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

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

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

row_label: m-Anisyl alcohol / rCcAAO


enzyme_display_name: aryl-alcohol oxidase

organism: Coprinopsis cinerea

substrate_name: 3-Hydroxybenzyl alcohol

source_db: oed

verification_status: unverified

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_accession and applied mutation signature L416F to reconstruct the assayed variant sequence.

mutation_type: substitution

data_origin: experimental

enzyme: aryl-alcohol oxidase

substrate: 3-Hydroxybenzyl alcohol

status: unverified

source: oed


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


verification_status: corrected

mutation_signature: Unknown

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

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

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

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

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

row_label: 3-Hydroxybenzyl alcohol / rCcAAO

table_label: Table 2

status: corrected


substrate_name: 4-anisyl alcohol

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

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

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

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

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

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

substrate: 4-anisyl alcohol


enzyme_display_name: alcohol oxidase

organism: Phanerodontia chrysosporium

verification_status: verified

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

smiles: CCCO

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

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

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

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

enzyme: alcohol oxidase

status: verified


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

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

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

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


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

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

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

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


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

row_label: 1-propanol / wild-type

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


substrate_name: ethanol

smiles: CCO

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

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

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

row_label: ethanol

substrate: ethanol


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

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

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


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

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

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


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

row_label: ethanol / wild-type


substrate_name: methanol

smiles: CO

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

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

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

row_label: methanol

substrate: methanol


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

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

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


enzyme_display_name: pyranose oxidase

organism: Trametes ochracea

substrate_name: L-sorbose

source_db: brenda

kcat_display: Not reported

kcat_over_km_display: Not reported

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

normalized_value_unit_evidence: km paper=38 mM

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

row_label: l-Sorbose

table_label: Table 3

enzyme: pyranose oxidase

substrate: L-sorbose

source: brenda


substrate_name: D-gluconolactone

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

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

substrate: D-gluconolactone


substrate_name: D-mannoheptose

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

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

normalized_value_unit_evidence: km paper=110 mM

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

row_label: d-Mannoheptose

substrate: D-mannoheptose


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

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

row_label: DCIP (pH 4.5)

table_label: Table 4


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

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

row_label: DCIP


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

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

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

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


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

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

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


substrate_name: D-Allose

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

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

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

row_label: d-Allose

substrate: D-Allose


substrate_name: D-Gentiobiose

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

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

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

row_label: Gentiobiose

substrate: D-Gentiobiose


substrate_name: D-Mannoheptose

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

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

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

substrate: D-Mannoheptose


substrate_name: D-Xylose

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

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

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

row_label: d-Xylose

substrate: D-Xylose


substrate_name: L-Arabinose

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

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

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

row_label: l-Arabinose

substrate: L-Arabinose


substrate_name: L-Sorbose

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

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

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

substrate: L-Sorbose


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

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

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

row_label: ABTS cation radical


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

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

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


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

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

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

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


organism: Lyophyllum shimeji

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

row_label: LsP2Ox row D-xylose

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


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

row_label: LsP2Ox row BQ

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


organism: Pleurotus eryngii

smiles: CC=CC=CC=O

assay_conditions_summary: pH 6; 297.15 K; buffer pH 6

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

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

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


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

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

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


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

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


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

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

row_label: m-Chlorobenzaldehyde


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

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

row_label: m-Fluorobenzaldehyde


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

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

row_label: p-Anisaldehyde


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


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

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

row_label: p-Chlorobenzaldehyde


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

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

row_label: p-Fluorobenzaldehyde


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

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

row_label: p-Nitrobenzaldehyde


enzyme_display_name: galactose oxidase

organism: Gibberella zeae

substrate_name: D-Galactose

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

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

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

row_label: Y436H/V494A — D-galactose

table_label: Table II

enzyme: galactose oxidase

substrate: D-Galactose


substrate_name: Methyl alpha-D-galactopyranoside

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

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

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

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

substrate: Methyl alpha-D-galactopyranoside


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

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

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

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


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

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

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

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


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

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

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

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


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

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

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

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


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

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

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

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


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

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

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

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


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

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

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

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

table_label: OUP/ISU full text Table II


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


substrate_name: melibiose

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

row_label: LsP2Ox row melibiose

substrate: melibiose


substrate_name: D-galactose

substrate: D-galactose


substrate_name: D-xylose

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

substrate: D-xylose


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

row_label: LsP2Ox row L-sorbose


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

row_label: LsP2Ox row DCIP


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

row_label: LsP2Ox row D-galactose


substrate_name: D-glucose

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

row_label: LsP2Ox row D-glucose

substrate: D-glucose


substrate_name: ferrocenium ion

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

row_label: LsP2Ox row Fc+

substrate: ferrocenium ion


substrate_name: 3-Chloro-4-methoxybenzyl alcohol

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

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

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

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

row_label: 3-Chloro-p-anisyl alcohol

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

substrate: 3-Chloro-4-methoxybenzyl alcohol


substrate_name: 3-Chlorobenzyl alcohol

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

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

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

row_label: m-Chlorobenzyl alcohol

substrate: 3-Chlorobenzyl alcohol


substrate_name: 3-Methoxybenzyl alcohol

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

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

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

substrate: 3-Methoxybenzyl alcohol


substrate_name: 4-Hydroxymethylbenzoic acid

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

row_label: p-(Hydroxymethyl) benzoic acid

substrate: 4-Hydroxymethylbenzoic acid


substrate_name: 4-Methoxybenzyl alcohol

substrate: 4-Methoxybenzyl alcohol


substrate_name: Isovanillyl alcohol

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

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

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

row_label: Isovanillyl alcohol

substrate: Isovanillyl alcohol


substrate_name: m-Fluorobenzyl alcohol

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

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

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

row_label: m-Fluorobenzyl alcohol

substrate: m-Fluorobenzyl alcohol


substrate_name: p-Chlorobenzyl alcohol

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

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

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

row_label: p-Chlorobenzyl alcohol

substrate: p-Chlorobenzyl alcohol


substrate_name: p-Fluorobenzyl alcohol

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

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

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

row_label: p-Fluorobenzyl alcohol

substrate: p-Fluorobenzyl alcohol


substrate_name: cinnamyl alcohol

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

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

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

row_label: Cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: benzaldehyde

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

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

row_label: Benzaldehyde

substrate: benzaldehyde


substrate_name: veratraldehyde

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

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

row_label: Veratraldehyde

substrate: veratraldehyde


substrate_name: methanol

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

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

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

row_label: methanol

substrate: methanol


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

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

row_label: methanol / wild-type


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

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

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


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

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

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


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

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

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


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

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

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


substrate_name: D-galactose

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

substrate: D-galactose


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


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


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


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


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

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

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

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

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

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


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


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


substrate_name: D-melibiose

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

substrate: D-melibiose


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


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


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


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


substrate_name: ferrocenium hexafluorophosphate

substrate: ferrocenium hexafluorophosphate


enzyme_display_name: cholesterol oxidase

organism: Streptomyces sp. SA-COO

substrate_name: cholesterol

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

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

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

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

enzyme: cholesterol oxidase

substrate: cholesterol


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


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

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

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


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

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

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


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

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

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

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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12676 and applied mutation signature L80C with inferred residue-numbering offset +37 to reconstruct the assayed variant sequence.

column_label: Table 1: Michaelis-Menten Constants and Tryptophan Fluorescence Emission Maxima for Wild-Type ChoA and ChoA Mutants (Biochemistry 2018, 57(36):5370-5378); Table 1, row 'mutant 1, L80C'; column 'kcat (s^-1)' prints 89; column 'Km (uM)' prints 11; column 'kcat/Km (M^-1 s^-1)' prints 8.4 x 10^6; column 'lambda-max Trp (nm)' prints 330.

normalized_value_unit_evidence: kcat: printed Table 1 cell 89 s^-1; already in s^-1, no conversion; the exported value is 89.0 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 11 uM; 11 / 1000 = 0.011 mM; the exported value is 0.011 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 8.4 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.4 x 10^6 / 1000 = 8400.0 s^-1 mM^-1. The exported ratio is 8090.909090909091 s^(-1)*mM^(-1), which is the quotient 89.0 / 0.011 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 8400.0 and kcat and Km are unchanged.

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


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

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

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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12676 and applied mutation signature T168C/A276C with inferred residue-numbering offset +37 to reconstruct the assayed variant sequence.

column_label: Table 1: Michaelis-Menten Constants and Tryptophan Fluorescence Emission Maxima for Wild-Type ChoA and ChoA Mutants (Biochemistry 2018, 57(36):5370-5378); Table 1, row 'mutant 5, T168C/A276C'; column 'kcat (s^-1)' prints 46; column 'Km (uM)' prints 14; column 'kcat/Km (M^-1 s^-1)' prints 3.4 x 10^6; column 'lambda-max Trp (nm)' prints 328.

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

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


column_label: Table 1: Michaelis-Menten Constants and Tryptophan Fluorescence Emission Maxima for Wild-Type ChoA and ChoA Mutants (Biochemistry 2018, 57(36):5370-5378); Table 1, row 'wild type'; column 'kcat (s^-1)' prints 67; column 'Km (uM)' prints 13; column 'kcat/Km (M^-1 s^-1)' prints 5.1 x 10^6; column 'lambda-max Trp (nm)' prints 329.

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

row_label: Table 1, row 'wild type'


organism: Fusarium graminearum

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

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

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

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

row_label: 3-Methoxybenzyl (m-anisyl) alcohol

table_label: Table 1


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

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

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

row_label: DFF


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

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

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

row_label: FgrAAO / HMFCA


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

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

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

row_label: FgrAAO / HMF


substrate_name: benzyl alcohol

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

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

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

row_label: FgrAAO / Benzyl alcohol

substrate: benzyl alcohol


substrate_name: veratryl alcohol

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

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

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

substrate: veratryl alcohol


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

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

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


organism: Fusarium oxysporum f. sp. lycopersici

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

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

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

row_label: FoxAAO / DFF


substrate_name: 3-Methoxybenzyl alcohol

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

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

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

substrate: 3-Methoxybenzyl alcohol


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

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

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

row_label: FoxAAO / HMFCA


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

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

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

row_label: FoxAAO / HMF


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


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


organism: Phanerochaete chrysosporium

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


substrate_name: alpha-D-Glucose

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

row_label: alpha-D(+)-Glucose

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

substrate: alpha-D-Glucose


substrate_name: beta-D-Glucose

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

row_label: beta-D(+)-Glucose

substrate: beta-D-Glucose


substrate_name: D-Glucose

substrate: D-Glucose


substrate_name: D-Xylose

row_label: D-Xylose

substrate: D-Xylose


substrate_name: L-Sorbose

row_label: L-Sorbose

substrate: L-Sorbose


substrate_name: Maltose

row_label: Maltose

substrate: Maltose


smiles: O=O

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

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

row_label: oxygen

table_label: Springer abstract prose


organism: Tricholoma matsutake

substrate_name: D-arabinose

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

assay_conditions_summary: pH 7

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

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

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

source_databases_merged: brenda uniprot

substrate: D-arabinose


substrate_name: D-xylose

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

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

substrate: D-xylose


substrate_name: trehalose

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

row_label: trehalose / T. matsutake pyranose oxidase

substrate: trehalose


substrate_name: D-maltose

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

row_label: maltose / T. matsutake pyranose oxidase

substrate: D-maltose


substrate_name: L-sorbose

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

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

substrate: L-sorbose


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

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


organism: Pleurotus sapidus

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

assay_conditions_summary: pH 6

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

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

row_label: Benzyl alcohol

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


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

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

row_label: Veratryl alcohol


substrate_name: anisyl alcohol

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

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

row_label: Anisyl alcohol

substrate: anisyl alcohol


organism: Ogataea thermomethanolica (nom. inval.)

substrate_name: methanol

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

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

row_label: Methanol

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

substrate: methanol


substrate_name: ethanol

substrate: ethanol


organism: Trametes sp.

substrate_name: D-glucose

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

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

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

substrate: D-glucose


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

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


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

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


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

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


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

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

row_label: TsPOx


organism: Arthrobacter chlorophenolicus

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

smiles: CCCCCCO

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

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


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


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


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


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


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


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

row_label: WT


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


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


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


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


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


organism: Aspergillus terreus

substrate_name: 3,4-dimethoxybenzyl alcohol

assay_conditions_summary: pH 6; 303.15 K; buffer 0.1 M sodium phosphate

column_label: Table 2 row Veratryl alcohol columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); expected value tuple belongs to a different substrate row.

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

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

substrate: 3,4-dimethoxybenzyl alcohol


substrate_name: 3-Methoxybenzyl alcohol

substrate: 3-Methoxybenzyl alcohol


substrate_name: benzyl alcohol

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

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

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

substrate: benzyl alcohol


substrate_name: 4-Methoxybenzyl alcohol

substrate: 4-Methoxybenzyl alcohol


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

normalized_value_unit_evidence: Km normalized_value=36.6 mM.

raw_value_unit_evidence: Methanol Km = 36.6 mM.

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


substrate_name: glycerol

smiles: C(C(CO)O)O

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

normalized_value_unit_evidence: Km normalized 1.9 mM.

raw_value_unit_evidence: Km raw 1.9 mM for glycerol.

row_label: Glycerol

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

substrate: glycerol


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

normalized_value_unit_evidence: Km normalized_value=22.5 mM.

raw_value_unit_evidence: Ethanol Km = 22.5 mM.

row_label: Ethanol


substrate_name: n-Pentanol

smiles: CCCCCO

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

normalized_value_unit_evidence: Km normalized 10.9 mM.

raw_value_unit_evidence: Km raw 10.9 mM for n-Pentanol.

row_label: n-Pentanol

substrate: n-Pentanol


substrate_name: n-Propanol

substrate: n-Propanol


enzyme_display_name: Pyranose 2-oxidase

organism: Phlebiopsis gigantea

source_db: uniprot

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

raw_value_unit_evidence: Km raw_value=0.65 mM raw_unit=mM

row_label: Prose segment: oxygen Km

table_label: PubMed PMID 8319689 abstract

enzyme: Pyranose 2-oxidase

source: uniprot


raw_value_unit_evidence: Km raw_value=1.1 mM raw_unit=mM

row_label: Prose segment: D-glucose Km


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


raw_value_unit_evidence: Km raw_value=29.4 mM raw_unit=mM

row_label: Prose segment: D-xylose Km


raw_value_unit_evidence: Km raw_value=50.0 mM raw_unit=mM

row_label: Prose segment: L-sorbose Km


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


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


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


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


organism: Thermothelomyces thermophilus

assay_conditions_summary: pH 6; 303.15 K; buffer pH 6

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

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

table_label: Table 1. MtAAOx substrate specificity and kinetic parameters


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

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

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

row_label: anisyl alcohol

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


substrate_name: cinnamyl alcohol

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

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

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

row_label: cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: veratryl alcohol

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

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

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

row_label: veratryl alcohol

substrate: veratryl alcohol


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


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


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


organism: Trametes pubescens

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

proof_lines:
Pyranose 2-oxidase
L-arabinose
Trametes pubescens


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

proof_lines:
Pyranose 2-oxidase
D-galactose
Trametes pubescens


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

proof_lines:
Pyranose 2-oxidase
melibiose
Trametes pubescens


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

proof_lines:
Pyranose 2-oxidase
L-sorbose
Trametes pubescens


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


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


enzyme_display_name: pyridoxine 4-oxidase

organism: Microbacterium luteolum

sequence_source: multiple

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

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

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

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

enzyme: pyridoxine 4-oxidase


substrate_name: vitamin K3

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

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

row_label: vitamin K3

substrate: vitamin K3


substrate_name: pyridoxine

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

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

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

row_label: pyridoxine (PN)

substrate: pyridoxine


organism: Peniophora sp.

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

source_databases_merged: brenda skid


substrate_name: D-xylose

substrate: D-xylose


substrate_name: L-sorbose

substrate: L-sorbose


organism: Mesorhizobium loti

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


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


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


organism: Pleurotus pulmonarius

substrate_name: m-anisyl alcohol

substrate: m-anisyl alcohol


substrate_name: 3,4-dimethoxybenzyl alcohol


substrate_name: p-anisyl alcohol

km_display: Not reported

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

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

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

raw_value_unit_evidence: Kcat raw_value=48.46 raw_unit=s-1

row_label: p-Anisyl alcohol

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

substrate: p-anisyl alcohol


enzyme_display_name: UniProt P0CS93

source_db: skid

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

smiles: C=C(CO)CO

proof_lines: oxidizes a range of primary alcohols to aldehydes

source_databases_merged: skid uniprot

enzyme: UniProt P0CS93

source: skid


substrate_name: D-galactose

substrate: D-galactose


organism: Methylovorus sp. MP688

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

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


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

row_label: MetspHMFO row / DFF substrate

table_label: PMC7414962 Table 3


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


organism: [Candida] methanosorbosa

substrate_name: methanol

substrate: methanol


substrate_name: ethanol

substrate: ethanol


substrate_name: benzyl alcohol


organism: Castellaniella sp.

substrate_name: cholesterol

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

assay_conditions_summary: pH 8

substrate: cholesterol


organism: Brevibacterium sterolicum


organism: Pseudomonas aeruginosa

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

raw_value_unit_evidence: Km raw_value=92.6 microM raw_unit=microM

row_label: Pseudomonas aeruginosa PA157 cholesterol oxidase / cholesterol

table_label: PubMed XML abstract PMID 25573142


organism: Fusarium graminearum


substrate_name: galactoglucomannan

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

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

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

row_label: GaO / Galacto-glucomannan

table_label: PDF Table 1

substrate: galactoglucomannan


organism: Chryseobacterium gleum

substrate_name: taurocholate

substrate: taurocholate


organism: Chrysomela tremula

substrate_name: 2-hydroxybenzyl alcohol

proof_lines:
2-hydroxybenzyl alcohol
pH 6.0

substrate: 2-hydroxybenzyl alcohol


organism: Trametes ochracea

proof_lines: Pyranose 2-oxidase from Trametes multicolor


substrate_name: D-glucose

substrate: D-glucose


organism: Chrysomela populi


organism: Gloeophyllum trabeum


organism: Gibberella zeae

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

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

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


organism: Fusarium sp.

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


organism: Streptomyces sp.


substrate_name: pregnenolone

substrate: pregnenolone


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


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


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


substrate_name: guar

substrate: guar


smiles: CC=CC=CCO


organism: Streptomyces virginiae

substrate_name: diosgenin

substrate: diosgenin


substrate_name: dehydroepiandrosterone

substrate: dehydroepiandrosterone


substrate_name: sitosterol

substrate: sitosterol


enzyme_display_name: 2-oxoglutarate reductase

organism: Escherichia coli

enzyme: 2-oxoglutarate reductase


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


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


enzyme_display_name: L-lactate dehydrogenase (cytochrome)

organism: Saccharomyces cerevisiae

substrate_name: Fluoropyruvate

enzyme: L-lactate dehydrogenase (cytochrome)

substrate: Fluoropyruvate


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: L-lactate

substrate: L-lactate


substrate_name: L-Mandelate

proof_lines: wild type enzyme with ferricyanide as electron acceptor

substrate: L-Mandelate


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


enzyme_display_name: alcohol dehydrogenase (cytochrome c)

organism: Pseudomonas putida

substrate_name: ethanol

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

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

enzyme: alcohol dehydrogenase (cytochrome c)


substrate_name: Propanol

assay_conditions_summary: pH 9

substrate: Propanol


proof_lines: pH 9.0, temperature not specified in the publication


enzyme_display_name: D-lactate dehydrogenase (cytochrome)

substrate_name: D-lactate

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

enzyme: D-lactate dehydrogenase (cytochrome)

substrate: D-lactate


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


enzyme_display_name: glucose oxidase

organism: Aspergillus niger

substrate_name: phenazine methosulfate

enzyme: glucose oxidase

substrate: phenazine methosulfate


substrate_name: cholesterol

substrate: cholesterol


organism: Streptomyces sp. SA-COO

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


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


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


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

organism: Ignisphaera aggregans

substrate_name: NADH

assay_conditions_summary: pH 7; cofactor NADH

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

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

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 7; cofactor NADPH

substrate: NADPH


substrate_name: ferricytochrome c

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

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

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

substrate: ferricytochrome c


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

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


assay_conditions_summary: pH 7.5; 298.15 K; cofactor FMN

proof_lines: Y143F mutant with cytochrome c as electron acceptor

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


proof_lines: native enzyme mutant with ferricyanide as electron acceptor


enzyme_display_name: UniProt Q9UJM8

organism: Homo sapiens

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt Q9UJM8


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


enzyme_display_name: long-chain-alcohol oxidase

organism: Simmondsia chinensis

substrate_name: Dodecanol

smiles: CCCCCCCCCCCCO

enzyme: long-chain-alcohol oxidase

substrate: Dodecanol


organism: Rhodopseudomonas palustris


smiles: CCO

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

substrate: ethanol


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


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


organism: Staphylococcus aureus

assay_conditions_summary: cofactor NADPH


substrate_name: ribulose 5-phosphate

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

substrate: ribulose 5-phosphate


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

organism: Rattus sp.

substrate_name: L-leucine

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

proof_lines:
isozymes beta1 and beta2
isozyme beta2
pH 7.5

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

substrate: L-leucine


proof_lines:
isozyme beta1
isozyme beta2
pH 7.0


substrate_name: L-Phenyllactate

proof_lines:
isozyme beta1
isozyme beta2
pH 7.0 and 7.5

substrate: L-Phenyllactate


proof_lines:
isozyme beta1
isozyme beta2
pH 7.5


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


organism: Aerococcus viridans

smiles: O=O

assay_conditions_summary: cofactor FMN


substrate_name: (S)-lactate

substrate: (S)-lactate


enzyme_display_name: choline oxidase

organism: Cylindrocarpon didymum

substrate_name: choline

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

enzyme: choline oxidase

substrate: choline


substrate_name: Betaine aldehyde

substrate: Betaine aldehyde


substrate_name: N,N-Dimethylaminoethanol

smiles: CN(C)CCO

substrate: N,N-Dimethylaminoethanol


organism: Tanacetum vulgare


substrate_name: n-Octanol

smiles: CCCCCCCCO

substrate: n-Octanol


substrate_name: geraniol

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

substrate: geraniol


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


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


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

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


organism: Mesostigma viride

substrate_name: glycolate

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

substrate: glycolate


substrate_name: L-lactate

substrate: L-lactate


organism: Mycolicibacterium smegmatis


proof_lines:
4°C, pH 7
25°C, pH 7


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


enzyme_display_name: ecdysone oxidase

organism: Calliphora vicina

substrate_name: oxidized 2,6-dichloroindophenol

enzyme: ecdysone oxidase

substrate: oxidized 2,6-dichloroindophenol


substrate_name: ecdysone

proof_lines:
optical assay
radio assay

substrate: ecdysone


organism: Rattus norvegicus


substrate_name: betaine aldehyde

proof_lines: oxidation of choline is competitively inhibited

substrate: betaine aldehyde


enzyme_display_name: N-acylhexosamine oxidase

organism: Pseudomonas sp.

substrate_name: N-acetyl-D-galactosamine

enzyme: N-acylhexosamine oxidase

substrate: N-acetyl-D-galactosamine


substrate_name: N-Glycolyl-D-glucosamine

substrate: N-Glycolyl-D-glucosamine


substrate_name: D-galactosamine

substrate: D-galactosamine


substrate_name: N,N-diacetylchitobiose

substrate: N,N-diacetylchitobiose


substrate_name: N-acetyl muramic acid

substrate: N-acetyl muramic acid


substrate_name: D-mannose

substrate: D-mannose


substrate_name: L-Mandelate

substrate: L-Mandelate


substrate_name: DL-glycerate

proof_lines:
at pH 6.0
at pH 7.0

substrate: DL-glycerate


substrate_name: (S)-lactate

substrate: (S)-lactate


substrate_name: DL-alpha-hydroxy-n-valerate

substrate: DL-alpha-hydroxy-n-valerate


organism: Fusarium oxysporum

substrate_name: choline

substrate: choline


substrate_name: Betaine aldehyde

substrate: Betaine aldehyde


substrate_name: glycolate

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

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

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

substrate: glycolate


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


organism: Amaranthus retroflexus

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


enzyme_display_name: secondary-alcohol oxidase

substrate_name: polyvinyl alcohol

enzyme: secondary-alcohol oxidase

substrate: polyvinyl alcohol


smiles: CCCC(CCC)O


organism: Geotrichum candidum


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


enzyme_display_name: thiamine oxidase

organism: unidentified soil bacterium

substrate_name: thiamine

enzyme: thiamine oxidase

substrate: thiamine


organism: Pseudomonas putida


organism: Manduca sexta

substrate_name: ecdysone

substrate: ecdysone


enzyme_display_name: Glycolate oxidase

organism: Spinacia oleracea

substrate_name: L-lactate

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

enzyme: Glycolate oxidase

substrate: L-lactate


substrate_name: L-mandelate

substrate: L-mandelate


enzyme_display_name: nucleoside oxidase

organism: Stenotrophomonas maltophilia

substrate_name: Inosine

enzyme: nucleoside oxidase

substrate: Inosine


smiles: OO


enzyme_display_name: hydroxyphytanate oxidase

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

enzyme: hydroxyphytanate oxidase


enzyme_display_name: UniProt P56216

organism: Penicillium simplicissimum

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

enzyme: UniProt P56216


enzyme_display_name: alditol oxidase

organism: Streptomyces coelicolor

smiles: CCCC(CO)N

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

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

enzyme: alditol oxidase


smiles: C=CCCO


smiles: CCC(CO)O


smiles: C=CC(CO)O


smiles: CCCC(CO)O


substrate_name: L-arabinose

substrate: L-arabinose


smiles: CCCCC(CO)O


smiles: C(CO)C(CO)O


organism: Ralstonia solanacearum

substrate_name: N-acetyl-beta-D-glucosamine

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

row_label: A3RXB7 / GlcNAc

table_label: Table 1

substrate: N-acetyl-beta-D-glucosamine


substrate_name: D-galactosamine

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

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

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

row_label: A3RXB7 / D-galactosamine

substrate: D-galactosamine


substrate_name: D-galactose

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

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

row_label: A3RXB7 / D-galactose

substrate: D-galactose


enzyme_display_name: 2-Hydroxyacid oxidase 2

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

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

enzyme: 2-Hydroxyacid oxidase 2


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


enzyme_display_name: 2-Hydroxyacid oxidase 1

organism: Homo sapiens

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

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

enzyme: 2-Hydroxyacid oxidase 1


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


enzyme_display_name: Glycolate oxidase 2

organism: Arabidopsis thaliana

substrate_name: (S)-lactate

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

enzyme: Glycolate oxidase 2


substrate_name: glyoxylate

assay_conditions_summary: pH 7; cofactor FMN

substrate: glyoxylate


enzyme_display_name: nucleoside oxidase (H2O2-forming)

organism: Elizabethkingia meningoseptica

enzyme: nucleoside oxidase (H2O2-forming)


substrate_name: guanosine

substrate: guanosine


substrate_name: 6-mercaptopurine arabinoside

substrate: 6-mercaptopurine arabinoside


substrate_name: thymidine

substrate: thymidine


substrate_name: tubercidin

substrate: tubercidin


substrate_name: uridine

substrate: uridine


substrate_name: cytidine

substrate: cytidine


enzyme_display_name: Choline oxidase

organism: Arthrobacter globiformis

substrate_name: choline

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

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

enzyme: Choline oxidase

substrate: choline


substrate_name: betaine aldehyde

substrate: betaine aldehyde


enzyme_display_name: D-mannitol oxidase

organism: Cornu aspersum

smiles: O=O

enzyme: D-mannitol oxidase


substrate_name: D-mannitol

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

substrate: D-mannitol


organism: Limacus flavus


substrate_name: D-arabinitol

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

substrate: D-arabinitol


organism: Arion ater


enzyme_display_name: vanillyl-alcohol oxidase

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

enzyme: vanillyl-alcohol oxidase


substrate_name: p-Cresol

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

substrate: p-Cresol


substrate_name: propylphenol

substrate: propylphenol


substrate_name: Vanillyl alcohol

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

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

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

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

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

substrate: Vanillyl alcohol


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

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

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

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


substrate_name: chavicol

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

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

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

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

substrate: chavicol