.

raw_value_unit_evidence: Table 1 reports Km 16 uM, kcat 1.3 s^-1, kcat/Km 81 x 10^3 s^-1 M^-1.


column_label: Table 1; (S)-1-(4'-Hydroxyphenyl)ethanol; Km, kcat, kcat/Km columns

normalized_value_unit_evidence: not accepted: normalized kcat/Km explicit cell is 170 s^-1 mM^-1, export expects 169.23076923076925.

raw_value_unit_evidence: Table 1 reports Km 26 uM, kcat 4.4 s^-1, kcat/Km 170 x 10^3 s^-1 M^-1.


organism: Arthrobacter chlorophenolicus

sequence_variant_note: Resolved canonical sequence from UniProtKB:B8H740 and applied mutation signature M359R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; buffer air-saturated 100 mM potassium phosphate

table_label: Table 1: Kinetic parameters of choline oxidase variants with choline

substrate: choline


sequence_variant_note: Resolved canonical sequence from UniProtKB:B8H740 and applied mutation signature S101A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:B8H740 and applied mutation signature S101A/D250G/F253R/V355T/F357R/M359R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:B8H740 and applied mutation signature S101A/V355T/F357R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:B8H740 and applied mutation signature S101A/V355T/F357R/M359R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:B8H740 and applied mutation signature V355T/F357R to reconstruct the assayed variant sequence.


enzyme_display_name: (S)-2-hydroxy-acid oxidase

organism: Homo sapiens

substrate_name: Acceptor

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

smiles: [At]

proof_lines:
DCIP
oxygen electrode

enzyme: (S)-2-hydroxy-acid oxidase

substrate: Acceptor


substrate_name: Glyoxylate

smiles: O=CC(=O)O

substrate: Glyoxylate


substrate_name: L-Lactate

column_label: Table 2, row L-Lactate, columns kcatapp, Kmapp, and kcatapp/Kmapp.

row_label: L-Lactate

table_label: Table 2

substrate: L-Lactate


substrate_name: (S)-Mandelate

column_label: Table 2, row L-Mandelate, columns kcatapp, Kmapp, and kcatapp/Kmapp.

row_label: L-Mandelate

substrate: (S)-Mandelate


substrate_name: glycolate

smiles: O=C(O)CO


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

column_label: Table 1, row Chavicol / Wild Type, reports kcat 7.4 +/- 0.1 s^-1, Km 6.5 +/- 0.3 uM, displayed kcat/Km 1138 s^-1 mM^-1, and Ki 7.0 +/- 1.1 mM. Km normalizes to 0.0065 mM. The exact same-row efficiency used by this package is 7.4 s^-1 / 0.0065 mM = 1138.4615384615386 s^-1 mM^-1; the table displays that efficiency to the integer 1138.

raw_value_unit_evidence: Chavicol / Wild Type: kcat 7.4 +/- 0.1 s^-1; Km 6.5 +/- 0.3 uM; displayed kcat/Km 1138 s^-1 mM^-1; Ki 7.0 +/- 1.1 mM; same-row exact efficiency evidence 7.4 s^-1 / 0.0065 mM.

row_label: Chavicol / Wild Type

table_label: Table 1. Apparent steady-state kinetic parameters for the oxidation of vanillyl alcohol and chavicol by VAO variants


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P56216 and applied mutation signature Y108F to reconstruct the assayed variant sequence.

column_label: Table 1, Chavicol substrate group, VAO variant row 'Y108F': column kcat (s^-1) = 3.4; column Km (uM) = 67; column kcat/Km (s^-1 mM^-1) = 51.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.4 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 3.4 s^(-1). Km: printed Table 1 cell 67 uM; 1 uM is 0.001 mM, so 67 / 1000 = 0.067 mM, which is the exported value. kcat/Km: printed Table 1 cell 51 s^-1 mM^-1; the column head already prints s^-1 mM^-1, so no unit conversion applies. Quotient disclosure for this cell group: 3.4 / 0.067 = 50.74626865671642 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 1 uses.

raw_value_unit_evidence: Table 1, Chavicol substrate group, VAO variant row 'Y108F': kcat = 3.4 s^-1; Km = 67 uM; printed kcat/Km = 51 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P56216 and applied mutation signature Y108F/Y503F to reconstruct the assayed variant sequence.

column_label: Table 1 Chavicol row Y108F/Y503F reports kcat 0.13 +/- 0.01 s^-1, Km 74 +/- 6 uM, kcat/Km 1.8 s^-1 mM^-1, and Ki 1.4 +/- 0.2 mM.

normalized_value_unit_evidence: kcat normalized 0.13 s^-1; Km normalized 0.074 mM; kcat/Km normalized 1.8 s^-1 mM^-1 from the table cell and 1.7567567567567568 s^-1 mM^-1 from listed kcat/Km row-derived values.

row_label: Chavicol / Y108F/Y503F


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P56216 and applied mutation signature Y503F to reconstruct the assayed variant sequence.

column_label: Table 1, Chavicol substrate group, VAO variant row 'Y503F': column kcat (s^-1) = 3.3; column Km (uM) = 21; column kcat/Km (s^-1 mM^-1) = 157.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.3 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 3.3 s^(-1). Km: printed Table 1 cell 21 uM; 1 uM is 0.001 mM, so 21 / 1000 = 0.021 mM, which is the exported value. kcat/Km: printed Table 1 cell 157 s^-1 mM^-1; the column head already prints s^-1 mM^-1, so no unit conversion applies. Quotient disclosure for this cell group: 3.3 / 0.021 = 157.14285714285714 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 1 uses.

raw_value_unit_evidence: Table 1, Chavicol substrate group, VAO variant row 'Y503F': kcat = 3.3 s^-1; Km = 21 uM; printed kcat/Km = 157 s^-1 mM^-1.


column_label: Table 1 Vanillyl alcohol row Y108F reports kcat 0.042 +/- 0.006 s^-1, Km 1750 +/- 420 uM, and kcat/Km 0.024 s^-1 mM^-1.

normalized_value_unit_evidence: kcat normalized 0.042 s^-1; Km normalized 1.75 mM; kcat/Km normalized 0.024 s^-1 mM^-1.

row_label: Vanillyl alcohol / Y108F

substrate: Vanillyl alcohol


column_label: Table 1, Vanillyl alcohol substrate group, VAO variant row 'Y503F': column kcat (s^-1) = 0.055; column Km (uM) = 990; column kcat/Km (s^-1 mM^-1) = 0.056.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.055 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 0.055 s^(-1). Km: printed Table 1 cell 990 uM; 1 uM is 0.001 mM, so 990 / 1000 = 0.99 mM, which is the exported value. kcat/Km: printed Table 1 cell 0.056 s^-1 mM^-1; the column head already prints s^-1 mM^-1, so no unit conversion applies. Quotient disclosure for this cell group: 0.055 / 0.99 = 0.05555555555555556 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 1 uses.

raw_value_unit_evidence: Table 1, Vanillyl alcohol substrate group, VAO variant row 'Y503F': kcat = 0.055 s^-1; Km = 990 uM; printed kcat/Km = 0.056 s^-1 mM^-1.


enzyme_display_name: UniProt O94219

organism: Pleurotus eryngii

enzyme: UniProt O94219


enzyme_display_name: UniProt E3Q9X3

organism: Colletotrichum graminicola

enzyme: UniProt E3Q9X3


substrate_name: 4-methoxybenzyl alcohol

substrate: 4-methoxybenzyl alcohol


enzyme_display_name: 5-(hydroxymethyl)furfural oxidase

organism: Methylovorus sp. MP688

substrate_name: 4-Hydroxy-3-methoxybenzyl alcohol

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F434A to reconstruct the assayed variant sequence.

enzyme: 5-(hydroxymethyl)furfural oxidase

substrate: 4-Hydroxy-3-methoxybenzyl alcohol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H467A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M103A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N511A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V367K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V367R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V465A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W369A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W466A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W466F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V367R/W466F to reconstruct the assayed variant sequence.


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


sequence_variant_note: Mutation signature Y334W 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.


enzyme_display_name: alditol oxidase

substrate_name: D-mannitol

column_label: Table 1. Steady-state kinetic parameters for recombinant HotAldO and AldO; row D-mannitol; AldO columns Km (mM), kcat (s^-1), kcat/Km (s^-1 M^-1); cells 36, 9.2, 260

normalized_value_unit_evidence: Km=36 mM; kcat=9.2 s^-1; kcat/Km=0.26 s^-1 mM^-1 (explicit table value / 1000)

raw_value_unit_evidence: AldO / D-mannitol: Km=36 mM; kcat=9.2 s^-1; kcat/Km=260 s^-1 M^-1

row_label: D-mannitol

enzyme: alditol oxidase

substrate: D-mannitol


substrate_name: D-sorbitol

column_label: Table 1. Steady-state kinetic parameters for recombinant HotAldO and AldO; row D-sorbitol; AldO columns Km (mM), kcat (s^-1), kcat/Km (s^-1 M^-1); cells 1.4, 17, 12000

normalized_value_unit_evidence: Km=1.4 mM; kcat=17 s^-1; kcat/Km=12 s^-1 mM^-1 (explicit table value / 1000)

raw_value_unit_evidence: AldO / D-sorbitol: Km=1.4 mM; kcat=17 s^-1; kcat/Km=12000 s^-1 M^-1

row_label: D-sorbitol

substrate: D-sorbitol


substrate_name: glycerol

smiles: OCC(O)CO

column_label: Table 1. Steady-state kinetic parameters for recombinant HotAldO and AldO; row Glycerol; AldO columns Km (mM), kcat (s^-1), kcat/Km (s^-1 M^-1); cells 350, 1.6, 4.6

normalized_value_unit_evidence: Km=350 mM; kcat=1.6 s^-1; kcat/Km=0.0046 s^-1 mM^-1 (explicit table value / 1000)

raw_value_unit_evidence: AldO / Glycerol: Km=350 mM; kcat=1.6 s^-1; kcat/Km=4.6 s^-1 M^-1

row_label: Glycerol

substrate: glycerol


column_label: Table 1. Steady-state kinetic parameters for recombinant HotAldO and AldO; row (R)-1-phenyl-1,2-ethanediol; AldO columns Km (mM), kcat (s^-1), kcat/Km (s^-1 M^-1); cells 101, 0.74, 7.3

normalized_value_unit_evidence: Km=101 mM; kcat=0.74 s^-1; kcat/Km=0.0073 s^-1 mM^-1 (explicit table value / 1000)

raw_value_unit_evidence: AldO / (R)-1-phenyl-1,2-ethanediol: Km=101 mM; kcat=0.74 s^-1; kcat/Km=7.3 s^-1 M^-1


substrate_name: xylitol

column_label: Table 1. Steady-state kinetic parameters for recombinant HotAldO and AldO; row Xylitol; AldO columns Km (mM), kcat (s^-1), kcat/Km (s^-1 M^-1); cells 0.32, 13, 41000

normalized_value_unit_evidence: Km=0.32 mM; kcat=13 s^-1; kcat/Km=41 s^-1 mM^-1 (explicit table value / 1000)

raw_value_unit_evidence: AldO / Xylitol: Km=0.32 mM; kcat=13 s^-1; kcat/Km=41000 s^-1 M^-1

row_label: Xylitol

substrate: xylitol


column_label: Table 1. Steady-state kinetic parameters for recombinant HotAldO and AldO; row 1-Phenyl-1,2-ethanediol; AldO columns Km (mM), kcat (s^-1), kcat/Km (s^-1 M^-1); cells 83, 0.36, 4.3

normalized_value_unit_evidence: Km=83 mM; kcat=0.36 s^-1; kcat/Km=0.0043 s^-1 mM^-1 (explicit table value / 1000)

raw_value_unit_evidence: AldO / 1-Phenyl-1,2-ethanediol: Km=83 mM; kcat=0.36 s^-1; kcat/Km=4.3 s^-1 M^-1


organism: Arthrobacter globiformis

substrate_name: Betaine aldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S101C to reconstruct the assayed variant sequence.

proof_lines:
Ser101Cys
betaine aldehyde
pH 10.0

substrate: Betaine aldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S101T to reconstruct the assayed variant sequence.

proof_lines:
Ser101Thr
betaine aldehyde
pH 10.0


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S101V to reconstruct the assayed variant sequence.

proof_lines:
Ser101Val
betaine aldehyde
pH 10.0


organism: Oryza sativa subsp. japonica

substrate_name: glycolate (at pH 8.0 and 30 degrees Celsius)

assay_conditions_summary: pH 8; buffer pH 8

column_label: Official Oxford Academic HTML Table 2 reports Km (for glycolate): nitrate leaves 0.46 mM and ammonium leaves 0.50 mM; neither exact cell equals the exported 0.4 mM.

raw_value_unit_evidence: Km raw_value=0.46/0.50 raw_unit=mM

row_label: Km (for glycolate)

table_label: Table 2 - GLO kinetic parameters (mM)


substrate_name: glyoxylate (at pH 8.0 and 30 degrees Celsius)

column_label: Official Oxford Academic HTML Table 2 reports Km (for glyoxylate): nitrate leaves 4.53 mM and ammonium leaves 5.05 mM; neither exact cell equals the exported 4.0 mM.

raw_value_unit_evidence: Km raw_value=4.53/5.05 raw_unit=mM

row_label: Km (for glyoxylate)


substrate_name: choline

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F357A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M62A/F357A to reconstruct the assayed variant sequence.


enzyme_display_name: Long-chain-alcohol oxidase FAO1

organism: Lotus japonicus

smiles: CCCCCCCCCCCCO

enzyme: Long-chain-alcohol oxidase FAO1


smiles: CCCCCCCCCCCCCCCCO


enzyme_display_name: Long-chain-alcohol oxidase FAO3

enzyme: Long-chain-alcohol oxidase FAO3


substrate_name: vanillylamine

substrate: vanillylamine


substrate_name: creosol

proof_lines:
pH 7.4, 25°C
Raw SKiD Env: Temp=25°C, pH=10
Raw SKiD Env: Temp=25°C, pH=7.5

substrate: creosol


organism: Acidothermus cellulolyticus

column_label: Table 1. Steady-state kinetic parameters for recombinant HotAldO and AldO; row D-mannitol; HotAldO columns Km (mM), kcat (s^-1), kcat/Km (s^-1 M^-1); cells 5.5, 2.5, 450

normalized_value_unit_evidence: Km=5.5 mM; kcat=2.5 s^-1; kcat/Km=0.45 s^-1 mM^-1 (explicit table value / 1000)

raw_value_unit_evidence: HotAldO / D-mannitol: Km=5.5 mM; kcat=2.5 s^-1; kcat/Km=450 s^-1 M^-1


column_label: Table 1. Steady-state kinetic parameters for recombinant HotAldO and AldO; row D-sorbitol; HotAldO columns Km (mM), kcat (s^-1), kcat/Km (s^-1 M^-1); cells 0.44, 1.2, 2700

normalized_value_unit_evidence: Km=0.44 mM; kcat=1.2 s^-1; kcat/Km=2.7 s^-1 mM^-1 (explicit table value / 1000)

raw_value_unit_evidence: HotAldO / D-sorbitol: Km=0.44 mM; kcat=1.2 s^-1; kcat/Km=2700 s^-1 M^-1


column_label: Table 1. Steady-state kinetic parameters for recombinant HotAldO and AldO; row Glycerol; HotAldO columns Km (mM), kcat (s^-1), kcat/Km (s^-1 M^-1); cells 270, 1.3, 4.8

normalized_value_unit_evidence: Km=270 mM; kcat=1.3 s^-1; kcat/Km=0.0048 s^-1 mM^-1 (explicit table value / 1000)

raw_value_unit_evidence: HotAldO / Glycerol: Km=270 mM; kcat=1.3 s^-1; kcat/Km=4.8 s^-1 M^-1


column_label: Table 1. Steady-state kinetic parameters for recombinant HotAldO and AldO; row Xylitol; HotAldO columns Km (mM), kcat (s^-1), kcat/Km (s^-1 M^-1); cells 0.07, 1.9, 27000

normalized_value_unit_evidence: Km=0.07 mM; kcat=1.9 s^-1; kcat/Km=27 s^-1 mM^-1 (explicit table value / 1000)

raw_value_unit_evidence: HotAldO / Xylitol: Km=0.07 mM; kcat=1.9 s^-1; kcat/Km=27000 s^-1 M^-1


column_label: Table 1. Steady-state kinetic parameters for recombinant HotAldO and AldO; row 1-Phenyl-1,2-ethanediol; HotAldO columns Km (mM), kcat (s^-1), kcat/Km (s^-1 M^-1); cells 68, 0.1, 1.5

normalized_value_unit_evidence: Km=68 mM; kcat=0.1 s^-1; kcat/Km=0.0015 s^-1 mM^-1 (explicit table value / 1000)

raw_value_unit_evidence: HotAldO / 1-Phenyl-1,2-ethanediol: Km=68 mM; kcat=0.1 s^-1; kcat/Km=1.5 s^-1 M^-1


organism: Trametes cinnabarina

substrate_name: 5-formyl-2-furan carboxylic acid

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

substrate: 5-formyl-2-furan carboxylic acid


substrate_name: 2,5-hydroxymethylfurancarboxylic acid

substrate: 2,5-hydroxymethylfurancarboxylic acid


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


proof_lines:
pH 6, 25°C, presence of 1 mM H2O2
pH 6, 25°C, presence of 15 mM H2O2
pH 6, 25°C


proof_lines: pH 6, 25°C, presence of 6 mM formylfurancarboxylic acid

proof_lines: pH 6, 25°C, presence of 0.8 mM formylfurancarboxylic acid


organism: Fusarium graminearum

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


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


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


substrate_name: 3-Methoxybenzyl alcohol

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

substrate: 3-Methoxybenzyl alcohol


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


enzyme_display_name: (R)-mandelonitrile oxidase

organism: Chamberlinius hualienensis

substrate_name: (R,S)-mandelonitrile

sequence_source: GenBank LC036560.1 CDS translation

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

assay_conditions_summary: pH 5

enzyme: (R)-mandelonitrile oxidase

substrate: (R,S)-mandelonitrile


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


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 / 3,4-Dimethoxybenzyl (veratryl) alcohol; FoxAAO columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1); cells KM=3.0 +/- 0.24; kcat=25 +/- 1.2; kcat/KM=8300

normalized_value_unit_evidence: kcat normalized_value=25.0 s^-1; Km normalized_value=3.0 mM; kcat/Km normalized_value=8.333333333333334 s^-1*mM^-1 (printed table efficiency normalized=8.3 s^-1*mM^-1)

raw_value_unit_evidence: kcat raw_value=25 +/- 1.2 s^-1; Km raw_value=3.0 +/- 0.24 mM; kcat/Km raw_value=8300 M^-1 s^-1; source/export central value derived from same-row kcat/Km = 8.333333333333334 s^-1*mM^-1


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


column_label: Table 1. Substrate specificity of FgrAAO and FoxAAO; row FoxAAO / Benzyl alcohol; FoxAAO columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1); cells KM=30 +/- 19; kcat=31 +/- 4.2; kcat/KM=1000 (350 +/- 20)a

normalized_value_unit_evidence: kcat normalized_value=31.0 s^-1; Km normalized_value=30.0 mM; kcat/Km normalized_value=1.0333333333333334 s^-1*mM^-1 (printed table efficiency normalized=1.0 s^-1*mM^-1)

raw_value_unit_evidence: kcat raw_value=31 +/- 4.2 s^-1; Km raw_value=30 +/- 19 mM; kcat/Km raw_value=1000 (350 +/- 20)a M^-1 s^-1; source/export central value derived from same-row kcat/Km = 1.0333333333333334 s^-1*mM^-1

row_label: FoxAAO / Benzyl alcohol


substrate_name: 4-methoxybenzyl alcohol

column_label: Table 1; enzyme column group FoxAAO; row_label: 4-Methoxybenzyl (p-anisyl) alcohol; columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1)

normalized_value_unit_evidence: normalized: kcat=34 s^-1; km=51 mM; kcat_over_km=0.29 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for FoxAAO / 4-Methoxybenzyl (p-anisyl) alcohol: KM=51 +/- 12 mM; kcat=34 +/- 2.9 s^-1; kcat/KM=290 M^-1 s^-1

row_label: 4-Methoxybenzyl (p-anisyl) 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


enzyme_display_name: 4-hydroxymandelate oxidase

organism: Streptomyces coelicolor

substrate_name: L-Mandelate

enzyme: 4-hydroxymandelate oxidase

substrate: L-Mandelate


assay_conditions_summary: pH 7