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.


enzyme_display_name: vanillyl-alcohol oxidase

organism: Penicillium simplicissimum

substrate_name: chavicol

source_db: brenda

verification_status: verified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

mutation_type: substitution

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.

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)

data_origin: experimental

enzyme: vanillyl-alcohol oxidase

substrate: chavicol

status: verified

source: brenda


mutation_signature: Unknown

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

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

substrate_name: Vanillyl alcohol

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

assay_conditions_summary: pH 7

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

substrate: Vanillyl alcohol


verification_status: unverified

assay_conditions_summary: pH 10

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

status: unverified


substrate_name: creosol

assay_conditions_summary: pH 8

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


km_display: Not reported

kcat_over_km_display: Not reported

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


enzyme_display_name: alditol oxidase

organism: Acidothermus cellulolyticus

enzyme: alditol oxidase


substrate_name: D-mannitol

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

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: 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

verification_status: corrected

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

status: corrected


substrate_name: xylitol

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

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.


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


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


organism: Streptomyces coelicolor

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

sequence_source: multiple

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

source_databases_merged: brenda skid


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: 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)

source_db: uniprot

kcat_display: Not reported

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

source: uniprot


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

smiles: O=O

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.


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

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


substrate_name: p-Cresol

substrate: p-Cresol


enzyme_display_name: 2-Hydroxyacid oxidase 2

organism: Rattus norvegicus

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

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

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


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


enzyme_display_name: Glycolate oxidase

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.

enzyme: Glycolate oxidase

substrate: glycolate (at 25 degrees Celsius)


enzyme_display_name: UniProt Q9UJM8

organism: Homo sapiens

substrate_name: glycolate

source_db: skid

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

source_databases_merged: skid uniprot

enzyme: UniProt Q9UJM8

substrate: glycolate

source: skid


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

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

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

source_databases_merged: brenda uniprot

enzyme: choline oxidase

substrate: choline


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


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

table_label: Table 1

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


source_db: oed

source: oed


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


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

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

source_license: CC BY-NC-ND 4.0

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

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.


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

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.

substrate: choline


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


organism: Penicillium simplicissimum

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

substrate: 4-methoxybenzyl alcohol


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

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

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


enzyme_display_name: 4-hydroxymandelate oxidase

organism: Streptomyces coelicolor

substrate_name: L-Mandelate

enzyme: 4-hydroxymandelate oxidase

substrate: L-Mandelate


organism: Methylovorus sp. MP688


enzyme_display_name: C-glycoside oxidase

organism: Microbacterium sp. 5-2b

substrate_name: carminate

proof_lines: kcat is 4.3 sec(-1) with carminic acid as substrate.

enzyme: C-glycoside oxidase

substrate: carminate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I73V/H74Y/G356H/V367L/T414K/A419Y/A435E to reconstruct the assayed variant sequence.


organism: Methylovorus sp. (strain MP688)

substrate_name: phenylmethanethiol

proof_lines: kcat is 9.9 sec(-1) with 5-(hydroxymethyl)furfural as substrate. kcat is 21.1 sec(-1) with 1,4-benzenedimethanol as substrate. kcat is 14.0 sec(-1) with 1,3-benzenedimethanol as substrate. kcat is 13.5 sec(-1) with benzyl alcohol as substra

substrate: phenylmethanethiol


assay_conditions_summary: pH 8; buffer 50 mM potassium phosphate

column_label: Table 1, row 1,4-Benzenedimethanol, column Km (mM), cell 1.4 mM

raw_value_unit_evidence: Table 1 row 1,4-Benzenedimethanol, Km (mM) = 1.4 mM

table_label: Table 1. Steady-state kinetic parameters of HMFO


column_label: Table 1, row 1,3-Benzenedimethanol, column Km (mM), cell 1.5 mM

raw_value_unit_evidence: Table 1 row 1,3-Benzenedimethanol, Km (mM) = 1.5 mM


column_label: Table 1, row Benzyl alcohol, column Km (mM), cell 1.3 mM

raw_value_unit_evidence: Table 1 row Benzyl alcohol, Km (mM) = 1.3 mM

row_label: Benzyl alcohol


substrate_name: 4-hydroxybenzyl alcohol

column_label: Table 1, row 4-Hydroxybenzyl alcohol, column Km (mM), cell 0.3 mM

raw_value_unit_evidence: Table 1 row 4-Hydroxybenzyl alcohol, Km (mM) = 0.3 mM

row_label: 4-Hydroxybenzyl alcohol

substrate: 4-hydroxybenzyl alcohol


substrate_name: 4-aminobenzyl alcohol

column_label: Table 1, row 4-Aminobenzyl alcohol, column Km (mM), cell 1.44 mM

raw_value_unit_evidence: Table 1 row 4-Aminobenzyl alcohol, Km (mM) = 1.44 mM

row_label: 4-Aminobenzyl alcohol

substrate: 4-aminobenzyl alcohol


substrate_name: 4-chlorobenzyl alcohol

column_label: Table 1, row 4-Chlorobenzyl alcohol, column Km (mM), cell 0.08 mM

raw_value_unit_evidence: Table 1 row 4-Chlorobenzyl alcohol, Km (mM) = 0.08 mM

row_label: 4-Chlorobenzyl alcohol

substrate: 4-chlorobenzyl alcohol


column_label: Table 1, row Cinnamyl alcohol, column Km (mM), cell 0.07 mM

raw_value_unit_evidence: Table 1 row Cinnamyl alcohol, Km (mM) = 0.07 mM

row_label: Cinnamyl alcohol


smiles: CC=CC=CCO

column_label: Table 1, row 2,4-Hexadien-1-ol, column Km (mM), cell 0.59 mM

raw_value_unit_evidence: Table 1 row 2,4-Hexadien-1-ol, Km (mM) = 0.59 mM


substrate_name: vanillyl alcohol

column_label: Table 1, row Vanillyl alcohol, column Km (mM), cell 0.73 mM

raw_value_unit_evidence: Table 1 row Vanillyl alcohol, Km (mM) = 0.73 mM

row_label: Vanillyl alcohol

substrate: vanillyl alcohol


organism: Amycolatopsis orientalis

substrate_name: (S)-Mandelate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y128F to reconstruct the assayed variant sequence.

substrate: (S)-Mandelate


column_label: Results prose line with active Hmo oxidase metric; row label Hmo WT (S)-mandelate to benzoylformate; metric kcat

normalized_value_unit_evidence: normalized: kcat=5.17 s^-1

raw_value_unit_evidence: paper text: kcat = 5.17 s^-1 and Km = 0.16 mM for conversion of (S)-mandelate to benzoylformate

row_label: Hmo WT conversion of (S)-mandelate to benzoylformate

table_label: Results prose on Hmo activity


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

column_label: Table 1 Fgr AAO DFF row lists 10+/-2.9, 3.6+/-0.27, and 360.

normalized_value_unit_evidence: KM normalized_value=10 normalized_unit=mM; kcat normalized_value=3.6 normalized_unit=s^-1; kcat/KM normalized_value=0.36 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: DFF row reports KM raw_value=10+/-2.9 raw_unit=mM; kcat raw_value=3.6+/-0.27 raw_unit=s^-1; kcat/KM raw_value=360 raw_unit=M^-1 s^-1.

row_label: Fgr AAO DFF row

table_label: PMC8207647 Table 1


column_label: Table 1 Fgr AAO 3-methoxybenzyl alcohol row lists 6.5+/-1.5, 52+/-1.5, and 8000.

normalized_value_unit_evidence: KM normalized_value=6.5 normalized_unit=mM; kcat normalized_value=52 normalized_unit=s^-1; kcat/KM normalized_value=8 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: 3-Methoxybenzyl alcohol row reports KM raw_value=6.5+/-1.5 raw_unit=mM; kcat raw_value=52+/-1.5 raw_unit=s^-1; kcat/KM raw_value=8000 raw_unit=M^-1 s^-1.

row_label: Fgr AAO 3-methoxybenzyl alcohol row


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

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

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 Fgr AAO benzyl alcohol row lists 86+/-12, 37+/-2.8, and 430.

normalized_value_unit_evidence: KM normalized_value=86 normalized_unit=mM; kcat normalized_value=37 normalized_unit=s^-1; kcat/KM normalized_value=0.43 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Benzyl alcohol row reports KM raw_value=86+/-12 raw_unit=mM; kcat raw_value=37+/-2.8 raw_unit=s^-1; kcat/KM raw_value=430 raw_unit=M^-1 s^-1.

row_label: Fgr AAO benzyl alcohol row


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

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_name: 4-Methoxybenzyl alcohol

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

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: 4-Methoxybenzyl alcohol


substrate_name: 4-Hydroxy-3-methoxybenzyl alcohol

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

substrate: 4-Hydroxy-3-methoxybenzyl alcohol


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


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


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


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

proof_lines: mutant enzyme V367R/W466F, at pH 7.5 and 25°C


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


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


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


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


proof_lines: Km above 4.0 mM, wild type enzyme, at pH 7.5 and 25°C


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

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 / 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

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


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

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

row_label: FoxAAO / HMFCA


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

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

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


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

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


substrate_name: terephthaldehyde

column_label: Table 2: degree of hydration and kinetic parameters for HMFO of all studied aldehydes at 25 C, pH 7.0; Entry 5, substrate 8 (terephthaldehyde); required column(s): kcat/KM [s^-1 mM^-1].

raw_value_unit_evidence: Table 2 entry 5 substrate 8: gem-Diol 8.4%; kcat 1.3 s^-1; KM 0.085 mM; kcat/KM 15 s^-1 mM^-1. Required metric evidence: kcat/KM [s^-1 mM^-1] = 15.0 s^(-1)*mM^(-1).

substrate: terephthaldehyde


column_label: Table 2: degree of hydration and kinetic parameters for HMFO of all studied aldehydes at 25 C, pH 7.0; Entry 4, substrate 7 (4-(Hydroxymethyl)benzaldehyde); required column(s): kcat/KM [s^-1 mM^-1], KM [mM][a].

raw_value_unit_evidence: Table 2 entry 4 substrate 7: gem-Diol 0.4%; kcat 8.6 s^-1; KM 0.15 mM; kcat/KM 57 s^-1 mM^-1. Required metric evidence: kcat/KM [s^-1 mM^-1] = 57.0 s^(-1)*mM^(-1); KM [mM][a] = 0.15 mM.


column_label: Table 2: degree of hydration and kinetic parameters for HMFO of all studied aldehydes at 25 C, pH 7.0; Entry 4, substrate 7 (4-(Hydroxymethyl)benzaldehyde); required column(s): kcat/KM [s^-1 mM^-1].

raw_value_unit_evidence: Table 2 entry 4 substrate 7: gem-Diol 0.4%; kcat 8.6 s^-1; KM 0.15 mM; kcat/KM 57 s^-1 mM^-1. Required metric evidence: kcat/KM [s^-1 mM^-1] = 57.0 s^(-1)*mM^(-1).


enzyme_display_name: vanillyl-alcohol oxidase

substrate_name: Vanillyl alcohol

enzyme: vanillyl-alcohol oxidase

substrate: Vanillyl alcohol


enzyme_display_name: Alditol oxidase

organism: Streptomyces sp. (strain IKD472 / FERM P-14339)

substrate_name: xylitol

column_label: PMID 16232758 Table 4, Xylitol row, Km column, 0.68 mM.

raw_value_unit_evidence: Table 4 reports Km = 0.68 mM for xylitol.

row_label: Xylitol

table_label: Table 4

enzyme: Alditol oxidase

substrate: xylitol


substrate_name: D-sorbitol

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

substrate: D-sorbitol


column_label: Catalytic properties prose reports oxygen K_m 12 uM during vanillyl-alcohol oxidation.

raw_value_unit_evidence: Km raw_value=12 raw_unit=uM

row_label: oxygen electron acceptor

table_label: Catalytic properties prose - electron acceptor kinetics


substrate_name: phenazine methosulfate

column_label: Catalytic properties prose reports phenazine methosulfate K_m 43 uM as replacement electron acceptor.

raw_value_unit_evidence: Km raw_value=43 raw_unit=uM

row_label: phenazine methosulfate electron acceptor

substrate: phenazine methosulfate


organism: Pleurotus eryngii

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: Mutation signature H91N/L170M/F501W could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Pseudomonas nitroreducens

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


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

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

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


column_label: TABLE 3. Steady-state kinetic constants for the oxidation of vanillyl alcohol, HMF, DFF, and FDCA by HMFOs; row Vanillyl alcohol / PseniHMFOHis; columns kcat, Km, kcat/Km; kcat raw_value=60 +/- 3 raw_unit=min^-1; Km raw_value=0.8 +/- 0.2 raw_unit=mM; kcat/Km raw_value=78 +/- 17 raw_unit=mM^-1*min^-1

normalized_value_unit_evidence: kcat normalized_value=1.0 normalized_unit=s^-1; Km normalized_value=0.8 normalized_unit=mM; kcat/Km normalized_value=1.25 normalized_unit=s^-1*mM^-1

row_label: Vanillyl alcohol / PseniHMFOHis


organism: Escherichia coli


enzyme_display_name: ecdysone oxidase

organism: Spodoptera littoralis

substrate_name: ecdysone

enzyme: ecdysone oxidase

substrate: ecdysone


organism: Alcaligenes sp.

substrate_name: Betaine aldehyde

column_label: Abstract states the values of Km for choline and betaine aldehyde were 0.87 and 6.2 mM respectively.

raw_value_unit_evidence: Km raw_value=6.2 raw_unit=mM

row_label: Alcaligenes sp. choline oxidase with betaine aldehyde

table_label: PubMed abstract PMID 6997283

substrate: Betaine aldehyde


organism: Homo sapiens

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


organism: Arthrobacter globiformis

substrate_name: choline

substrate: choline


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H351Q with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


organism: Penicillium simplicissimum


enzyme_display_name: long-chain-alcohol oxidase

organism: uncultured marine group II/III euryarchaeote KM3_72_H01

column_label: PMID 34709726 / DOI 10.1002/cbic.202100510, Biochemical characterisation paragraph, A0A075HNX4 LCAO with 1-dodecanol, K_M value = 27.7 uM (+/-3.8 uM).

raw_value_unit_evidence: Main text reports K_M value of 27.7 uM (+/-3.8 uM) for 1-dodecanol and specific activity of 0.23 umol min^-1 mg^-1.

row_label: A0A075HNX4 / 1-dodecanol

table_label: Main text Biochemical characterisation paragraph

enzyme: long-chain-alcohol oxidase


enzyme_display_name: glycerol-3-phosphate oxidase

organism: Enterococcus casseliflavus

substrate_name: sn-Glycerol 3-phosphate

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

enzyme: glycerol-3-phosphate oxidase

substrate: sn-Glycerol 3-phosphate


enzyme_display_name: N-acylhexosamine oxidase

organism: Ralstonia solanacearum

substrate_name: chitobiose

column_label: PMID 34709726 / DOI 10.1002/cbic.202100510, Table 1, row chitobiose, column K_M [mM] / A3RXB7 = 19.

normalized_value_unit_evidence: Km=19 mM.

raw_value_unit_evidence: Table 1 row chitobiose, K_M [mM] / A3RXB7 column = 19; adjacent specific activity / A3RXB7 column = 0.9 umol min^-1 mg^-1.

row_label: A3RXB7 / chitobiose

enzyme: N-acylhexosamine oxidase

substrate: chitobiose


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


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


proof_lines: (S)-mandelate benzoylformate Hmo


enzyme_display_name: prosolanapyrone-II oxidase

organism: Alternaria solani

substrate_name: prosolanapyrone II

assay_conditions_summary: pH 7; buffer 50 mM potassium phosphate

column_label: ScienceDirect full-text section 3.5 reports Km for conversion of prosolanapyrone II (5) to solanapyrone A (1) as 16 uM from the Fig. 4 double-reciprocal plot.

raw_value_unit_evidence: Km raw_value=16 raw_unit=uM

row_label: prosolanapyrone II (5) conversion to solanapyrone A (1)

table_label: Section 3.5 / Fig. 4 double-reciprocal plot

enzyme: prosolanapyrone-II oxidase

substrate: prosolanapyrone II


organism: Methylovorus sp. MP688

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I73V/H74Y/G356H/V367L/T414K/A419Y/A435E to reconstruct the assayed variant sequence.


column_label: Table I row 4-Propylphenol has kcat 3.9 s^-1 and Km 3 uM.

raw_value_unit_evidence: Table I reports 4-Propylphenol kcat = 3.9 s^-1 and Km = 3 uM.

table_label: Biotechnology and Bioengineering Table I, kinetic parameters for 4-alkylphenols by VAO


organism: Candida tropicalis

substrate_name: Tetradecanol

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

smiles: CCCCCCCCCCCCCCO

substrate: Tetradecanol


substrate_name: hexadecanol

substrate: hexadecanol


substrate_name: Dodecanol

proof_lines:
aqueous phase
octane/aqueous phase 99/1

substrate: Dodecanol


substrate_name: Decanol

smiles: CCCCCCCCCCO

substrate: Decanol


smiles: O=O


substrate_name: Octanol

smiles: CCCCCCCCO

substrate: Octanol


organism: Sus scrofa

substrate_name: glycolate

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

substrate: glycolate


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

proof_lines:
short chain oxidase
short chain oxidase, at pH 6.0 and 37°C
long chain oxidase


substrate_name: L-lactate

substrate: L-lactate


substrate_name: DL-beta-phenyllactate

ki_unit: mM

substrate: DL-beta-phenyllactate


organism: Oryza sativa Japonica Group


substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: glycerate

substrate: glycerate


enzyme_display_name: UniProt P13650

organism: Acinetobacter calcoaceticus

substrate_name: cellobiose

proof_lines:
Raw SKiD Env: Temp=-----, pH=7
Raw SKiD Env: Temp=25°C, pH=7

enzyme: UniProt P13650

substrate: cellobiose


substrate_name: D-galactose

substrate: D-galactose


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


enzyme_display_name: UniProt Q88JH0

organism: Pseudomonas putida

substrate_name: ethanol

smiles: CCO

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

enzyme: UniProt Q88JH0

substrate: ethanol


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


enzyme_display_name: UniProt B8MX95

organism: Aspergillus flavus

substrate_name: D-glucose

enzyme: UniProt B8MX95

substrate: D-glucose


enzyme_display_name: cholesterol oxidase

organism: Streptomyces sp.

substrate_name: dehydroepiandrosterone

enzyme: cholesterol oxidase

substrate: dehydroepiandrosterone


substrate_name: cholesterol

proof_lines: enzyme from cultured immobilized cells, pH and temperature not specified in the publication

proof_lines: enzyme from cultured free cells, pH and temperature not specified in the publication

substrate: cholesterol


enzyme_display_name: glucose 1-dehydrogenase (PQQ, quinone)

organism: Escherichia coli

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

proof_lines: N462H mutant isozyme PQQGDH-B, pH 7.0, 25°C

enzyme: glucose 1-dehydrogenase (PQQ, quinone)


proof_lines: N452T mutant isozyme PQQGDH-B, pH 7.0, 25°C


substrate_name: lactose

substrate: lactose


substrate_name: maltose

substrate: maltose


proof_lines: wild-type isozyme PQQGDH-B, pH 7.0, 25°C


enzyme_display_name: alcohol dehydrogenase (quinone)

organism: Komagataeibacter xylinus

substrate_name: acetaldehyde

smiles: CC=O

proof_lines: using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication

enzyme: alcohol dehydrogenase (quinone)

substrate: acetaldehyde


substrate_name: n-butanol

smiles: CCCCO

substrate: n-butanol


substrate_name: allylic alcohol

smiles: C=CCO

substrate: allylic alcohol


proof_lines: using ethanol as cosubstrate, pH and temperature not specified in the publication


substrate_name: 5-(hydroxymethyl)furoic acid

proof_lines: mutant enzyme F412V/W561A, pH and temperature not specified in the publication

substrate: 5-(hydroxymethyl)furoic acid


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


organism: Pseudomonas aeruginosa


substrate_name: citronellol

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

substrate: citronellol


substrate_name: geraniol

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

substrate: geraniol


substrate_name: citral

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

substrate: citral


substrate_name: citronellal

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

substrate: citronellal


enzyme_display_name: glucose 1-dehydrogenase (FAD, quinone)

organism: Pseudomonas sp.

substrate_name: coenzyme Q1

enzyme: glucose 1-dehydrogenase (FAD, quinone)

substrate: coenzyme Q1


substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


assay_conditions_summary: pH 6

proof_lines: reaction with 2,6-dichlorophenolindophenol at pH 6.0

proof_lines: reaction with phenazine methosulfate/2,6-dichlorophenolindophenol at pH 8.75


substrate_name: tetramethyl-p-phenylenediamine

substrate: tetramethyl-p-phenylenediamine


substrate_name: ferricyanide

substrate: ferricyanide


organism: Gluconacetobacter diazotrophicus

substrate_name: D-galactose

substrate: D-galactose


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


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


substrate_name: ethanol

proof_lines: in the presence of ethylamine, at pH 9.0 and 25°C

proof_lines: in the presence of pentylamine, at pH 9.0 and 25°C

substrate: ethanol


smiles: CCCO


organism: Colletotrichum gloeosporioides

substrate_name: D-xylose

proof_lines:
native enzyme, pH 5.5, 30°C
recombinant enzyme, pH 5.5, 30°C
native enzyme, pH 7.5, 30°C

substrate: D-xylose


substrate_name: D-glucose

proof_lines:
recombinant enzyme, pH 5.5, 30°C
native enzyme, pH 5.5, 30°C
native enzyme, pH 7.5, 30°C

substrate: D-glucose


organism: Burkholderia cepacia

proof_lines: wild type enzyme, at pH 7.0, temperature not specified in the publication

proof_lines: A472F mutant, higher specificity toward glucose compared to the wild type enzyme, no activity towards maltose

proof_lines: N475D mutant, higher specificity toward glucose compared to the wild type enzyme, no activity towards maltose


proof_lines: mutant enzyme C213S, at pH 7.0, temperature not specified in the publication


proof_lines: recombinant wild-type isozyme PQQGDH-B, pH 7.0

proof_lines: pH 7.0, temperature not specified in the publication, wild-type enzyme


substrate_name: lactose

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

substrate: lactose


assay_conditions_summary: pH 6.5; 298.15 K; cofactor FAD

proof_lines: mutant enzyme V149C/G190C, at pH 6.5 and 25°C

proof_lines: mutant enzyme V149C7G190C, at pH 6.5 and 25°C


substrate_name: glucose

assay_conditions_summary: cofactor FAD

substrate: glucose


organism: Aspergillus niger

proof_lines: at pH 6.5, temperature not specified in the publication


organism: Pyrobaculum aerophilum

substrate_name: maltose

proof_lines: in 50 mM Bis-Tris propane (pH 8.0), at 50°C

proof_lines: in 50 mM Bis?-ris propane (pH 8.0), at 50°C

substrate: maltose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: D-fructose

substrate: D-fructose


organism: Arthrobacter globiformis


substrate_name: N-methylphenazonium methyl sulfate

proof_lines: with D-glucose as cosubstrate, at pH 5.0 and 45°C

substrate: N-methylphenazonium methyl sulfate


proof_lines: wild-type isozyme PQQGDH-B, pH 7.0, 25°C


proof_lines: recombinant wild-type enzyme with bound Mg2+, pH 6.5, 25°C


organism: Pseudomonas taetrolens


substrate_name: sucrose

substrate: sucrose


enzyme_display_name: cyclic alcohol dehydrogenase (quinone)

organism: Gluconobacter frateurii

substrate_name: Cyclopentanol

enzyme: cyclic alcohol dehydrogenase (quinone)

substrate: Cyclopentanol


organism: Aspergillus terreus

proof_lines:
apparent turnover number
apparent KM-value


organism: Mucor circinelloides

assay_conditions_summary: pH 7; 310.15 K; cofactor FAD

proof_lines: recombinant enzyme, apparent value, at pH 7.0 and 37°C


proof_lines: at 40°C after preincubation of the enzyme at 70°C for 30 min


assay_conditions_summary: 313.15 K; cofactor FAD

proof_lines: pH and temperature not specified in the publication


organism: Acinetobacter baumannii


organism: Aspergillus oryzae

assay_conditions_summary: pH 7.4; 310.15 K; cofactor FAD

proof_lines: pH 7.4, 37°C, enzyme immobilized on amperometric electrode


organism: Acidomonas methanolica


organism: Acinetobacter calcoaceticus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D167E/N452T to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7


substrate_name: allose

substrate: allose


organism: Rasamsonia emersonii

proof_lines: pH 7.0, 37°C, glycosylated recombinant protein

proof_lines: pH 7.0, 37°C, unglycosylated recombinant protein


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I278F with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N279H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D275E/D276E with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


organism: Thermus thermophilus

substrate_name: xylitol

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

substrate: xylitol


substrate_name: mannitol

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

substrate: mannitol


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y156A with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


substrate_name: methanol

smiles: CO

source_databases_merged: brenda oed

substrate: methanol


substrate_name: D-glucosamine

substrate: D-glucosamine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y156K with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


substrate_name: L-arabinose

substrate: L-arabinose


substrate_name: D-galactose

substrate: D-galactose


substrate_name: D-cellobiose

substrate: D-cellobiose


substrate_name: D-glucose 6-phosphate

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

substrate: D-glucose 6-phosphate


substrate_name: D-ribose

substrate: D-ribose


substrate_name: maltotriose

substrate: maltotriose


substrate_name: maltose

substrate: maltose


organism: Thermoascus crustaceus

substrate_name: D-glucose

assay_conditions_summary: pH 7; cofactor FAD

substrate: D-glucose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T416V/T417V to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant T416V/T417V, pH 7.0, 25°C


enzyme_display_name: quinoprotein glucose dehydrogenase (PQQ, quinone)

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

column_label: Table 1; row_label: wild type / 2-deoxy-D-glucose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=1141 s^-1; Km=40 mM; kcat/Km=29.483 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for wild type / 2-deoxy-D-glucose: kcat=1141 s^-1; Km=0.04 M; kcat/Km=29483 s^-1 M^-1

row_label: wild type / 2-deoxy-D-glucose

table_label: Table 1


sequence_variant_note: Resolved canonical sequence from ncbi_genbank_accession:AFN86158.1 and applied mutation signature Y156A to reconstruct the assayed variant sequence.

column_label: Table 1; row_label: Y156A / 2-deoxy-D-glucose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=69 s^-1; Km=80 mM; kcat/Km=0.921 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156A / 2-deoxy-D-glucose: kcat=69 s^-1; Km=0.08 M; kcat/Km=921 s^-1 M^-1

row_label: Y156A / 2-deoxy-D-glucose

enzyme: quinoprotein glucose dehydrogenase (PQQ, quinone)


sequence_variant_note: Resolved canonical sequence from ncbi_genbank_accession:AFN86158.1 and applied mutation signature Y156K to reconstruct the assayed variant sequence.

column_label: Table 1; row_label: Y156K / 2-deoxy-D-glucose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=128 s^-1; Km=140 mM; kcat/Km=0.903 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156K / 2-deoxy-D-glucose: kcat=128 s^-1; Km=0.14 M; kcat/Km=903 s^-1 M^-1

row_label: Y156K / 2-deoxy-D-glucose


substrate_name: alpha-D-lactose

column_label: Table 1; row_label: wild type / alpha-D-lactose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=1953 s^-1; Km=190 mM; kcat/Km=10.28 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for wild type / alpha-D-lactose: kcat=1953 s^-1; Km=0.19 M; kcat/Km=10280 s^-1 M^-1

row_label: wild type / alpha-D-lactose

substrate: alpha-D-lactose


column_label: Table 1; row_label: Y156A / alpha-D-lactose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=282 s^-1; Km=640 mM; kcat/Km=0.439 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156A / alpha-D-lactose: kcat=282 s^-1; Km=0.64 M; kcat/Km=439 s^-1 M^-1

row_label: Y156A / alpha-D-lactose


column_label: Table 1; row_label: Y156K / alpha-D-lactose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=225 s^-1; Km=650 mM; kcat/Km=0.343 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156K / alpha-D-lactose: kcat=225 s^-1; Km=0.65 M; kcat/Km=343 s^-1 M^-1

row_label: Y156K / alpha-D-lactose


column_label: Table 1; row_label: wild type / D-cellobiose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=1042 s^-1; Km=70 mM; kcat/Km=14.893 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for wild type / D-cellobiose: kcat=1042 s^-1; Km=0.07 M; kcat/Km=14893 s^-1 M^-1

row_label: wild type / D-cellobiose


column_label: Table 1; row_label: Y156A / D-cellobiose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=160 s^-1; Km=300 mM; kcat/Km=0.527 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156A / D-cellobiose: kcat=160 s^-1; Km=0.3 M; kcat/Km=527 s^-1 M^-1

row_label: Y156A / D-cellobiose


column_label: Table 1; row_label: Y156K / D-cellobiose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=186 s^-1; Km=230 mM; kcat/Km=0.808 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156K / D-cellobiose: kcat=186 s^-1; Km=0.23 M; kcat/Km=808 s^-1 M^-1

row_label: Y156K / D-cellobiose


column_label: Table 1; row_label: wild type / D-galactose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=823 s^-1; Km=110 mM; kcat/Km=7.488 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for wild type / D-galactose: kcat=823 s^-1; Km=0.11 M; kcat/Km=7488 s^-1 M^-1

row_label: wild type / D-galactose


enzyme_display_name: Alcohol dehydrogenase (quinone), dehydrogenase subunit

organism: Gluconobacter oxydans (strain 621H)

substrate_name: ubiquinone-2 (for ubiquinone reduction activity in inactive ADH at pH 5)

column_label: Official ScienceDirect HTML Table 2 row G. suboxydans inactive ADH gives Q2 Km 7.7 uM for ubiquinone reduction.

raw_value_unit_evidence: Km raw_value=7.7 raw_unit=uM

row_label: G. suboxydans inactive ADH; Q2 column

table_label: Table 2. Kinetic parameters for ubiquinone reduction and ubiquinol oxidation activities in active and inactive ADHs of G. suboxydans and active ADH of A. aceti


substrate_name: ubiquinol-2 (for ubiquinol oxidation activity in inactive ADH at pH 5)

column_label: Official ScienceDirect HTML Table 2 row G. suboxydans inactive ADH gives Q2H2 Km 13 uM for ubiquinol oxidation.

raw_value_unit_evidence: Km raw_value=13 raw_unit=uM

row_label: G. suboxydans inactive ADH; Q2H2 column

enzyme: Alcohol dehydrogenase (quinone), dehydrogenase subunit


substrate_name: ferricyanide (for ubiquinol oxidation activity in active ADH at pH 5)

column_label: Official ScienceDirect HTML Table 2 row G. suboxydans active ADH gives Ferricyanide Km 170 uM for ubiquinol oxidation.

raw_value_unit_evidence: Km raw_value=170 raw_unit=uM

row_label: G. suboxydans active ADH; Ferricyanide column


enzyme_display_name: Alcohol dehydrogenase (quinone), cytochrome c subunit

substrate: ubiquinone-2 (for ubiquinone reduction activity in inactive ADH at pH 5)


enzyme: Alcohol dehydrogenase (quinone), cytochrome c subunit

substrate: ubiquinol-2 (for ubiquinol oxidation activity in inactive ADH at pH 5)


substrate: ferricyanide (for ubiquinol oxidation activity in active ADH at pH 5)


enzyme_display_name: malate dehydrogenase (quinone)

organism: Plasmodium falciparum

substrate_name: decylubiquinone

column_label: ScienceDirect Fig. 3 caption states Km values were 6.21 +/- 0.65 uM and 5990 +/- 340 uM for dUQ and L-malate, respectively.

normalized_value_unit_evidence: Km normalized 0.00621 mM, matching CatLog rounded value 0.0062 mM.

raw_value_unit_evidence: Km raw 6.21 +/- 0.65 uM for dUQ/decylubiquinone.

row_label: dUQ/decylubiquinone, panel A

table_label: Fig. 3 caption/prose, Biochemical studies of PfMQO

enzyme: malate dehydrogenase (quinone)

substrate: decylubiquinone


substrate_name: (S)-malate

normalized_value_unit_evidence: Km normalized 5.99 mM.

raw_value_unit_evidence: Km raw 5990 +/- 340 uM for L-malate.

row_label: L-malate, panel B

substrate: (S)-malate


column_label: Table 1; row_label: Y156A / maltose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=186 s^-1; Km=370 mM; kcat/Km=0.5 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156A / maltose: kcat=186 s^-1; Km=0.37 M; kcat/Km=500 s^-1 M^-1

row_label: Y156A / maltose


column_label: Table 1; row_label: Y156K / maltose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=170 s^-1; Km=260 mM; kcat/Km=0.654 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156K / maltose: kcat=170 s^-1; Km=0.26 M; kcat/Km=654 s^-1 M^-1

row_label: Y156K / maltose


column_label: Table 1; row_label: wild type / maltotriose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=772 s^-1; Km=130 mM; kcat/Km=6.16 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for wild type / maltotriose: kcat=772 s^-1; Km=0.13 M; kcat/Km=6160 s^-1 M^-1

row_label: wild type / maltotriose


column_label: Table 1; row_label: Y156A / maltotriose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=822 s^-1; Km=600 mM; kcat/Km=1.366 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156A / maltotriose: kcat=822 s^-1; Km=0.6 M; kcat/Km=1366 s^-1 M^-1

row_label: Y156A / maltotriose


column_label: Table 1; row_label: Y156K / maltotriose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=363 s^-1; Km=160 mM; kcat/Km=2.283 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156K / maltotriose: kcat=363 s^-1; Km=0.16 M; kcat/Km=2283 s^-1 M^-1

row_label: Y156K / maltotriose


substrate_name: mannitol

column_label: Table 1; row_label: wild type / mannitol; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=38 s^-1; Km=90 mM; kcat/Km=0.414 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for wild type / mannitol: kcat=38 s^-1; Km=0.09 M; kcat/Km=414 s^-1 M^-1

row_label: wild type / mannitol

substrate: mannitol


substrate_name: xylitol

column_label: Table 1; row_label: wild type / xylitol; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=15 s^-1; Km=90 mM; kcat/Km=0.173 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for wild type / xylitol: kcat=15 s^-1; Km=0.09 M; kcat/Km=173 s^-1 M^-1

row_label: wild type / xylitol

substrate: xylitol


substrate_name: D-Xylose

column_label: Table 1; row_label: wild type / D-Xylose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

raw_value_unit_evidence: paper Table 1 cells for wild type / D-Xylose: kcat=1681 s^-1; Km=0.14 M; kcat/Km=12011 s^-1 M^-1

row_label: wild type / D-Xylose

substrate: D-Xylose


column_label: Table 1; row_label: Y156A / D-Xylose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=305 s^-1; Km=460 mM; kcat/Km=0.699 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156A / D-Xylose: kcat=305 s^-1; Km=0.46 M; kcat/Km=699 s^-1 M^-1

row_label: Y156A / D-Xylose


column_label: Table 1; row_label: Y156K / D-Xylose; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=204 s^-1; Km=230 mM; kcat/Km=0.872 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156K / D-Xylose: kcat=204 s^-1; Km=0.23 M; kcat/Km=872 s^-1 M^-1

row_label: Y156K / D-Xylose


substrate_name: cellobiose

column_label: Table 2 row cellobiose columns Km (mM), Kcat (S-1), and Kcat/Km (S-1*mM-1).

raw_value_unit_evidence: Table row reports Km 0.59 mM, Kcat 10.55 s^-1, and Kcat/Km 17.86 s^-1*mM^-1.

row_label: cellobiose

table_label: Table 2. Substrate-Oxidizing Activity of the MQO from P. taetrolens

substrate: cellobiose


substrate_name: lactose

column_label: Table 2 row lactose columns Km (mM) and Kcat (S-1).

raw_value_unit_evidence: Table row reports Km 0.71 mM, Kcat 14.67 s^-1, and Kcat/Km 20.76 s^-1*mM^-1.

row_label: lactose

substrate: lactose