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

raw_value_unit_evidence: Table row reports Km 0.27 mM, Kcat 7.35 s^-1, and Kcat/Km 27.66 s^-1*mM^-1.

row_label: malate


enzyme_display_name: quinoprotein glucose dehydrogenase (PQQ, quinone)

organism: Thermus thermophilus

substrate_name: L-Arabinose

source_db: oed

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

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

raw_value_unit_evidence: paper Table 1 cells for wild type / L-Arabinose: kcat=1755 s^-1; Km=0.16 M; kcat/Km=10972 s^-1 M^-1

row_label: wild type / L-Arabinose

table_label: Table 1

data_origin: experimental

substrate: L-Arabinose

status: corrected

source: oed


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

mutation_type: substitution

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

normalized_value_unit_evidence: normalized: kcat=142 s^-1; Km=170 mM; kcat/Km=0.796 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156A / L-Arabinose: kcat=142 s^-1; Km=0.17 M; kcat/Km=796 s^-1 M^-1

row_label: Y156A / L-Arabinose

enzyme: quinoprotein glucose dehydrogenase (PQQ, quinone)


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

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

normalized_value_unit_evidence: normalized: kcat=154 s^-1; Km=140 mM; kcat/Km=1.079 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156K / L-Arabinose: kcat=154 s^-1; Km=0.14 M; kcat/Km=1079 s^-1 M^-1

row_label: Y156K / L-Arabinose


substrate_name: D-Mannose

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

raw_value_unit_evidence: paper Table 1 cells for wild type / D-Mannose: kcat=1627 s^-1; Km=0.13 M; kcat/Km=12518 s^-1 M^-1

row_label: wild type / D-Mannose

substrate: D-Mannose


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

normalized_value_unit_evidence: normalized: kcat=265 s^-1; Km=140 mM; kcat/Km=1.858 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156A / D-Mannose: kcat=265 s^-1; Km=0.14 M; kcat/Km=1858 s^-1 M^-1

row_label: Y156A / D-Mannose


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

normalized_value_unit_evidence: normalized: kcat=261 s^-1; Km=160 mM; kcat/Km=1.61 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156K / D-Mannose: kcat=261 s^-1; Km=0.16 M; kcat/Km=1610 s^-1 M^-1

row_label: Y156K / D-Mannose


substrate_name: D-Glucosamine

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

normalized_value_unit_evidence: normalized: kcat=197 s^-1; Km=20 mM; kcat/Km=12.989 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for wild type / D-Glucosamine: kcat=197 s^-1; Km=0.02 M; kcat/Km=12989 s^-1 M^-1

row_label: wild type / D-Glucosamine

substrate: D-Glucosamine


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

normalized_value_unit_evidence: normalized: kcat=104 s^-1; Km=20 mM; kcat/Km=5.727 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156A / D-Glucosamine: kcat=104 s^-1; Km=0.02 M; kcat/Km=5727 s^-1 M^-1

row_label: Y156A / D-Glucosamine


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

normalized_value_unit_evidence: normalized: kcat=117 s^-1; Km=20 mM; kcat/Km=8.696 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156K / D-Glucosamine: kcat=117 s^-1; Km=0.02 M; kcat/Km=8696 s^-1 M^-1

row_label: Y156K / D-Glucosamine


organism: Pyrobaculum aerophilum

substrate_name: D-galactose

column_label: Table 1, P. aerophilum (pH 8.0), row D-Galactose, columns kcat s^-1, Km M, and kcat/Km s^-1 M^-1: 4.3 +/- 0.11; 0.39 +/- 0.03; 11 +/- 1.1, respectively.

row_label: D-Galactose

table_label: Table 1. Substrate specificity of the P. aerophilum enzyme in comparison with the E. coli enzyme

substrate: D-galactose


substrate_name: D-glucose

column_label: Table 1, P. aerophilum (pH 8.0), row D-Glucose, columns kcat s^-1, Km M, and kcat/Km s^-1 M^-1: 4.1 +/- 0.12; 0.68 +/- 0.06; 6.1 +/- 0.7, respectively.

row_label: D-Glucose

substrate: D-glucose


substrate_name: maltose

column_label: Table 1, P. aerophilum (pH 8.0), row Maltose, columns kcat s^-1, Km M, and kcat/Km s^-1 M^-1: 2.3 +/- 0.10; 0.60 +/- 0.05; 3.9 +/- 0.5, respectively.

row_label: Maltose

substrate: maltose


substrate_name: D-Xylose

column_label: Table 1, P. aerophilum (pH 8.0), row D-Xylose, columns kcat s^-1, Km M, and kcat/Km s^-1 M^-1: 3.2 +/- 0.29; 0.50 +/- 0.04; 6.5 +/- 1.1, respectively.

row_label: D-Xylose

substrate: D-Xylose


column_label: Table 1, P. aerophilum (pH 8.0), row D-Mannose, columns kcat s^-1, Km M, and kcat/Km s^-1 M^-1: 3.1 +/- 0.23; 0.91 +/- 0.07; 3.4 +/- 0.5, respectively.

row_label: D-Mannose


enzyme_display_name: Alcohol dehydrogenase (quinone), dehydrogenase subunit

organism: Gluconobacter oxydans (strain 621H)

substrate_name: ethanol (for ubiquinone reduction activity in active ADH at pH 4.5)

source_db: uniprot

verification_status: unverified

kcat_display: Not reported

kcat_over_km_display: Not reported

smiles: CCO

status: unverified

source: uniprot


enzyme_display_name: Alcohol dehydrogenase (quinone), cytochrome c subunit

substrate: ethanol (for ubiquinone reduction activity in active ADH at pH 4.5)


enzyme_display_name: glucose 1-dehydrogenase (PQQ, quinone)

organism: Escherichia coli

substrate_name: pyrroloquinoline quinone

source_db: brenda

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

enzyme: glucose 1-dehydrogenase (PQQ, quinone)

substrate: pyrroloquinoline quinone

source: brenda


enzyme_display_name: glucose 1-dehydrogenase (FAD, quinone)

organism: Aspergillus flavus

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V149C/G190C with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

enzyme: glucose 1-dehydrogenase (FAD, quinone)


organism: Acinetobacter calcoaceticus

substrate_name: D-xylose

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

assay_conditions_summary: pH 7

substrate: D-xylose


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


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


enzyme_display_name: glycerol-3-phosphate dehydrogenase

organism: Sus scrofa

substrate_name: sn-Glycerol 3-phosphate

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

enzyme: glycerol-3-phosphate dehydrogenase

substrate: sn-Glycerol 3-phosphate


organism: Pseudomonas fluorescens

substrate_name: ubiquinone Q6

substrate: ubiquinone Q6


substrate_name: ubiquinone Q4

substrate: ubiquinone Q4


substrate_name: ubiquinone Q2

substrate: ubiquinone Q2


substrate_name: ubiquinone Q1

substrate: ubiquinone Q1


substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


proof_lines: pH 6.0, 25°C, reaction with 2,6-dichlorophenolindophenol


substrate_name: N,N,N,N-tetramethyl-o-phenylenediamine

substrate: N,N,N,N-tetramethyl-o-phenylenediamine


substrate_name: ferricyanide

substrate: ferricyanide


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

normalized_value_unit_evidence: normalized: kcat=160 s^-1; Km=380 mM; kcat/Km=0.417 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156A / D-galactose: kcat=160 s^-1; Km=0.38 M; kcat/Km=417 s^-1 M^-1

row_label: Y156A / D-galactose


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

normalized_value_unit_evidence: normalized: kcat=193 s^-1; Km=200 mM; kcat/Km=0.952 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156K / D-galactose: kcat=193 s^-1; Km=0.2 M; kcat/Km=952 s^-1 M^-1

row_label: Y156K / D-galactose


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

normalized_value_unit_evidence: normalized: kcat=1054 s^-1; Km=210 mM; kcat/Km=5.021 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for wild type / D-glucose: kcat=1054 s^-1; Km=0.21 M; kcat/Km=5021 s^-1 M^-1

row_label: wild type / D-glucose


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

normalized_value_unit_evidence: normalized: kcat=339 s^-1; Km=470 mM; kcat/Km=0.719 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156A / D-glucose: kcat=339 s^-1; Km=0.47 M; kcat/Km=719 s^-1 M^-1

row_label: Y156A / D-glucose


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

normalized_value_unit_evidence: normalized: kcat=316 s^-1; Km=250 mM; kcat/Km=1.287 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156K / D-glucose: kcat=316 s^-1; Km=0.25 M; kcat/Km=1287 s^-1 M^-1

row_label: Y156K / D-glucose


substrate_name: D-glucose 6-phosphate

column_label: Table 1; row_label: wild type / D-glucose 6-phosphate; columns kcat (s^-1), Km (M), kcat/Km (s^-1 M^-1)

normalized_value_unit_evidence: normalized: kcat=192 s^-1; Km=80 mM; kcat/Km=2.543 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for wild type / D-glucose 6-phosphate: kcat=192 s^-1; Km=0.08 M; kcat/Km=2543 s^-1 M^-1

row_label: wild type / D-glucose 6-phosphate

substrate: D-glucose 6-phosphate


substrate_name: D-ribose

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

normalized_value_unit_evidence: normalized: kcat=260 s^-1; Km=130 mM; kcat/Km=2.062 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for wild type / D-ribose: kcat=260 s^-1; Km=0.13 M; kcat/Km=2062 s^-1 M^-1

row_label: wild type / D-ribose

substrate: D-ribose


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

normalized_value_unit_evidence: normalized: kcat=181 s^-1; Km=70 mM; kcat/Km=2.724 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156A / D-ribose: kcat=181 s^-1; Km=0.07 M; kcat/Km=2724 s^-1 M^-1

row_label: Y156A / D-ribose


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

normalized_value_unit_evidence: normalized: kcat=715 s^-1; Km=440 mM; kcat/Km=1.631 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for Y156K / D-ribose: kcat=715 s^-1; Km=0.44 M; kcat/Km=1631 s^-1 M^-1

row_label: Y156K / D-ribose


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

normalized_value_unit_evidence: normalized: kcat=1022 s^-1; Km=170 mM; kcat/Km=6.012 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for wild type / maltose: kcat=1022 s^-1; Km=0.17 M; kcat/Km=6012 s^-1 M^-1

row_label: wild type / maltose


organism: Sorangium cellulosum

proof_lines: mutant enzyme Q219K/F220C, in 42 mM sodium phosphate buffer pH 7.5 at 37°C


proof_lines: mutant enzyme Q126E, in 42 mM sodium phosphate buffer pH 7.5 at 37°C


proof_lines: mutant enzyme Q219N/F220K, in 42 mM sodium phosphate buffer pH 7.5 at 37°C


proof_lines: mutant enzyme Q219E/F220E, in 42 mM sodium phosphate buffer pH 7.5 at 37°C


proof_lines: mutant enzyme Q126R, in 42 mM sodium phosphate buffer pH 7.5 at 37°C


proof_lines: mutant enzyme Q126S, in 42 mM sodium phosphate buffer pH 7.5 at 37°C


proof_lines: mutant enzyme Q219K/F220K, in 42 mM sodium phosphate buffer pH 7.5 at 37°C


proof_lines: wild type enzyme, in 42 mM sodium phosphate buffer pH 7.5 at 37°C


substrate_name: D-galactose

substrate: D-galactose


substrate_name: allose

substrate: allose


substrate_name: maltose

substrate: maltose


substrate_name: N-methylphenazonium methyl sulfate

proof_lines:
pH 8.5, reaction with D-galactose
membrane-bound enzyme form
pH 8.5, reaction with D-xylose

substrate: N-methylphenazonium methyl sulfate


substrate_name: L-arabinose

proof_lines: pH 8.5, reaction with N-ethylphenazonium ethyl sulfate as electron acceptor

proof_lines: pH 8.5, reaction with N-methylphenazonium methyl sulfate as electron acceptor

substrate: L-arabinose


substrate_name: N-ethylphenazonium ethyl sulfate

proof_lines:
pH 8.5, reaction with D-xylose
pH 8.5, reaction with D-glucose
pH 8.5, reaction with D-fucose

substrate: N-ethylphenazonium ethyl sulfate


substrate_name: D-fucose

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

substrate: D-fucose


substrate_name: D-melibiose

substrate: D-melibiose


substrate_name: L-Lyxose

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

substrate: L-Lyxose


substrate_name: D-glucose

substrate: D-glucose


substrate_name: pyrroliquinoline quinone

substrate: pyrroliquinoline quinone


substrate_name: pyrroloquinoline quinone

proof_lines: C-terminal periplasmic domain of glucose dehydrogenase

substrate: pyrroloquinoline quinone


substrate_name: ubiquinone Q2

substrate: ubiquinone Q2


substrate_name: coenzyme Q2

substrate: coenzyme Q2


substrate_name: coenzyme Q10

substrate: coenzyme Q10


substrate_name: coenzyme Q6

substrate: coenzyme Q6


substrate_name: coenzyme Q0

substrate: coenzyme Q0


substrate_name: sn-glycerol 3-phosphate

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

proof_lines: with 2,6-dichloroindophenol, phenazine methosulfate, coenzyme Q0, coenzyme Q1, coenzyme Q2 or coenzyme Q6 as electron acceptor

substrate: sn-glycerol 3-phosphate


proof_lines: recombinant chimeric mutant enzyme, pH 7.0

proof_lines: recombinant triple mutant enzyme, pH 7.0, 25°C


proof_lines:
recombinant Arg-tagged enzyme, pH 7.0
recombinant tagged enzyme, pH 7.0, 25°C


organism: Erwinia sp.


substrate_name: maltotriose

substrate: maltotriose


substrate_name: maltose

substrate: maltose


substrate_name: ubiquinone Q6

substrate: ubiquinone Q6


substrate_name: ubiquinone Q9

substrate: ubiquinone Q9


proof_lines:
membrane-bound enzyme form
soluble enzyme form


substrate_name: ubiquinone Q1

substrate: ubiquinone Q1


organism: Vibrio alginolyticus

substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


substrate_name: ferricyanide

substrate: ferricyanide


proof_lines: with phenazine methosulfate as electron acceptor


enzyme_display_name: cholesterol oxidase

organism: Streptomyces sp.

substrate_name: cholesterol

enzyme: cholesterol oxidase

substrate: cholesterol


enzyme_display_name: (S)-2-hydroxyglutarate dehydrogenase

organism: Homo sapiens

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

assay_conditions_summary: cofactor FAD

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

enzyme: (S)-2-hydroxyglutarate dehydrogenase


enzyme_display_name: fructose 5-dehydrogenase

organism: Gluconobacter oxydans

substrate_name: D-fructose

enzyme: fructose 5-dehydrogenase

substrate: D-fructose


enzyme_display_name: 4-hydroxybenzoyl-CoA reductase

organism: Pseudomonas sp.

assay_conditions_summary: cofactor CoA

enzyme: 4-hydroxybenzoyl-CoA reductase


organism: Gluconobacter cerinus

proof_lines: in presence of 2,6-dichlorophenolindophenol, 67 mM, pH 5.5, 15°C


enzyme_display_name: D-lactate dehydrogenase (quinone)

organism: Pseudomonas putida KT2440

substrate_name: D-glycerate

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

assay_conditions_summary: pH 7.4; cofactor FAD

proof_lines: isolated FAD-containing dehydrogenase domain, pH 7.4. 30°C

enzyme: D-lactate dehydrogenase (quinone)

substrate: D-glycerate


substrate_name: (S)-lactate

substrate: (S)-lactate


proof_lines: cosubstrate (R)-lactate, isolated FAD-containing dehydrogenase domain, pH 7.4, 30°C


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


organism: Arabidopsis thaliana


enzyme_display_name: alcohol dehydrogenase (azurin)

organism: Pseudomonas putida

substrate_name: Oxidized azurin; 1-Butanol

verification_status: verified

km_display: Not reported

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

assay_conditions_summary: pH 8

column_label: Table 1, row azurin (Pp); 30 mM Tris-HCl (pH 8.0), columns kcat (s^-1), Vmax (units/mg).

raw_value_unit_evidence: Table 1 printed values: kcat 71.8; vmax 62.5 units mg^-1.

row_label: azurin (Pp); 30 mM Tris-HCl (pH 8.0)

enzyme: alcohol dehydrogenase (azurin)

substrate: Oxidized azurin; 1-Butanol

status: verified


column_label: Table 1, row azurin (Pp); 30 mM Tris-HCl and 0.1 M KCl, columns Km (uM), Vmax (units/mg).

raw_value_unit_evidence: Table 1 printed values: km 51 uM; vmax 52.6 units mg^-1.


column_label: Table 1, row azurin (Pp); 30 mM Tris-HCl and 0.5 M KCl, columns kcat (s^-1), Km (uM), Vmax (units/mg).

raw_value_unit_evidence: Table 1 printed values: kcat 48.0; km 25 uM; vmax 41.7 units mg^-1.


column_label: Table 1, row azurin (Pa); 30 mM Tris-HCl (pH 8.0), columns kcat (s^-1), Km (uM), Vmax (units/mg).

raw_value_unit_evidence: Table 1 printed values: kcat 25.6; km 202 uM; vmax 22.3 units mg^-1.

row_label: azurin (Pa); 30 mM Tris-HCl (pH 8.0)


substrate_name: ADH IIB; Oxidized azurin

substrate: ADH IIB; Oxidized azurin


substrate_name: iodonitrotetrazolium

substrate: iodonitrotetrazolium


enzyme_display_name: D-2-hydroxyacid dehydrogenase (quinone)

enzyme: D-2-hydroxyacid dehydrogenase (quinone)


substrate_name: L-lactate

substrate: L-lactate


substrate_name: D-lactate

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

substrate: D-lactate


enzyme_display_name: F420H2:quinone oxidoreductase

organism: Archaeoglobus fulgidus

substrate_name: reduced coenzyme F420

enzyme: F420H2:quinone oxidoreductase

substrate: reduced coenzyme F420


organism: Methanofollis liminatans

smiles: CCCC(=O)C


smiles: CCC(=O)C


substrate_name: Cyclopentanone

substrate: Cyclopentanone


substrate_name: Cyclopentanol

substrate: Cyclopentanol


smiles: CCCC(C)O


smiles: CCC(C)O


smiles: CC(C)O


substrate_name: oxidized coenzyme F420

substrate: oxidized coenzyme F420


substrate_name: propanone

smiles: CC(=O)C

substrate: propanone


organism: Methanoculleus thermophilus


enzyme_display_name: choline dehydrogenase

organism: Canis lupus familiaris

substrate_name: choline

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

enzyme: choline dehydrogenase

substrate: choline


organism: Methanosarcina mazei G?1


organism: Gluconobacter sp.

proof_lines:
slow reaction phase
fast reaction phase


sequence_source: multiple

assay_conditions_summary: pH 5

proof_lines:
slow reaction phase
fast reaction phase
at pH 5.0 and 37°C

source_databases_merged: brenda uniprot


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate_name: FPR (at pH 8.5 and 25 degrees Celsius)

proof_lines: kcat is 12.7 min(-1) for epimerase activity with FPR as substrate (at pH 8.5 and 25 degrees Celsius).

substrate: FPR (at pH 8.5 and 25 degrees Celsius)


organism: Rhodococcus jostii

substrate_name: D-glucose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K197N with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

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

substrate: D-glucose 6-phosphate


enzyme_display_name: Quinohemoprotein alcohol dehydrogenase

organism: Comamonas testosteroni

substrate_name: ethanol

smiles: CCO

enzyme: Quinohemoprotein alcohol dehydrogenase

substrate: ethanol


organism: Mycobacterium tuberculosis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E109Q with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines:
wild-type and mutant FGD
variant panel including H40A and E109Q
reduced catalytic efficiencies


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q0RVH7 and applied mutation signature H40A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Apparent Steady-State Kinetic Parameters for Wild-Type FGD and Its Variants), printed line 'H40A', G6P axis; column 'G6P kcat(app) (s-1)' = 0.0016 +/- 0.0001; column 'G6P Km(app) (uM)' = 27 +/- 5; column 'G6P kcat/Km (M-1 s-1)' = (6.0 +/- 1.0) x 10^1. The value printed after the plus/minus sign in each cell is the printed uncertainty and is not an exported metric; the F420 columns of the same printed line carry the other measurement axis.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.0016 in a column headed G6P kcat(app) (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.0016 s^(-1). Km: printed Table 3 cell 27 in a column headed G6P Km(app) (uM); 1 uM is 0.001 mM, so 27 / 1000 = 0.027 mM. kcat/Km: printed Table 3 cell 6.0 x 10^1 in a column headed G6P kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 60.0 / 1000 = 0.06 s^(-1)*mM^(-1). The exported values are kcat 0.0016 s^(-1), Km 0.027 mM and kcat_over_km 0.05925925925925926 s^(-1)*mM^(-1), and the quotient of the two printed component cells is 0.0016 / 0.027 = 0.05925925925925926 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, printed line 'H40A', G6P columns: kcat = 0.0016 s-1; Km = 27 uM; printed kcat/Km = 6.0 x 10^1 in a column headed G6P kcat/Km (M-1 s-1).

table_label: Table 3: Apparent Steady-State Kinetic Parameters for Wild-Type FGD and Its Variants (Biochemistry 2016, 55(39):5566-5577). Printed column heads: FGD; G6P kcat(app) (s-1); F420 kcat(app) (s-1); G6P Km(app) (uM); F420 Km(app) (uM); G6P kcat/Km (M-1 s-1); F420 kcat/Km (M-1 s-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q0RVH7 and applied mutation signature W44A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Apparent Steady-State Kinetic Parameters for Wild-Type FGD and Its Variants), printed line 'W44A', G6P axis; column 'G6P kcat(app) (s-1)' = 0.0012 +/- 0.0003; column 'G6P Km(app) (uM)' = 280 +/- 40; column 'G6P kcat/Km (M-1 s-1)' = 4.0 +/- 1.0. The value printed after the plus/minus sign in each cell is the printed uncertainty and is not an exported metric; the F420 columns of the same printed line carry the other measurement axis.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.0012 in a column headed G6P kcat(app) (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.0012 s^(-1). Km: printed Table 3 cell 280 in a column headed G6P Km(app) (uM); 1 uM is 0.001 mM, so 280 / 1000 = 0.28 mM. kcat/Km: printed Table 3 cell 4.0 in a column headed G6P kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.0 / 1000 = 0.004 s^(-1)*mM^(-1). The exported values are kcat 0.0012 s^(-1), Km 0.28 mM and kcat_over_km 0.004285714285714285 s^(-1)*mM^(-1), and the quotient of the two printed component cells is 0.0012 / 0.28 = 0.004285714285714286 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, printed line 'W44A', G6P columns: kcat = 0.0012 s-1; Km = 280 uM; printed kcat/Km = 4.0 in a column headed G6P kcat/Km (M-1 s-1).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W44F with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q0RVH7 and applied mutation signature W44Y with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Apparent Steady-State Kinetic Parameters for Wild-Type FGD and Its Variants), printed line 'W44Y', G6P axis; column 'G6P kcat(app) (s-1)' = 0.041 +/- 0.001; column 'G6P Km(app) (uM)' = 170 +/- 20; column 'G6P kcat/Km (M-1 s-1)' = (2.0 +/- 0.2) x 10^2. The value printed after the plus/minus sign in each cell is the printed uncertainty and is not an exported metric; the F420 columns of the same printed line carry the other measurement axis.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.041 in a column headed G6P kcat(app) (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.041 s^(-1). Km: printed Table 3 cell 170 in a column headed G6P Km(app) (uM); 1 uM is 0.001 mM, so 170 / 1000 = 0.17 mM. kcat/Km: printed Table 3 cell 2.0 x 10^2 in a column headed G6P kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 200.0 / 1000 = 0.2 s^(-1)*mM^(-1). The exported values are kcat 0.041 s^(-1), Km 0.17 mM and kcat_over_km 0.2411764705882353 s^(-1)*mM^(-1), and the quotient of the two printed component cells is 0.041 / 0.17 = 0.2411764705882353 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, printed line 'W44Y', G6P columns: kcat = 0.041 s-1; Km = 170 uM; printed kcat/Km = 2.0 x 10^2 in a column headed G6P kcat/Km (M-1 s-1).


column_label: Table 3 (Apparent Steady-State Kinetic Parameters for Wild-Type FGD and Its Variants), printed line 'wild-type', G6P axis; column 'G6P kcat(app) (s-1)' = 1.4 +/- 0.1; column 'G6P Km(app) (uM)' = 22 +/- 2; column 'G6P kcat/Km (M-1 s-1)' = (6.0 +/- 0.5) x 10^4. The value printed after the plus/minus sign in each cell is the printed uncertainty and is not an exported metric; the F420 columns of the same printed line carry the other measurement axis.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.4 in a column headed G6P kcat(app) (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 1.4 s^(-1). Km: printed Table 3 cell 22 in a column headed G6P Km(app) (uM); 1 uM is 0.001 mM, so 22 / 1000 = 0.022 mM. kcat/Km: printed Table 3 cell 6.0 x 10^4 in a column headed G6P kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 60000.0 / 1000 = 60.0 s^(-1)*mM^(-1). The exported values are kcat 1.4 s^(-1), Km 0.022 mM and kcat_over_km 63.63636363636363 s^(-1)*mM^(-1), and the quotient of the two printed component cells is 1.4 / 0.022 = 63.63636363636363 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, printed line 'wild-type', G6P columns: kcat = 1.4 s-1; Km = 22 uM; printed kcat/Km = 6.0 x 10^4 in a column headed G6P kcat/Km (M-1 s-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q0RVH7 and applied mutation signature E109Q with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Apparent Steady-State Kinetic Parameters for Wild-Type FGD and Its Variants), printed line 'E109Q', F420 axis; column 'F420 kcat(app) (s-1)' = 0.020 +/- 0.003; column 'F420 Km(app) (uM)' = 5.6 +/- 1.0; column 'F420 kcat/Km (M-1 s-1)' = (4.0 +/- 0.8) x 10^3. The value printed after the plus/minus sign in each cell is the printed uncertainty and is not an exported metric; the G6P columns of the same printed line carry the other measurement axis.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.020 in a column headed F420 kcat(app) (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.02 s^(-1). Km: printed Table 3 cell 5.6 in a column headed F420 Km(app) (uM); 1 uM is 0.001 mM, so 5.6 / 1000 = 0.0056 mM. kcat/Km: printed Table 3 cell 4.0 x 10^3 in a column headed F420 kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4000.0 / 1000 = 4.0 s^(-1)*mM^(-1). The exported values are kcat 0.02 s^(-1), Km 0.0056 mM and kcat_over_km 3.5714285714285716 s^(-1)*mM^(-1), and the quotient of the two printed component cells is 0.020 / 0.0056 = 3.5714285714285716 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, printed line 'E109Q', F420 columns: kcat = 0.020 s-1; Km = 5.6 uM; printed kcat/Km = 4.0 x 10^3 in a column headed F420 kcat/Km (M-1 s-1).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H40A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


column_label: Table 3 (Apparent Steady-State Kinetic Parameters for Wild-Type FGD and Its Variants), printed line 'W44A', F420 axis; column 'F420 kcat(app) (s-1)' = 0.0010 +/- 0.0003; column 'F420 Km(app) (uM)' = 0.9 +/- 0.2; column 'F420 kcat/Km (M-1 s-1)' = (1.0 +/- 0.5) x 10^3. The value printed after the plus/minus sign in each cell is the printed uncertainty and is not an exported metric; the G6P columns of the same printed line carry the other measurement axis.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.0010 in a column headed F420 kcat(app) (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.001 s^(-1). Km: printed Table 3 cell 0.9 in a column headed F420 Km(app) (uM); 1 uM is 0.001 mM, so 0.9 / 1000 = 0.0009 mM. kcat/Km: printed Table 3 cell 1.0 x 10^3 in a column headed F420 kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1000.0 / 1000 = 1.0 s^(-1)*mM^(-1). The exported values are kcat 0.001 s^(-1), Km 0.0009 mM and kcat_over_km 1.1111111111111112 s^(-1)*mM^(-1), and the quotient of the two printed component cells is 0.0010 / 0.0009 = 1.1111111111111112 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, printed line 'W44A', F420 columns: kcat = 0.0010 s-1; Km = 0.9 uM; printed kcat/Km = 1.0 x 10^3 in a column headed F420 kcat/Km (M-1 s-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q0RVH7 and applied mutation signature W44F with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Apparent Steady-State Kinetic Parameters for Wild-Type FGD and Its Variants), printed line 'W44F', F420 axis; column 'F420 kcat(app) (s-1)' = 3.2 +/- 0.3; column 'F420 Km(app) (uM)' = 5.4 +/- 1.0; column 'F420 kcat/Km (M-1 s-1)' = (6.0 +/- 1.0) x 10^5. The value printed after the plus/minus sign in each cell is the printed uncertainty and is not an exported metric; the G6P columns of the same printed line carry the other measurement axis.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.2 in a column headed F420 kcat(app) (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 3.2 s^(-1). Km: printed Table 3 cell 5.4 in a column headed F420 Km(app) (uM); 1 uM is 0.001 mM, so 5.4 / 1000 = 0.0054 mM. kcat/Km: printed Table 3 cell 6.0 x 10^5 in a column headed F420 kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 600000.0 / 1000 = 600.0 s^(-1)*mM^(-1). The exported values are kcat 3.2 s^(-1), Km 0.0054 mM and kcat_over_km 592.5925925925926 s^(-1)*mM^(-1), and the quotient of the two printed component cells is 3.2 / 0.0054 = 592.5925925925926 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, printed line 'W44F', F420 columns: kcat = 3.2 s-1; Km = 5.4 uM; printed kcat/Km = 6.0 x 10^5 in a column headed F420 kcat/Km (M-1 s-1).


substrate_name: benzyl alcohol

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

substrate: benzyl alcohol


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

smiles: CCCCO

column_label: table label: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); row label: quinohaemoprotein alcohol dehydrogenase / butan-1-ol; column label: Km (mM); raw value: 0.005; raw unit: mM; normalized value: 0.005; normalized unit: mM; assay condition: Holoenzyme assay after apoenzyme plus PQQ reconstitution; 20 mM Tris-HCl pH 7.7, 3 mM CaCl2, 0.15 mM Wurster Blue electron acceptor, substrate varied for Lineweaver-Burk apparent Km.; captured paper segment: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); quinohaemoprotein alcohol dehydrogenase / butan-1-ol; Km 0.005 mM.

normalized_value_unit_evidence: Km normalized value: 0.005; normalized unit: mM

raw_value_unit_evidence: Km raw value: 0.005; raw unit: mM


smiles: CCCCCO

column_label: table label: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); row label: quinohaemoprotein alcohol dehydrogenase / pentan-1-ol; column label: Km (mM); raw value: 0.005; raw unit: mM; normalized value: 0.005; normalized unit: mM; assay condition: Holoenzyme assay after apoenzyme plus PQQ reconstitution; 20 mM Tris-HCl pH 7.7, 3 mM CaCl2, 0.15 mM Wurster Blue electron acceptor, substrate varied for Lineweaver-Burk apparent Km.; captured paper segment: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); quinohaemoprotein alcohol dehydrogenase / pentan-1-ol; Km 0.005 mM.


smiles: CCCCCCCCO

column_label: table label: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); row label: quinohaemoprotein alcohol dehydrogenase / octan-1-ol; column label: Km (mM); raw value: 0.005; raw unit: mM; normalized value: 0.005; normalized unit: mM; assay condition: Holoenzyme assay after apoenzyme plus PQQ reconstitution; 20 mM Tris-HCl pH 7.7, 3 mM CaCl2, 0.15 mM Wurster Blue electron acceptor, substrate varied for Lineweaver-Burk apparent Km.; captured paper segment: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); quinohaemoprotein alcohol dehydrogenase / octan-1-ol; Km 0.005 mM.


substrate_name: octanal

smiles: CCCCCCCC=O

column_label: table label: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); row label: quinohaemoprotein alcohol dehydrogenase / octanal; column label: Km (mM); raw value: 0.04; raw unit: mM; normalized value: 0.04; normalized unit: mM; assay condition: Holoenzyme assay after apoenzyme plus PQQ reconstitution; 20 mM Tris-HCl pH 7.7, 3 mM CaCl2, 0.15 mM Wurster Blue electron acceptor, substrate varied for Lineweaver-Burk apparent Km.; captured paper segment: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); quinohaemoprotein alcohol dehydrogenase / octanal; Km 0.04 mM.

normalized_value_unit_evidence: Km normalized value: 0.04; normalized unit: mM

raw_value_unit_evidence: Km raw value: 0.04; raw unit: mM

substrate: octanal


smiles: CCCO

column_label: table label: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); row label: quinohaemoprotein alcohol dehydrogenase / propan-1-ol; column label: Km (mM); raw value: 0.06; raw unit: mM; normalized value: 0.06; normalized unit: mM; assay condition: Holoenzyme assay after apoenzyme plus PQQ reconstitution; 20 mM Tris-HCl pH 7.7, 3 mM CaCl2, 0.15 mM Wurster Blue electron acceptor, substrate varied for Lineweaver-Burk apparent Km.; captured paper segment: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); quinohaemoprotein alcohol dehydrogenase / propan-1-ol; Km 0.06 mM.

normalized_value_unit_evidence: Km normalized value: 0.06; normalized unit: mM

raw_value_unit_evidence: Km raw value: 0.06; raw unit: mM


substrate_name: butyraldehyde

smiles: CCCC=O

column_label: table label: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); row label: quinohaemoprotein alcohol dehydrogenase / butyraldehyde; column label: Km (mM); raw value: 0.1; raw unit: mM; normalized value: 0.1; normalized unit: mM; assay condition: Holoenzyme assay after apoenzyme plus PQQ reconstitution; 20 mM Tris-HCl pH 7.7, 3 mM CaCl2, 0.15 mM Wurster Blue electron acceptor, substrate varied for Lineweaver-Burk apparent Km.; captured paper segment: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); quinohaemoprotein alcohol dehydrogenase / butyraldehyde; Km 0.1 mM.

normalized_value_unit_evidence: Km normalized value: 0.1; normalized unit: mM

raw_value_unit_evidence: Km raw value: 0.1; raw unit: mM

substrate: butyraldehyde


smiles: C(CCCO)CCN

column_label: table label: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); row label: quinohaemoprotein alcohol dehydrogenase / 6-aminohexan-1-ol; column label: Km (mM); raw value: 0.2; raw unit: mM; normalized value: 0.2; normalized unit: mM; assay condition: Holoenzyme assay after apoenzyme plus PQQ reconstitution; 20 mM Tris-HCl pH 7.7, 3 mM CaCl2, 0.15 mM Wurster Blue electron acceptor, substrate varied for Lineweaver-Burk apparent Km.; captured paper segment: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); quinohaemoprotein alcohol dehydrogenase / 6-aminohexan-1-ol; Km 0.2 mM.

normalized_value_unit_evidence: Km normalized value: 0.2; normalized unit: mM

raw_value_unit_evidence: Km raw value: 0.2; raw unit: mM


substrate_name: acetaldehyde

smiles: CC=O

column_label: table label: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); row label: quinohaemoprotein alcohol dehydrogenase / acetaldehyde; column label: Km (mM); raw value: 0.9; raw unit: mM; normalized value: 0.9; normalized unit: mM; assay condition: Holoenzyme assay after apoenzyme plus PQQ reconstitution; 20 mM Tris-HCl pH 7.7, 3 mM CaCl2, 0.15 mM Wurster Blue electron acceptor, substrate varied for Lineweaver-Burk apparent Km.; captured paper segment: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); quinohaemoprotein alcohol dehydrogenase / acetaldehyde; Km 0.9 mM.

normalized_value_unit_evidence: Km normalized value: 0.9; normalized unit: mM

raw_value_unit_evidence: Km raw value: 0.9; raw unit: mM

substrate: acetaldehyde


substrate_name: formaldehyde

smiles: C=O

column_label: table label: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); row label: quinohaemoprotein alcohol dehydrogenase / formaldehyde; column label: Km (mM); raw value: 3; raw unit: mM; normalized value: 3; normalized unit: mM; assay condition: Holoenzyme assay after apoenzyme plus PQQ reconstitution; 20 mM Tris-HCl pH 7.7, 3 mM CaCl2, 0.15 mM Wurster Blue electron acceptor, substrate varied for Lineweaver-Burk apparent Km.; captured paper segment: Table 2 (Substrate specificity of quinohaemoprotein alcohol dehydrogenase); quinohaemoprotein alcohol dehydrogenase / formaldehyde; Km 3 mM.

normalized_value_unit_evidence: Km normalized value: 3; normalized unit: mM

raw_value_unit_evidence: Km raw value: 3; raw unit: mM

substrate: formaldehyde


enzyme_display_name: Oxygen-dependent choline dehydrogenase

organism: Escherichia coli (strain K12)

substrate_name: NAD (at pH 7.5 and 37 degrees Celsius)

enzyme: Oxygen-dependent choline dehydrogenase

substrate: NAD (at pH 7.5 and 37 degrees Celsius)


substrate_name: glycine betaine aldehyde (at pH 7.5 and 37 degrees Celsius)

column_label: Prose in Localization and properties of enzymes: apparent Km values for choline and glycine betaine aldehyde were 1.5 and 1.6 mM, respectively.

raw_value_unit_evidence: Km raw_value=1.6 raw_unit=mM raw_cell=1.6

row_label: glycine betaine aldehyde / membrane-bound choline dehydrogenase

table_label: Prose kinetic constants for membrane-bound choline dehydrogenase


substrate_name: NADP (at pH 7.5 and 37 degrees Celsius)

substrate: NADP (at pH 7.5 and 37 degrees Celsius)


substrate_name: choline (at pH 7.5 and 37 degrees Celsius)

column_label: Prose results p. 852; row label: membrane-bound O2-dependent/electron-transfer-linked choline dehydrogenase; substrate column: choline; metric: apparent Km; raw value = 1.5 mM; normalized Km=1.5 mM; pH optimum 7.5 in sodium phosphate; Table 2 context identifies the membrane fraction/toluene-treated-cell choline dehydrogenase activity.

normalized_value_unit_evidence: normalized: Km=1.5 mM

raw_value_unit_evidence: p. 852 prose: apparent Km values for choline and glycine betaine aldehyde were 1.5 and 1.6 mM, respectively.

row_label: Membrane-bound O2-dependent choline dehydrogenase (BetA/P17444-like sequence); substrate choline; metric column: apparent Km

table_label: Prose results, journal p. 852: localization and properties of enzymes; Table 2 fraction/activity context


substrate_name: Hexacyanoferrate(III)

proof_lines:
ADH IIB
azurin
Pseudomonas putida HK5

substrate: Hexacyanoferrate(III)


enzyme_display_name: Quinohemoprotein alcohol dehydrogenase ADH IIB


smiles: CC(CO)O

enzyme: Quinohemoprotein alcohol dehydrogenase ADH IIB


substrate_name: potassium ferricyanide (in the presence of 30 mM Tris-HCl pH 8.0 and 0.1 M KCl)


substrate_name: oxidized coenzyme F420

column_label: Table 3 (Apparent Steady-State Kinetic Parameters for Wild-Type FGD and Its Variants), printed line 'W44Y', F420 axis; column 'F420 kcat(app) (s-1)' = 0.06 +/- 0.01; column 'F420 Km(app) (uM)' = 4.2 +/- 0.8; column 'F420 kcat/Km (M-1 s-1)' = (2.0 +/- 0.4) x 10^4. The value printed after the plus/minus sign in each cell is the printed uncertainty and is not an exported metric; the G6P columns of the same printed line carry the other measurement axis.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.06 in a column headed F420 kcat(app) (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.06 s^(-1). Km: printed Table 3 cell 4.2 in a column headed F420 Km(app) (uM); 1 uM is 0.001 mM, so 4.2 / 1000 = 0.0042 mM. kcat/Km: printed Table 3 cell 2.0 x 10^4 in a column headed F420 kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 20000.0 / 1000 = 20.0 s^(-1)*mM^(-1). The exported values are kcat 0.06 s^(-1), Km 0.0042 mM and kcat_over_km 14.285714285714286 s^(-1)*mM^(-1), and the quotient of the two printed component cells is 0.06 / 0.0042 = 14.285714285714286 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, printed line 'W44Y', F420 columns: kcat = 0.06 s-1; Km = 4.2 uM; printed kcat/Km = 2.0 x 10^4 in a column headed F420 kcat/Km (M-1 s-1).


column_label: Table 3 (Apparent Steady-State Kinetic Parameters for Wild-Type FGD and Its Variants), printed line 'wild-type', F420 axis; column 'F420 kcat(app) (s-1)' = 1.4 +/- 0.3; column 'F420 Km(app) (uM)' = 2.6 +/- 0.3; column 'F420 kcat/Km (M-1 s-1)' = (6.0 +/- 1.0) x 10^5. The value printed after the plus/minus sign in each cell is the printed uncertainty and is not an exported metric; the G6P columns of the same printed line carry the other measurement axis.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.4 in a column headed F420 kcat(app) (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 1.4 s^(-1). Km: printed Table 3 cell 2.6 in a column headed F420 Km(app) (uM); 1 uM is 0.001 mM, so 2.6 / 1000 = 0.0026 mM. kcat/Km: printed Table 3 cell 6.0 x 10^5 in a column headed F420 kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 600000.0 / 1000 = 600.0 s^(-1)*mM^(-1). The exported values are kcat 1.4 s^(-1), Km 0.0026 mM and kcat_over_km 538.4615384615385 s^(-1)*mM^(-1), and the quotient of the two printed component cells is 1.4 / 0.0026 = 538.4615384615385 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, printed line 'wild-type', F420 columns: kcat = 1.4 s-1; Km = 2.6 uM; printed kcat/Km = 6.0 x 10^5 in a column headed F420 kcat/Km (M-1 s-1).


enzyme_display_name: 1-butanol dehydrogenase (quinone)

organism: Thauera butanivorans

column_label: PMC full text reports BOH high affinity toward 1-butanol with Km = 1.7 +/- 0.2 microM; this is the row-level Km evidence for 1-butanol.

normalized_value_unit_evidence: Km 1.7 microM = 0.0017 mM

raw_value_unit_evidence: 1-butanol Km 1.7 +/- 0.2 microM

table_label: PMC full-text abstract and BOH kinetic constants results prose for PMID 12142403

enzyme: 1-butanol dehydrogenase (quinone)


substrate_name: Butyraldehyde

column_label: PMC full text reports BOH also oxidized butyraldehyde and 2-butanol with Km values of 369 +/- 85 microM and 662 +/- 98 microM, respectively; butyraldehyde maps to the first value.

normalized_value_unit_evidence: Km 369 microM = 0.369 mM

raw_value_unit_evidence: butyraldehyde Km 369 +/- 85 microM

row_label: butyraldehyde

substrate: Butyraldehyde


column_label: PMC full text reports BOH also oxidized butyraldehyde and 2-butanol with Km values of 369 +/- 85 microM and 662 +/- 98 microM, respectively; 2-butanol maps to the second value.

normalized_value_unit_evidence: Km 662 microM = 0.662 mM

raw_value_unit_evidence: 2-butanol Km 662 +/- 98 microM


column_label: metric: kcat; table label: Table 3 (Fe-S d-iLDH kinetics with different electron acceptors); row label: Fe-S d-iLDH / MTT electron acceptor; column label: kcat (s^-1), Fe-S d-iLDH; raw value: 128 +/- 5.7; raw unit: s^-1; normalized value: 128; normalized unit: s^-1; assay condition: 30 C assay in 1 ml 50 mM Tris-HCl pH 7.4 with 1.0 mM D-lactate as substrate; electron acceptor ranges: MTT 0.003-0.25 mM, coenzyme Q10 0.003-0.03 mM, cytochrome c 0.003-0.10 mM.; captured paper segment: Table 3 (Fe-S d-iLDH kinetics with different electron acceptors) | Fe-S d-iLDH / MTT electron acceptor | kcat (s^-1), Fe-S d-iLDH | 128 +/- 5.7 s^-1 || metric: kcat_over_km; table label: Table 3 (Fe-S d-iLDH kinetics with different electron acceptors); row label: Fe-S d-iLDH / MTT electron acceptor; column label: derived kcat/Km from Fe-S d-iLDH kcat and Km cells; raw value: 128 / 48; raw unit: s^-1 per microM; normalized value: 2666.666666666666666666666667; normalized unit: s^-1 mM^-1; assay condition: 30 C assay in 1 ml 50 mM Tris-HCl pH 7.4 with 1.0 mM D-lactate as substrate; electron acceptor ranges: MTT 0.003-0.25 mM, coenzyme Q10 0.003-0.03 mM, cytochrome c 0.003-0.10 mM.; captured paper segment: Table 3 (Fe-S d-iLDH kinetics with different electron acceptors) | Fe-S d-iLDH / MTT electron acceptor | derived kcat/Km from Fe-S d-iLDH kcat and Km cells | 128 / 48 s^-1 per microM || metric: km; table label: Table 3 (Fe-S d-iLDH kinetics with different electron acceptors); row label: Fe-S d-iLDH / MTT electron acceptor; column label: Km (microM), Fe-S d-iLDH; raw value: 48 +/- 1.9; raw unit: microM; normalized value: 0.048; normalized unit: mM; assay condition: 30 C assay in 1 ml 50 mM Tris-HCl pH 7.4 with 1.0 mM D-lactate as substrate; electron acceptor ranges: MTT 0.003-0.25 mM, coenzyme Q10 0.003-0.03 mM, cytochrome c 0.003-0.10 mM.; captured paper segment: Table 3 (Fe-S d-iLDH kinetics with different electron acceptors) | Fe-S d-iLDH / MTT electron acceptor | Km (microM), Fe-S d-iLDH | 48 +/- 1.9 microM

normalized_value_unit_evidence: kcat normalized value: 128; normalized unit: s^-1; kcat_over_km normalized value: 2666.666666666666666666666667; normalized unit: s^-1 mM^-1; km normalized value: 0.048; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 128 +/- 5.7; raw unit: s^-1; kcat_over_km raw value: 128 / 48; raw unit: s^-1 per microM; km raw value: 48 +/- 1.9; raw unit: microM

row_label: Fe-S d-iLDH / MTT electron acceptor


column_label: table label: Table 1 (Fe-S d-iLDH kinetic parameters toward different substrates); row label: Fe-S d-iLDH / D-2-Hydroxybutyrate; column label: kcat (s^-1), Fe-S d-iLDH; derived kcat/Km from Fe-S d-iLDH kcat and Km cells; Km (microM), Fe-S d-iLDH; raw value/unit and normalized value/unit preserved per metric; assay condition: 30 C assay in 1 ml 50 mM Tris-HCl pH 7.4 with MTT as electron acceptor; substrate ranges: D-lactate 0.005-0.35 mM, L-lactate 0.30-6.25 mM, D-2-hydroxybutyrate 0.015-1.25 mM, D-glycerate 0.30-6.25 mM.; captured paper segment: Table 1 (Fe-S d-iLDH kinetic parameters toward different substrates); Fe-S d-iLDH / D-2-Hydroxybutyrate; kcat 66 s^-1, kcat_over_km 660 s^-1 mM^-1, km 0.1 mM.

normalized_value_unit_evidence: kcat normalized value: 66; normalized unit: s^-1; kcat_over_km normalized value: 660; normalized unit: s^-1 mM^-1; km normalized value: 0.1; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 66; raw unit: s^-1; kcat_over_km raw value: 66 / 100; raw unit: s^-1 per microM; km raw value: 100; raw unit: microM

row_label: Fe-S d-iLDH / D-2-Hydroxybutyrate


column_label: table label: Table 3 (Fe-S d-iLDH kinetics with different electron acceptors); row label: Fe-S d-iLDH / coenzyme Q10 electron acceptor; column label: kcat (s^-1), Fe-S d-iLDH; derived kcat/Km from Fe-S d-iLDH kcat and Km cells; Km (microM), Fe-S d-iLDH; raw value/unit and normalized value/unit preserved per metric; assay condition: 30 C assay in 1 ml 50 mM Tris-HCl pH 7.4 with 1.0 mM D-lactate as substrate; electron acceptor ranges: MTT 0.003-0.25 mM, coenzyme Q10 0.003-0.03 mM, cytochrome c 0.003-0.10 mM.; captured paper segment: Table 3 (Fe-S d-iLDH kinetics with different electron acceptors); Fe-S d-iLDH / coenzyme Q10 electron acceptor; kcat 2.4 s^-1, kcat_over_km 585.3658536585365853658536585 s^-1 mM^-1, km 0.0041 mM.

normalized_value_unit_evidence: kcat normalized value: 2.4; normalized unit: s^-1; kcat_over_km normalized value: 585.3658536585365853658536585; normalized unit: s^-1 mM^-1; km normalized value: 0.0041; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 2.4; raw unit: s^-1; kcat_over_km raw value: 2.4 / 4.1; raw unit: s^-1 per microM; km raw value: 4.1; raw unit: microM


substrate_name: D-Glycerate

column_label: table label: Table 1 (Fe-S d-iLDH kinetic parameters toward different substrates); row label: Fe-S d-iLDH / D-Glycerate; column label: kcat (s^-1), Fe-S d-iLDH; derived kcat/Km from Fe-S d-iLDH kcat and Km cells; Km (microM), Fe-S d-iLDH; raw value/unit and normalized value/unit preserved per metric; assay condition: 30 C assay in 1 ml 50 mM Tris-HCl pH 7.4 with MTT as electron acceptor; substrate ranges: D-lactate 0.005-0.35 mM, L-lactate 0.30-6.25 mM, D-2-hydroxybutyrate 0.015-1.25 mM, D-glycerate 0.30-6.25 mM.; captured paper segment: Table 1 (Fe-S d-iLDH kinetic parameters toward different substrates); Fe-S d-iLDH / D-Glycerate; kcat 8 s^-1, kcat_over_km 5.79710144927536231884057971 s^-1 mM^-1, km 1.38 mM.

normalized_value_unit_evidence: kcat normalized value: 8; normalized unit: s^-1; kcat_over_km normalized value: 5.79710144927536231884057971; normalized unit: s^-1 mM^-1; km normalized value: 1.38; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 8; raw unit: s^-1; kcat_over_km raw value: 8 / 1380; raw unit: s^-1 per microM; km raw value: 1380; raw unit: microM

row_label: Fe-S d-iLDH / D-Glycerate

substrate: D-Glycerate


substrate_name: D-Lactate

column_label: table label: Table 1 (Fe-S d-iLDH kinetic parameters toward different substrates); row label: Fe-S d-iLDH / D-Lactate; column label: kcat (s^-1), Fe-S d-iLDH; derived kcat/Km from Fe-S d-iLDH kcat and Km cells; Km (microM), Fe-S d-iLDH; raw value/unit and normalized value/unit preserved per metric; assay condition: 30 C assay in 1 ml 50 mM Tris-HCl pH 7.4 with MTT as electron acceptor; substrate ranges: D-lactate 0.005-0.35 mM, L-lactate 0.30-6.25 mM, D-2-hydroxybutyrate 0.015-1.25 mM, D-glycerate 0.30-6.25 mM.; captured paper segment: Table 1 (Fe-S d-iLDH kinetic parameters toward different substrates); Fe-S d-iLDH / D-Lactate; kcat 120 s^-1, kcat_over_km 2105.263157894736842105263158 s^-1 mM^-1, km 0.057 mM.

normalized_value_unit_evidence: kcat normalized value: 120; normalized unit: s^-1; kcat_over_km normalized value: 2105.263157894736842105263158; normalized unit: s^-1 mM^-1; km normalized value: 0.057; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 120; raw unit: s^-1; kcat_over_km raw value: 120 / 57; raw unit: s^-1 per microM; km raw value: 57; raw unit: microM

row_label: Fe-S d-iLDH / D-Lactate

substrate: D-Lactate


substrate_name: L-Lactate

column_label: table label: Table 1 (Fe-S d-iLDH kinetic parameters toward different substrates); row label: Fe-S d-iLDH / L-Lactate; column label: kcat (s^-1), Fe-S d-iLDH; derived kcat/Km from Fe-S d-iLDH kcat and Km cells; Km (microM), Fe-S d-iLDH; raw value/unit and normalized value/unit preserved per metric; assay condition: 30 C assay in 1 ml 50 mM Tris-HCl pH 7.4 with MTT as electron acceptor; substrate ranges: D-lactate 0.005-0.35 mM, L-lactate 0.30-6.25 mM, D-2-hydroxybutyrate 0.015-1.25 mM, D-glycerate 0.30-6.25 mM.; captured paper segment: Table 1 (Fe-S d-iLDH kinetic parameters toward different substrates); Fe-S d-iLDH / L-Lactate; kcat 9.5 s^-1, kcat_over_km 9.134615384615384615384615385 s^-1 mM^-1, km 1.04 mM.

normalized_value_unit_evidence: kcat normalized value: 9.5; normalized unit: s^-1; kcat_over_km normalized value: 9.134615384615384615384615385; normalized unit: s^-1 mM^-1; km normalized value: 1.04; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 9.5; raw unit: s^-1; kcat_over_km raw value: 9.5 / 1040; raw unit: s^-1 per microM; km raw value: 1040; raw unit: microM

row_label: Fe-S d-iLDH / L-Lactate

substrate: L-Lactate


substrate_name: (R)-lactate

substrate: (R)-lactate


substrate_name: (S)-lactate

substrate: (S)-lactate


column_label: metric: kcat; table label: Table 1 (Fe-S d-iLDH kinetic parameters toward different substrates); row label: Fe-S d-iLDH / D-Glycerate; column label: kcat (s^-1), Fe-S d-iLDH; raw value: 8.0 +/- 1.4; raw unit: s^-1; normalized value: 8; normalized unit: s^-1; assay condition: 30 C assay in 1 ml 50 mM Tris-HCl pH 7.4 with MTT as electron acceptor; substrate ranges: D-lactate 0.005-0.35 mM, L-lactate 0.30-6.25 mM, D-2-hydroxybutyrate 0.015-1.25 mM, D-glycerate 0.30-6.25 mM.; captured paper segment: Table 1 (Fe-S d-iLDH kinetic parameters toward different substrates) | Fe-S d-iLDH / D-Glycerate | kcat (s^-1), Fe-S d-iLDH | 8.0 +/- 1.4 s^-1 || metric: kcat_over_km; table label: Table 1 (Fe-S d-iLDH kinetic parameters toward different substrates); row label: Fe-S d-iLDH / D-Glycerate; column label: derived kcat/Km from Fe-S d-iLDH kcat and Km cells; raw value: 8 / 1380; raw unit: s^-1 per microM; normalized value: 5.79710144927536231884057971; normalized unit: s^-1 mM^-1; assay condition: 30 C assay in 1 ml 50 mM Tris-HCl pH 7.4 with MTT as electron acceptor; substrate ranges: D-lactate 0.005-0.35 mM, L-lactate 0.30-6.25 mM, D-2-hydroxybutyrate 0.015-1.25 mM, D-glycerate 0.30-6.25 mM.; captured paper segment: Table 1 (Fe-S d-iLDH kinetic parameters toward different substrates) | Fe-S d-iLDH / D-Glycerate | derived kcat/Km from Fe-S d-iLDH kcat and Km cells | 8 / 1380 s^-1 per microM || metric: km; table label: Table 1 (Fe-S d-iLDH kinetic parameters toward different substrates); row label: Fe-S d-iLDH / D-Glycerate; column label: Km (microM), Fe-S d-iLDH; raw value: 1380; raw unit: microM; normalized value: 1.38; normalized unit: mM; assay condition: 30 C assay in 1 ml 50 mM Tris-HCl pH 7.4 with MTT as electron acceptor; substrate ranges: D-lactate 0.005-0.35 mM, L-lactate 0.30-6.25 mM, D-2-hydroxybutyrate 0.015-1.25 mM, D-glycerate 0.30-6.25 mM.; captured paper segment: Table 1 (Fe-S d-iLDH kinetic parameters toward different substrates) | Fe-S d-iLDH / D-Glycerate | Km (microM), Fe-S d-iLDH | 1380 microM

raw_value_unit_evidence: kcat raw value: 8.0 +/- 1.4; raw unit: s^-1; kcat_over_km raw value: 8 / 1380; raw unit: s^-1 per microM; km raw value: 1380; raw unit: microM


substrate_name: coenzyme F420 (at pH 7 and 40 degrees Celsius)

column_label: Abstract reports apparent Km values for F420 and glucose-6-phosphate were, respectively, 0.004 and 1.6 mM.

raw_value_unit_evidence: Km raw_value=0.004 mM raw_unit=mM

row_label: Mycobacterium smegmatis F420-dependent glucose-6-phosphate dehydrogenase / F420

table_label: PubMed XML abstract PMID 8631674


substrate_name: D-glucose 6-phosphate (at pH 7 and 40 degrees Celsius)

raw_value_unit_evidence: Km raw_value=1.6 mM raw_unit=mM

row_label: Mycobacterium smegmatis F420-dependent glucose-6-phosphate dehydrogenase / glucose-6-phosphate


substrate_name: D-lactate

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

proof_lines:
Escherichia coli
membrane-bound D-lactate dehydrogenase

substrate: D-lactate


organism: Corynebacterium glutamicum

column_label: PMC full-text Discussion says the determined Km of 0.62 mM for D-lactate is similar to D-lactate dehydrogenases from Neisseria meningitidis and E. coli.

normalized_value_unit_evidence: Km normalized_value=0.62 normalized_unit=mM; CatLog row stores 0.61 mM.

raw_value_unit_evidence: Discussion prose reports the determined Km of 0.62 mM for D-lactate.

row_label: C. glutamicum Dld D-lactate Km sentence

table_label: PMC3022706 full-text Discussion prose


substrate_name: ATP (in the presence of 0.2 mM dGTP)

assay_conditions_summary: cofactor ATP

substrate: ATP (in the presence of 0.2 mM dGTP)


substrate_name: GTP (in the presence of 0.8 mM dTTP)

substrate: GTP (in the presence of 0.8 mM dTTP)


substrate_name: UTP (in the presence of 0.4 mM ATP)

substrate: UTP (in the presence of 0.4 mM ATP)


enzyme_display_name: Quinohemoprotein alcohol dehydrogenase ADH-IIG

substrate_name: ethanol

column_label: Table 7 lists ADH IIG ethanol Km = 33.2 mM.

raw_value_unit_evidence: KM raw_value=33.2 raw_unit=mM

row_label: ADH IIG / Ethanol

table_label: PMID 7730276 Table 7

substrate: ethanol


enzyme: Quinohemoprotein alcohol dehydrogenase ADH-IIG


substrate_name: glycerol

smiles: C(C(CO)O)O

column_label: Table 7 lists ADH IIG glycerol Km = 2.40 mM.

raw_value_unit_evidence: KM raw_value=2.40 raw_unit=mM

row_label: ADH IIG / Glycerol

substrate: glycerol


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: glucose 6-phosphate

column_label: Figure 6C caption and Results text report the Km for glucose 6-phosphate/G6P as 100 uM.

raw_value_unit_evidence: Km raw_value=100 uM raw_unit=uM

row_label: M. tuberculosis FGD1 / glucose 6-phosphate (G6P)

table_label: JBC Figure 6C caption and Results paragraph

substrate: glucose 6-phosphate


organism: Pseudomonas putida KT2440

substrate_name: coenzyme Q10

row_label: Fe-S d-iLDH / coenzyme Q10 electron acceptor

table_label: Table 3 (Fe-S d-iLDH kinetics with different electron acceptors)

substrate: coenzyme Q10


enzyme_display_name: lactate-malate transhydrogenase

organism: Veillonella parvula

substrate_name: oxaloacetate

enzyme: lactate-malate transhydrogenase

substrate: oxaloacetate


substrate_name: L-malate

substrate: L-malate


substrate_name: L-lactate

substrate: L-lactate


substrate_name: pyruvate

substrate: pyruvate


enzyme_display_name: D-lactate dehydrogenase (acceptor)

organism: Sulfurisphaera tokodaii

proof_lines: pH 8.5, 60°C, cosubstrate: 2,6-dichlorophenolindophenol

proof_lines: pH 8.5, 60°C, cosubstrate: 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide

enzyme: D-lactate dehydrogenase (acceptor)


substrate_name: CTP

proof_lines:
CTP reduction
ATP stimulation
class III ribonucleotide reductase

substrate: CTP


organism: Oryctolagus cuniculus

substrate_name: D-malate

substrate: D-malate


enzyme_display_name: pyridoxine 5-dehydrogenase

organism: Arthrobacter sp.

substrate_name: pyridoxine

enzyme: pyridoxine 5-dehydrogenase

substrate: pyridoxine


smiles: O=O


enzyme_display_name: dehydrogluconate dehydrogenase

organism: Gluconobacter oxydans

enzyme: dehydrogluconate dehydrogenase


organism: Aeropyrum pernix

substrate_name: (R)-lactate

assay_conditions_summary: pH 7; 333.15 K; cofactor FAD

substrate: (R)-lactate


organism: Candidatus Caldarchaeum subterraneum

proof_lines: pH 7.0, 60°C, electron acceptor: oxidized 2,6-dichlorophenolindophenol


enzyme_display_name: L-2-hydroxyglutarate dehydrogenase

organism: Indibacter alkaliphilus (strain CCUG 57479 / KCTC 22604 / LW1)

substrate_name: (S)-2-hydroxyglutarate (at pH 7.4 and 25 degrees Celsius)

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

proof_lines: kcat is 3.7 sec(-1) with DCPIP as electron acceptor (at pH 7.4 and 25 degrees Celsius).

enzyme: L-2-hydroxyglutarate dehydrogenase


organism: Thermoproteus tenax

substrate_name: D-lactate

proof_lines: 60°C, pH not specified in the publication


enzyme_display_name: glucoside 3-dehydrogenase (acceptor)

organism: Agrobacterium tumefaciens

substrate_name: D-glucose

enzyme: glucoside 3-dehydrogenase (acceptor)

substrate: D-glucose


substrate_name: sucrose

substrate: sucrose


substrate_name: cellobiose

substrate: cellobiose


substrate_name: Lactobionate

substrate: Lactobionate


substrate_name: Maltobionate

substrate: Maltobionate


organism: Pseudomonas sp.


enzyme_display_name: glycolate dehydrogenase

organism: Trichoderma harzianum

substrate_name: Nitro blue tetrazolium

enzyme: glycolate dehydrogenase

substrate: Nitro blue tetrazolium


substrate_name: glycolate

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

substrate: glycolate


substrate_name: dihydroxyacetone

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

substrate: dihydroxyacetone


organism: Homo sapiens


organism: Arabidopsis thaliana

substrate_name: (S)-2-hydroxyglutarate (with DCIP as acceptor molecule)

column_label: Downloaded OUP/PCP PDF states that kinetic parameters of A. thaliana L-2HGDH indicated KmL-2HG=0.24 +/- 0.08 mM.

raw_value_unit_evidence: Results text reports affinity constant KmL-2HG raw_value=0.24 +/- 0.08 raw_unit=mM.

row_label: Arabidopsis thaliana L-2HGDH with L-2HG

table_label: PDF Results section, L-2HGDH kinetic characterization


organism: Agaricus bisporus


substrate_name: D-cellobiose

substrate: D-cellobiose


substrate_name: D-xylose

substrate: D-xylose


organism: Chlamydomonas reinhardtii

proof_lines: with 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0 and 30°C


substrate: D-lactate


substrate_name: L-lactate

substrate: L-lactate


organism: Euglena gracilis


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


enzyme_display_name: sorbose dehydrogenase

enzyme: sorbose dehydrogenase


organism: Flavobacterium saccharophilum


substrate_name: validoxylamine A

substrate: validoxylamine A


enzyme_display_name: D-lactate dehydrogenase

organism: Anaerostipes hadrus

substrate_name: (R)-lactate (at pH 7.4 and 25 degrees Celsius)

proof_lines: kcat is 5.2 sec(-1) with DCPIP as electron acceptor (at pH 7.4 and 25 degrees Celsius).

enzyme: D-lactate dehydrogenase


organism: Thalassiosira pseudonana


substrate_name: L(+)-lactate

substrate: L(+)-lactate


substrate_name: D(-)-lactate

substrate: D(-)-lactate


enzyme_display_name: cellobiose dehydrogenase (acceptor)

organism: Termitomyces clypeatus

substrate_name: cellotriose

enzyme: cellobiose dehydrogenase (acceptor)

substrate: cellotriose


substrate_name: cellotetraose

substrate: cellotetraose


substrate_name: cellopentaose

substrate: cellopentaose


substrate_name: 2,6-dichlorophenol indophenol

substrate: 2,6-dichlorophenol indophenol


substrate_name: ferricyanide

substrate: ferricyanide


organism: Phanerodontia chrysosporium


substrate_name: oxygen

substrate: oxygen


substrate_name: Mn(III)-malonate

substrate: Mn(III)-malonate


enzyme_display_name: UniProt A9XK88

organism: Thermothelomyces myriococcoides

source_db: skid

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=30°C, pH=6

enzyme: UniProt A9XK88

source: skid


organism: Humicola insolens

substrate_name: cellobiose

sequence_variant_note: Mutation signature C285Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: cellobiose


organism: Thermothelomyces fergusii

sequence_variant_note: Mutation signature C291Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: D-glucose

substrate: D-glucose


substrate_name: lactose

substrate: lactose


substrate_name: maltose

substrate: maltose


organism: Gluconobacter oxydans

substrate_name: L-sorbose

substrate: L-sorbose


enzyme_display_name: Glycolate oxidase subunit GlcD

organism: Escherichia coli (strain K12)

substrate_name: glycolate

proof_lines: Parameters measured from a partially purified enzyme from extracts of glycolate grown cells.

enzyme: Glycolate oxidase subunit GlcD

substrate: glycolate


substrate_name: D-lactate

substrate: D-lactate


enzyme_display_name: Glycolate oxidase subunit GlcE

enzyme: Glycolate oxidase subunit GlcE


enzyme_display_name: Glycolate oxidase iron-sulfur subunit

enzyme: Glycolate oxidase iron-sulfur subunit


organism: Sphingobacterium faecium

assay_conditions_summary: pH 6

column_label: PubMed abstract reports D-glucose apparent Km = 1.1 mM; this matches the current row value.

raw_value_unit_evidence: Km raw_value=1.1 mM raw_unit=mM

row_label: Prose segment: D-glucose apparent Km

table_label: PubMed PMID 24585380 abstract


substrate_name: sucrose

column_label: PubMed abstract reports sucrose apparent Km = 1.7 mM; this matches the current row value.

raw_value_unit_evidence: Km raw_value=1.7 mM raw_unit=mM

row_label: Prose segment: sucrose apparent Km

substrate: sucrose


substrate_name: validoxylamine A

column_label: PubMed abstract reports validoxylamine apparent Km = 2.1 mM; this matches the current row value.

raw_value_unit_evidence: Km raw_value=2.1 mM raw_unit=mM

row_label: Prose segment: validoxylamine apparent Km

substrate: validoxylamine A


organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

column_label: Kinetic analysis prose; row rDld / D-lactate; metric Km.

normalized_value_unit_evidence: Km=0.15 mM converted from 150 uM.

raw_value_unit_evidence: PMC94217 kinetic analysis reports a Km of 150 uM for D-lactate at 60 C.

row_label: rDld / D-lactate

table_label: Kinetic analysis prose


organism: Mycobacterium tuberculosis

substrate_name: oxidized coenzyme F420

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

substrate: oxidized coenzyme F420


substrate_name: D-glucose 6-phosphate

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

substrate: D-glucose 6-phosphate


enzyme_display_name: D-lactate dehydrogenase (quinone)

organism: Escherichia coli

substrate_name: (R)-lactate

enzyme: D-lactate dehydrogenase (quinone)

substrate: (R)-lactate


enzyme_display_name: alkan-1-ol dehydrogenase (acceptor)

organism: Sphingopyxis terrae

substrate_name: Tetraethylene glycol

smiles: C(COCCOCCOCCO)O

assay_conditions_summary: pH 9

proof_lines: mutant enzymes N511H and C472A, at pH 9.0, temperature not specified in the publication

enzyme: alkan-1-ol dehydrogenase (acceptor)

substrate: Tetraethylene glycol


proof_lines: mutant enzyme C382A, at pH 9.0, temperature not specified in the publication


proof_lines: mutant enzyme C379A, at pH 9.0, temperature not specified in the publication


organism: Archaeoglobus fulgidus


substrate_name: benzyl alcohol

substrate: benzyl alcohol


smiles: CCCCCCO


proof_lines: wild type enzyme, at pH 9.0, temperature not specified in the publication


proof_lines: mutant enzyme H467A, at pH 9.0, temperature not specified in the publication


organism: Trametes pubescens

proof_lines: pH 4.5, 30°C, electron acceptor: 2,6-dichlorophenol indophenol


substrate_name: cellopentaose

substrate: cellopentaose


substrate_name: cellotetraose

substrate: cellotetraose


substrate_name: xylobiose

substrate: xylobiose


substrate_name: thiocellobiose

substrate: thiocellobiose


substrate_name: 2,6-dichlorophenol indophenol

substrate: 2,6-dichlorophenol indophenol


substrate_name: cytochrome c

substrate: cytochrome c


substrate_name: benzyl alkohol

substrate: benzyl alkohol


organism: Mycothermus thermophilus


substrate_name: maltose

proof_lines:
pH 7.5, 40°C
review, different references

substrate: maltose


substrate_name: cellotriose

substrate: cellotriose


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: benzoquinone

substrate: benzoquinone


organism: Trametes villosa

substrate_name: glucose

substrate: glucose


organism: Agroathelia rolfsii

substrate_name: cellobiose

proof_lines: electron acceptors methylene blue or methylene green

substrate: cellobiose


organism: Trametes hirsuta


substrate_name: DCPIP

substrate: DCPIP


proof_lines:
electron donor
at pH 4.5


proof_lines:
at pH 4.5
electron donor


organism: Neurospora crassa

substrate_name: maltotriose

proof_lines:
isoform CDH IIB, at pH 6.0 and 30°C
isoform CDH IIA, at pH 6.0 and 30°C

substrate: maltotriose


substrate_name: maltotetraose

proof_lines: recombinant enzyme, in 100 mM sodium acetate (pH 4.5), at 30°C

substrate: maltotetraose


substrate_name: D-galactose

substrate: D-galactose


substrate_name: D-xylose

substrate: D-xylose


substrate_name: xylotriose

substrate: xylotriose


substrate_name: Mannopentaose

substrate: Mannopentaose


substrate_name: cellopentaose

substrate: cellopentaose


organism: Thermothelomyces myriococcoides

assay_conditions_summary: pH 6; 303.15 K; buffer 100 mM McIlvaine

proof_lines: recombinant wild type enzyme, in 100 mM McIlvaine buffer, pH 6.0, at 30°C


proof_lines: mutant enzyme N700S, in 100 mM McIlvaine buffer, pH 6.0, at 30°C


substrate_name: 2,6-dichlorophenol indophenol

substrate: 2,6-dichlorophenol indophenol


proof_lines: mutant enzyme 700S, in 100 mM McIlvaine buffer, pH 6.0, at 30°C


organism: Gelatoporia subvermispora

proof_lines: 2,6-dichloroindophenol as electron acceptor


substrate_name: D-glucose

substrate: D-glucose


substrate_name: ferricenium

substrate: ferricenium


organism: Ensifer sp. AS08

smiles: C(CO)O

assay_conditions_summary: pH 8; 298.15 K; buffer 0.1 M Tris-HCl

proof_lines: mutant enzyme H465A, in 0.1 M Tris-HCl buffer (pH 8.0), at 25°C


substrate_name: PEG-mono-4-nonylphenyl ether, averaging 10 ethoxy units


proof_lines: mutant enzyme N90A, in 0.1 M Tris-HCl buffer (pH 8.0), at 25°C

substrate: PEG-mono-4-nonylphenyl ether, averaging 10 ethoxy units


proof_lines: wild type enzyme, in 0.1 M Tris-HCl buffer (pH 8.0), at 25°C


organism: Arabidopsis thaliana


substrate_name: cellohexaose

substrate: cellohexaose


substrate_name: cellotetraose

substrate: cellotetraose


substrate_name: cellotriose

substrate: cellotriose


organism: Coprinopsis cinerea


substrate_name: maltose

proof_lines:
at pH 6.0 and 30°C
isoform CDH IIA, at pH 6.0 and 30°C
at pH 5.5 and 30°C

substrate: maltose


substrate_name: cytochrome c

substrate: cytochrome c


organism: Podospora anserina


substrate_name: lactose

substrate: lactose


organism: Thermothelomyces heterothallicus

proof_lines:
at 25°C
at 45°C


proof_lines:
at 25°C
at 45°C
at pH 4.5 and 25°C


substrate_name: ferricyanide

substrate: ferricyanide


protein_accession_database: NCBI Protein

sequence_source: paper_backed_accession:BAB61732.1 (PMID:11673442; polyethylene glycol dehydrogenase [Sphingopyxis terrae])

smiles: CCCCCCCO

column_label: Table 1 row 1-Heptanol lists K_m 0.4 mM for recombinant PEG-DH.

raw_value_unit_evidence: K_m raw_value=0.4 raw_unit=mM; Vmax context cell=23.5 U/mg protein

table_label: Table 1. Substrate specificity of recombinant PEG-DH


column_label: Table 1 row 1-Hexanol lists K_m 0.5 mM for recombinant PEG-DH.

raw_value_unit_evidence: K_m raw_value=0.5 raw_unit=mM; Vmax context cell=17.0 U/mg protein


substrate_name: benzyl alcohol

column_label: Table 1 row Benzyl alcohol lists K_m 0.6 mM for recombinant PEG-DH.

raw_value_unit_evidence: K_m raw_value=0.6 raw_unit=mM; Vmax context cell=17.8 U/mg protein

row_label: Benzyl alcohol

substrate: benzyl alcohol


column_label: Table 1 row PEG 400 lists K_m 0.7 mM for recombinant PEG-DH.

raw_value_unit_evidence: K_m raw_value=0.7 raw_unit=mM; Vmax context cell=10.2 U/mg protein

row_label: PEG 400


column_label: Table 1 row PEG 1000 lists K_m 1.6 mM for recombinant PEG-DH.

raw_value_unit_evidence: K_m raw_value=1.6 raw_unit=mM; Vmax context cell=12.1 U/mg protein


substrate_name: tetraethylene glycol-monoethyl ether

smiles: CCOCCOCCOCCOCCO

column_label: Table 1 row TEG-monoethyl ether lists K_m 4.2 mM for recombinant PEG-DH.

raw_value_unit_evidence: K_m raw_value=4.2 raw_unit=mM; Vmax context cell=6.6 U/mg protein

row_label: TEG-monoethyl ether

substrate: tetraethylene glycol-monoethyl ether


smiles: CCCO

column_label: Table 1 row 1-Propanol lists K_m 6.6 mM for recombinant PEG-DH.

raw_value_unit_evidence: K_m raw_value=6.6 raw_unit=mM; Vmax context cell=3.3 U/mg protein


substrate_name: Tetraethylene glycol

column_label: Table 1 row TEG lists K_m 14 mM for recombinant PEG-DH.

raw_value_unit_evidence: K_m raw_value=14 raw_unit=mM; Vmax context cell=14.7 U/mg protein

row_label: TEG

substrate: Tetraethylene glycol


organism: Fungi


substrate_name: cellobiose

substrate: cellobiose


assay_conditions_summary: pH 4; 303.15 K; buffer 100 mM sodium acetate

proof_lines: in 100 mM sodium acetate buffer, pH 4.0, at 30°C

proof_lines: CDH modified plain screen printed electrodes at 0 mV, pH and temperature not specified in the publication

proof_lines: 2,6-dichloroindophenol as electron acceptor, at 40°C


substrate_name: maltotetraose

substrate: maltotetraose


proof_lines: 2,6-diclorindophenol as electron acceptor, at 40°C


organism: Trametes versicolor


substrate_name: xylobiose

substrate: xylobiose


organism: Flavobacterium sp.

substrate_name: n-Butyraldehyde

smiles: CCCC=O

substrate: n-Butyraldehyde


substrate_name: ferricytochrome c

proof_lines: in the presence of 30 mM NaCl, at pH 7.5 and 30°C

proof_lines: in the presence of 30 mM NaCl, at pH 5.5 and 30°C

proof_lines: in the presence of 30 mM CaCl2, at pH 5.5 and 30°C

substrate: ferricytochrome c


organism: Pseudomonas sp.


organism: Trametes sanguinea

proof_lines:
pH 4.5, 30°C, without polysaccharide
at pH 4.5 and 30°C


organism: Phanerochaete sordida


organism: Monilia sitophila


organism: Coniophora puteana


organism: Trametes hirsuta

substrate_name: cellopentaose

substrate: cellopentaose


organism: Agroathelia rolfsii

substrate_name: D-glucose

substrate: D-glucose


organism: Coniophora puteana (Schum ex Fr) Karsten


organism: Physcomitrium patens

proof_lines: at pH 6.0, temperature not specified in the publication


organism: Thermothelomyces myriococcoides


proof_lines:
pH 4.5, 25°C, recombinant enzyme
at pH 4.5


organism: Thermothelomyces fergusii


organism: Cerrena unicolor

proof_lines: with 2,6-dichlorophenolindophenol as cosubstrate, at pH 4.5 and 30°C

proof_lines: with ferricytochrome c as cosubstrate, at pH 4.5 and 30°C


organism: Phanerodontia chrysosporium

proof_lines:
ferricyanide as electron acceptor
at pH 4.5 and 30°C
at pH 4.5 and 25°C


proof_lines: recombinant enzyme from Pichia pastoris, with ferricytochrome c as cosubstrate, at pH 7.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01738 and applied mutation signature H689V with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1, Cellobiose oxidation block, enzyme row 'H689V'; column 'kcat (s-1)' = 0.002; column 'Km (µM)' = 31; Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.002 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 0.002 s^(-1). Km: printed Table 1 cell 31 µM; 31 / 1000 = 0.031 mM; the paper value is 0.031 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 0.06451612903225806 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.002 / 0.031 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Cellobiose oxidation block, enzyme row 'H689V': kcat = 0.002 s-1; Km = 31 µM; Table 1 prints no kcat/Km cell for this row.

table_label: Table 1: Steady-State Kinetic Parameters for rCDH and H689 Variants (Biochemistry 2003, 42(14):4049-4056)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01738 and applied mutation signature H689A with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1, Cellobiose oxidation block, enzyme row 'H689A'; column 'kcat (s-1)' = 0.003; column 'Km (µM)' = 21; Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.003 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 0.003 s^(-1). Km: printed Table 1 cell 21 µM; 21 / 1000 = 0.021 mM; the paper value is 0.021 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 0.14285714285714285 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.003 / 0.021 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Cellobiose oxidation block, enzyme row 'H689A': kcat = 0.003 s-1; Km = 21 µM; Table 1 prints no kcat/Km cell for this row.


sequence_variant_note: Mutation context was captured, but conflicting substitutions targeted the same residue position.

proof_lines: pH 4.5, 23°C, mutant enzyme H689Q or mutant H689A

proof_lines: pH 4.5, 23°C, mutant enzyme H689Q or mutant enzyme H689A


proof_lines: pH 4.5, 23°C, mutant enzyme H689N or mutant H689Q


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01738 and applied mutation signature N732D with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'N732D', Cellobiose oxidation columns; column 'Cellobiose oxidation kcat (s-1)' = 0.004; column 'Cellobiose oxidation Km (µM)' = 170; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.004 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 0.004 s^(-1). Km: printed Table 2 cell 170 µM; 170 / 1000 = 0.17 mM; the paper value is 0.17 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 0.023529411764705882 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.004 / 0.17 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'N732D', Cellobiose oxidation columns: cellobiose kcat = 0.004 s-1; cellobiose Km = 170 µM; Table 2 prints no kcat/Km cell for this row.

table_label: Table 2: Steady-State Kinetic Parameters for rCDH and the N732 Variant (Biochemistry 2003, 42(14):4049-4056)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01738 and applied mutation signature H689E with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1, Cellobiose oxidation block, enzyme row 'H689E'; column 'kcat (s-1)' = 0.009; column 'Km (µM)' = 22; Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.009 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 0.009 s^(-1). Km: printed Table 1 cell 22 µM; 22 / 1000 = 0.022 mM; the paper value is 0.022 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 0.40909090909090906 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.009 / 0.022 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Cellobiose oxidation block, enzyme row 'H689E': kcat = 0.009 s-1; Km = 22 µM; Table 1 prints no kcat/Km cell for this row.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01738 and applied mutation signature N732E with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'N732E', Cellobiose oxidation columns; column 'Cellobiose oxidation kcat (s-1)' = 0.21; column 'Cellobiose oxidation Km (µM)' = 230; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.21 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 0.21 s^(-1). Km: printed Table 2 cell 230 µM; 230 / 1000 = 0.23 mM; the paper value is 0.23 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 0.9130434782608695 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.21 / 0.23 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'N732E', Cellobiose oxidation columns: cellobiose kcat = 0.21 s-1; cellobiose Km = 230 µM; Table 2 prints no kcat/Km cell for this row.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01738 and applied mutation signature N732A with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'N732A', Cellobiose oxidation columns; column 'Cellobiose oxidation kcat (s-1)' = 0.4; column 'Cellobiose oxidation Km (µM)' = 17; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.4 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 0.4 s^(-1). Km: printed Table 2 cell 17 µM; 17 / 1000 = 0.017 mM; the paper value is 0.017 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 23.52941176470588 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.4 / 0.017 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'N732A', Cellobiose oxidation columns: cellobiose kcat = 0.4 s-1; cellobiose Km = 17 µM; Table 2 prints no kcat/Km cell for this row.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01738 and applied mutation signature N732Q with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'N732Q', Cellobiose oxidation columns; column 'Cellobiose oxidation kcat (s-1)' = 1.0; column 'Cellobiose oxidation Km (µM)' = 41; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.0 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 1.0 s^(-1). Km: printed Table 2 cell 41 µM; 41 / 1000 = 0.041 mM; the paper value is 0.041 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 24.390243902439025 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.0 / 0.041 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'N732Q', Cellobiose oxidation columns: cellobiose kcat = 1.0 s-1; cellobiose Km = 41 µM; Table 2 prints no kcat/Km cell for this row.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01738 and applied mutation signature N732H with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'N732H', Lactose oxidation columns; column 'Lactose oxidation kcat (s-1)' = 1.7; column 'Lactose oxidation Km (µM)' = 2300; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.7 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 1.7 s^(-1). Km: printed Table 2 cell 2300 µM; 2300 / 1000 = 2.3 mM; the paper value is 2.3 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 0.7391304347826088 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.7 / 2.3 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'N732H', Lactose oxidation columns: lactose kcat = 1.7 s-1; lactose Km = 2300 µM; Table 2 prints no kcat/Km cell for this row.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H689Q with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.


substrate_name: FAD

assay_conditions_summary: pH 4.5; buffer 50 mM acetate; cofactor FAD

column_label: Table 1 row '-' / no added electron acceptor reports rate of FAD reduction 74 +/- 3 s^-1 for CDH.

raw_value_unit_evidence: kcat/rate raw_value=74 +/- 3 raw_unit=s^-1

row_label: CDH + no added electron acceptor

table_label: Table 1. Rate Constants of FAD and Heme Reduction of CDH in the Presence of Ferric Iron or MBQ

substrate: FAD


organism: Thermothielavioides terrestris


proof_lines: pH 4.5, electron acceptor: cytochrome c, wild-type enzyme

proof_lines: pH 4.5, 23°C, recombinant wild-type enzyme


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -13, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M685Y with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -3, so it is treated as a source-provided variant sequence.


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

proof_lines: pH 4.5, 30°C, acceptor: 2,6-dichlorophenolindophenol


proof_lines:
pH 4.5, 30°C
in presence of 0.24 mM O2
in absence of O2


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M65H with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

proof_lines: pH 4.5, electron acceptor: cytochrome c, mutant enzyme M65H

proof_lines: pH 4.5, electron acceptor: 2,6-dichlorophenol indophenol, mutant enzyme M65H


substrate_name: 2,6-dichlorophenol indophenol

proof_lines: pH 4.5, reaction with cellobiose, mutant enzyme M65H

substrate: 2,6-dichlorophenol indophenol


proof_lines: pH 4.5, reaction with cellobiose, wild-type enzyme


organism: Schizophyllum commune

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


substrate_name: cellotriose

substrate: cellotriose


substrate_name: cellotetraose

substrate: cellotetraose


organism: Dichomera saubinetii

assay_conditions_summary: pH 5; 303.15 K; buffer McIlvaine

column_label: Table 3 row Ds CDH IIA; cellobiose lists K_m 125 uM, kcat 27.8 s^-1, and kcat/K_m 2.22 x 10^5 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.125 normalized_unit=mM; kcat normalized_value=27.8 normalized_unit=s^-1; kcat/Km normalized_value=222.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=125 raw_unit=uM; kcat raw_value=27.8 raw_unit=s^-1; kcat/Km raw_value=2.22 x 10^5 raw_unit=M^-1 s^-1

row_label: Ds CDH IIA; cellobiose

table_label: Table 3. Steady-state kinetic constants for selected CDHs with carbohydrate electron donors


column_label: Table 3 row Ds CDH IIA; D-glucose lists K_m 79000 uM, kcat 23.6 s^-1, and kcat/K_m 300 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=79 normalized_unit=mM; kcat normalized_value=23.6 normalized_unit=s^-1; kcat/Km normalized_value=0.3 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=79000 raw_unit=uM; kcat raw_value=23.6 raw_unit=s^-1; kcat/Km raw_value=300 raw_unit=M^-1 s^-1

row_label: Ds CDH IIA; D-glucose


column_label: Table 3 row Ds CDH IIA; lactose lists K_m 215 uM, kcat 28.9 s^-1, and kcat/K_m 1.34 x 10^5 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.215 normalized_unit=mM; kcat normalized_value=28.9 normalized_unit=s^-1; kcat/Km normalized_value=134.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=215 raw_unit=uM; kcat raw_value=28.9 raw_unit=s^-1; kcat/Km raw_value=1.34 x 10^5 raw_unit=M^-1 s^-1

row_label: Ds CDH IIA; lactose


substrate_name: maltose

column_label: Table 3 row Ds CDH IIA; maltose lists K_m 8000 uM, kcat 1.38 s^-1, and kcat/K_m 175 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=8 normalized_unit=mM; kcat normalized_value=1.38 normalized_unit=s^-1; kcat/Km normalized_value=0.175 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=8000 raw_unit=uM; kcat raw_value=1.38 raw_unit=s^-1; kcat/Km raw_value=175 raw_unit=M^-1 s^-1

row_label: Ds CDH IIA; maltose

substrate: maltose


organism: Amesia atrobrunnea

assay_conditions_summary: pH 6; 303.15 K; buffer McIlvaine

column_label: Table 3 row Ca CDH IIA; cellobiose lists K_m 72 uM, kcat 20.1 s^-1, and kcat/K_m 2.79 x 10^5 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.072 normalized_unit=mM; kcat normalized_value=20.1 normalized_unit=s^-1; kcat/Km normalized_value=279.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=72 raw_unit=uM; kcat raw_value=20.1 raw_unit=s^-1; kcat/Km raw_value=2.79 x 10^5 raw_unit=M^-1 s^-1

row_label: Ca CDH IIA; cellobiose


column_label: Table 3 row Ca CDH IIA; D-glucose lists K_m 87000 uM, kcat 16.8 s^-1, and kcat/K_m 195 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=87 normalized_unit=mM; kcat normalized_value=16.8 normalized_unit=s^-1; kcat/Km normalized_value=0.195 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=87000 raw_unit=uM; kcat raw_value=16.8 raw_unit=s^-1; kcat/Km raw_value=195 raw_unit=M^-1 s^-1

row_label: Ca CDH IIA; D-glucose


substrate_name: lactose

column_label: Table 3 row Ca CDH IIA; lactose lists K_m 217 uM, kcat 33.7 s^-1, and kcat/K_m 1.55 x 10^5 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.217 normalized_unit=mM; kcat normalized_value=33.7 normalized_unit=s^-1; kcat/Km normalized_value=155.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=217 raw_unit=uM; kcat raw_value=33.7 raw_unit=s^-1; kcat/Km raw_value=1.55 x 10^5 raw_unit=M^-1 s^-1

row_label: Ca CDH IIA; lactose

substrate: lactose


column_label: Table 3 row Ca CDH IIA; maltose lists K_m 15500 uM, kcat 4.0 s^-1, and kcat/K_m 260 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=15.5 normalized_unit=mM; kcat normalized_value=4.0 normalized_unit=s^-1; kcat/Km normalized_value=0.26 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=15500 raw_unit=uM; kcat raw_value=4.0 raw_unit=s^-1; kcat/Km raw_value=260 raw_unit=M^-1 s^-1

row_label: Ca CDH IIA; maltose


assay_conditions_summary: pH 6; buffer 50 mM MES

column_label: Primary PDF page 10 (journal page 811), Table 3, Lactose row, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: Km=0.023 mM; kcat=1.40 s^-1; kcat/Km=62 s^-1 mM^-1. All exported values match the one printed row.

row_label: Lactose

table_label: Table 3. Apparent kinetic constants for various electron donors with TtCDH


column_label: Primary PDF page 10 (journal page 811), Table 3, Cellobiose row, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: Km=0.0039 mM; kcat=1.23 s^-1; kcat/Km=320 s^-1 mM^-1. All exported values match the one printed row.

row_label: Cellobiose


substrate_name: D-xylose

substrate: D-xylose


column_label: Primary PDF page 10 (journal page 811), Table 3, Glucose row, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: Km=54 mM; kcat=1.01 s^-1; printed kcat/Km=0.019 s^-1 mM^-1. The exported 0.018703703703703705 is the derived 1.01/54 quotient, not the explicit printed ratio.

row_label: Glucose


normalized_value_unit_evidence: Km=0.0039 mM; kcat=1.23 s^-1; printed kcat/Km=320 s^-1 mM^-1. The exported 315.3846153846154 is the derived 1.23/0.0039 quotient, not the explicit printed ratio.


column_label: Table label: Table 3 Apparent kinetic constants for various electron donors with TtCDH.. Row: Cellopentaose. Columns read: kcat (s^-1) cell 1.23, Km (uM) cell 7.5, kcat/Km (M^-1 s^-1) cell 1.6 x 10^5. metric: kcat; raw value: 1.23; raw unit: s^-1; normalized value: 1.23 s^(-1); metric: Km; raw value: 7.5; raw unit: uM; normalized value: 0.0075 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 164.0 s^-1 mM^-1, the quotient of this row's own kcat and Km cells; assay condition: Apparent kinetic constants for carbohydrate electron donors with purified recombinant TtCDH, determined with 110 uM DCPIP electron acceptor in 50 mM MES, pH 6.0; DCPIP is not saturating (Km = 78 uM); initial rate data fitted to the Michaelis-Menten equation with non-linear regression. Standard CDH activity assays monitored DCPIP absorbance at 600 nm at 25.0 C and were done in duplicate. Export row conditions: pH 6; 298.15 K.

normalized_value_unit_evidence: Table 3 row Cellopentaose: kcat 1.23 s^-1 = 1.23 s^(-1); Km 7.5 uM = 0.0075 mM (1 uM = 0.001 mM); kcat/Km 164.0 s^-1 mM^-1 is the quotient of this row's own printed kcat and Km cells: 1.23 s^-1 / 7.5 uM = 164.0 s^-1 mM^-1. The paper's printed kcat/Km cell for this row, 1.6 x 10^5 M^-1 s^-1 = 160.0 s^-1 mM^-1, equals that quotient rounded at the printed cell's own two-significant-figure precision, so the two agree and the difference is printed precision only. In the PDF text layer superscript exponents are flattened, so the printed cell `1.6 × 105` is the paper's 1.6 x 10^5 M^-1 s^-1; the multiplication sign renders as ×, the superscript minus one as − 1, and the micro sign as μ.

raw_value_unit_evidence: Table 3 Apparent kinetic constants for various electron donors with TtCDH. | metric header rows of Table 3: `Substrate           Vmax                  Km                kcat         kcat/Km` with unit row `(μM min− 1)           (μM)              (s− 1)       (M− 1 s− 1)` (the U+2212 minus renders the paper's superscript -1, so the columns read Vmax (uM min^-1), Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1)) | row: Cellopentaose       0.362 ± 0.003         7.5 ± 0.2         1.23         1.6 × 105 | cells read: Vmax = 0.362 ± 0.003 uM min^-1; Km = 7.5 ± 0.2 uM; kcat = 1.23 s^-1; kcat/Km = 1.6 x 10^5 M^-1 s^-1

row_label: TtCDH | Cellopentaose


column_label: Table label: Table 3 Apparent kinetic constants for various electron donors with TtCDH.. Row: Cellotetraose. Columns read: kcat (s^-1) cell 1.23, Km (uM) cell 5.6, kcat/Km (M^-1 s^-1) cell 2.2 x 10^5. metric: kcat; raw value: 1.23; raw unit: s^-1; normalized value: 1.23 s^(-1); metric: Km; raw value: 5.6; raw unit: uM; normalized value: 0.0056 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 219.64285714285714 s^-1 mM^-1, the quotient of this row's own kcat and Km cells; assay condition: Apparent kinetic constants for carbohydrate electron donors with purified recombinant TtCDH, determined with 110 uM DCPIP electron acceptor in 50 mM MES, pH 6.0; DCPIP is not saturating (Km = 78 uM); initial rate data fitted to the Michaelis-Menten equation with non-linear regression. Standard CDH activity assays monitored DCPIP absorbance at 600 nm at 25.0 C and were done in duplicate. Export row conditions: pH 6; 298.15 K.

normalized_value_unit_evidence: Table 3 row Cellotetraose: kcat 1.23 s^-1 = 1.23 s^(-1); Km 5.6 uM = 0.0056 mM (1 uM = 0.001 mM); kcat/Km 219.64285714285714 s^-1 mM^-1 is the quotient of this row's own printed kcat and Km cells: 1.23 s^-1 / 5.6 uM = 219.64285714285714 s^-1 mM^-1. The paper's printed kcat/Km cell for this row, 2.2 x 10^5 M^-1 s^-1 = 220.0 s^-1 mM^-1, equals that quotient rounded at the printed cell's own two-significant-figure precision, so the two agree and the difference is printed precision only. In the PDF text layer superscript exponents are flattened, so the printed cell `2.2 × 105` is the paper's 2.2 x 10^5 M^-1 s^-1; the multiplication sign renders as ×, the superscript minus one as − 1, and the micro sign as μ.

raw_value_unit_evidence: Table 3 Apparent kinetic constants for various electron donors with TtCDH. | metric header rows of Table 3: `Substrate           Vmax                  Km                kcat         kcat/Km` with unit row `(μM min− 1)           (μM)              (s− 1)       (M− 1 s− 1)` (the U+2212 minus renders the paper's superscript -1, so the columns read Vmax (uM min^-1), Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1)) | row: Cellotetraose       0.364 ± 0.003         5.6 ± 0.2         1.23         2.2 × 105 | cells read: Vmax = 0.364 ± 0.003 uM min^-1; Km = 5.6 ± 0.2 uM; kcat = 1.23 s^-1; kcat/Km = 2.2 x 10^5 M^-1 s^-1

row_label: TtCDH | Cellotetraose


column_label: Table label: Table 3 Apparent kinetic constants for various electron donors with TtCDH.. Row: Cellotriose. Columns read: kcat (s^-1) cell 1.25, Km (uM) cell 8.2, kcat/Km (M^-1 s^-1) cell 1.5 x 10^5. metric: kcat; raw value: 1.25; raw unit: s^-1; normalized value: 1.25 s^(-1); metric: Km; raw value: 8.2; raw unit: uM; normalized value: 0.0082 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 152.4390243902439 s^-1 mM^-1, the quotient of this row's own kcat and Km cells; assay condition: Apparent kinetic constants for carbohydrate electron donors with purified recombinant TtCDH, determined with 110 uM DCPIP electron acceptor in 50 mM MES, pH 6.0; DCPIP is not saturating (Km = 78 uM); initial rate data fitted to the Michaelis-Menten equation with non-linear regression. Standard CDH activity assays monitored DCPIP absorbance at 600 nm at 25.0 C and were done in duplicate. Export row conditions: pH 6; 298.15 K.

normalized_value_unit_evidence: Table 3 row Cellotriose: kcat 1.25 s^-1 = 1.25 s^(-1); Km 8.2 uM = 0.0082 mM (1 uM = 0.001 mM); kcat/Km 152.4390243902439 s^-1 mM^-1 is the quotient of this row's own printed kcat and Km cells: 1.25 s^-1 / 8.2 uM = 152.4390243902439 s^-1 mM^-1. The paper's printed kcat/Km cell for this row, 1.5 x 10^5 M^-1 s^-1 = 150.0 s^-1 mM^-1, equals that quotient rounded at the printed cell's own two-significant-figure precision, so the two agree and the difference is printed precision only. In the PDF text layer superscript exponents are flattened, so the printed cell `1.5 × 105` is the paper's 1.5 x 10^5 M^-1 s^-1; the multiplication sign renders as ×, the superscript minus one as − 1, and the micro sign as μ.

raw_value_unit_evidence: Table 3 Apparent kinetic constants for various electron donors with TtCDH. | metric header rows of Table 3: `Substrate           Vmax                  Km                kcat         kcat/Km` with unit row `(μM min− 1)           (μM)              (s− 1)       (M− 1 s− 1)` (the U+2212 minus renders the paper's superscript -1, so the columns read Vmax (uM min^-1), Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1)) | row: Cellotriose         0.370 ± 0.005         8.2 ± 0.4         1.25         1.5 × 105 | cells read: Vmax = 0.370 ± 0.005 uM min^-1; Km = 8.2 ± 0.4 uM; kcat = 1.25 s^-1; kcat/Km = 1.5 x 10^5 M^-1 s^-1

row_label: TtCDH | Cellotriose


column_label: Table II; row Cellotetraose; columns Km, kcat, and kcat/Km; exact cells 61 x 10^-3 mM, 20.7 s^-1, and 339 mM^-1 s^-1.

raw_value_unit_evidence: Table II cellotetraose row: Km 61 x 10^-3 mM; kcat 20.7 s^-1; kcat/Km 339 mM^-1 s^-1.

row_label: cellotetraose

table_label: Table II: Specificity of CDH for Substrates and Electron Acceptors


column_label: Table II; row Cellopentaose; columns Km, kcat, and kcat/Km; exact cells 55 x 10^-3 mM, 21.5 s^-1, and 391 mM^-1 s^-1.

raw_value_unit_evidence: Table II cellopentaose row: Km 55 x 10^-3 mM; kcat 21.5 s^-1; kcat/Km 391 mM^-1 s^-1.

row_label: cellopentaose


column_label: Table II; row Cellotriose; columns Km, kcat, and kcat/Km; exact cells 62 x 10^-3 mM, 24 s^-1, and 387 mM^-1 s^-1.

raw_value_unit_evidence: Table II cellotriose row: Km 62 x 10^-3 mM; kcat 24 s^-1; kcat/Km 387 mM^-1 s^-1.

row_label: cellotriose