enzyme_display_name: C-glycoside oxidase

organism: Microbacterium sp. 5-2b

substrate_name: carminate

assay_conditions_summary: pH 8

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

enzyme: C-glycoside oxidase

substrate: carminate


enzyme_display_name: 5-(hydroxymethyl)furfural oxidase

organism: Methylovorus sp. MP688

source_db: brenda

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

data_origin: experimental

enzyme: 5-(hydroxymethyl)furfural oxidase

status: unverified

source: brenda


mutation_signature: Unknown

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


organism: Methylovorus sp. (strain MP688)

substrate_name: phenylmethanethiol

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

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

substrate: phenylmethanethiol

source: uniprot


verification_status: corrected

assay_conditions_summary: pH 8; buffer 50 mM potassium phosphate

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

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

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

status: corrected


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

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


substrate_name: benzyl alcohol

verification_status: verified

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

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

row_label: Benzyl alcohol

substrate: benzyl alcohol

status: verified


substrate_name: 4-hydroxybenzyl alcohol

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

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

row_label: 4-Hydroxybenzyl alcohol

substrate: 4-hydroxybenzyl alcohol


substrate_name: 4-aminobenzyl alcohol

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

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

row_label: 4-Aminobenzyl alcohol

substrate: 4-aminobenzyl alcohol


substrate_name: 4-chlorobenzyl alcohol

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

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

row_label: 4-Chlorobenzyl alcohol

substrate: 4-chlorobenzyl alcohol


substrate_name: cinnamyl alcohol

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

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

row_label: Cinnamyl alcohol

substrate: cinnamyl alcohol


smiles: CC=CC=CCO

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

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


substrate_name: vanillyl alcohol

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

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

row_label: Vanillyl alcohol

substrate: vanillyl alcohol


enzyme_display_name: 4-hydroxymandelate oxidase

organism: Amycolatopsis orientalis

substrate_name: (S)-Mandelate

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

mutation_type: substitution

enzyme: 4-hydroxymandelate oxidase

substrate: (S)-Mandelate


km_display: Not reported

assay_conditions_summary: pH 7

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

normalized_value_unit_evidence: normalized: kcat=5.17 s^-1

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

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

table_label: Results prose on Hmo activity


organism: Fusarium graminearum

source_db: oed

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

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

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

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

row_label: Fgr AAO DFF row

table_label: PMC8207647 Table 1

source: oed


substrate_name: 3-Methoxybenzyl alcohol

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

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

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

row_label: Fgr AAO 3-methoxybenzyl alcohol row

substrate: 3-Methoxybenzyl alcohol


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

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

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

row_label: FgrAAO / HMFCA


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

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

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

row_label: FgrAAO / HMF


column_label: Table 1 Fgr AAO benzyl alcohol row lists 86+/-12, 37+/-2.8, and 430.

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

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

row_label: Fgr AAO benzyl alcohol row


substrate_name: veratryl alcohol

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

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

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

substrate: veratryl alcohol


substrate_name: 4-Methoxybenzyl alcohol

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

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

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

substrate: 4-Methoxybenzyl alcohol


substrate_name: 4-Hydroxy-3-methoxybenzyl alcohol

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

substrate: 4-Hydroxy-3-methoxybenzyl alcohol


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


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


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


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

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


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


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


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


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


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


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


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


organism: Streptomyces coelicolor

substrate_name: L-Mandelate

substrate: L-Mandelate


organism: Fusarium oxysporum f. sp. lycopersici

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

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

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

row_label: FoxAAO / DFF


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

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

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


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

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

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

row_label: FoxAAO / HMFCA


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

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

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

row_label: FoxAAO / HMF


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

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

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

row_label: FoxAAO / Benzyl alcohol


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

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

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


substrate_name: terephthaldehyde

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

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

substrate: terephthaldehyde


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

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


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

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


enzyme_display_name: vanillyl-alcohol oxidase

organism: Penicillium simplicissimum

substrate_name: Vanillyl alcohol

enzyme: vanillyl-alcohol oxidase

substrate: Vanillyl alcohol


enzyme_display_name: Alditol oxidase

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

substrate_name: xylitol

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

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

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

row_label: Xylitol

table_label: Table 4

enzyme: Alditol oxidase

substrate: xylitol


substrate_name: D-sorbitol

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

substrate: D-sorbitol


smiles: O=O

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

raw_value_unit_evidence: Km raw_value=12 raw_unit=uM

row_label: oxygen electron acceptor

table_label: Catalytic properties prose - electron acceptor kinetics


substrate_name: phenazine methosulfate

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

raw_value_unit_evidence: Km raw_value=43 raw_unit=uM

row_label: phenazine methosulfate electron acceptor

substrate: phenazine methosulfate


organism: Pleurotus eryngii

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


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


organism: Pseudomonas nitroreducens

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


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

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

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


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

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

row_label: Vanillyl alcohol / PseniHMFOHis


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

organism: Escherichia coli

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

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


enzyme_display_name: ecdysone oxidase

organism: Spodoptera littoralis

substrate_name: ecdysone

sequence_source: multiple

source_databases_merged: brenda uniprot

enzyme: ecdysone oxidase

substrate: ecdysone


enzyme_display_name: choline oxidase

organism: Alcaligenes sp.

substrate_name: Betaine aldehyde

sequence: DNPNHSR

wild_type_sequence: DNPNHSR

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

raw_value_unit_evidence: Km raw_value=6.2 raw_unit=mM

row_label: Alcaligenes sp. choline oxidase with betaine aldehyde

table_label: PubMed abstract PMID 6997283

enzyme: choline oxidase

substrate: Betaine aldehyde


organism: Homo sapiens

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


organism: Arthrobacter globiformis

substrate_name: choline

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

substrate: choline


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


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

source_databases_merged: brenda skid


enzyme_display_name: long-chain-alcohol oxidase

organism: uncultured marine group II/III euryarchaeote KM3_72_H01

smiles: CCCCCCCCCCCCO

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

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

row_label: A0A075HNX4 / 1-dodecanol

table_label: Main text Biochemical characterisation paragraph

enzyme: long-chain-alcohol oxidase


enzyme_display_name: glycerol-3-phosphate oxidase

organism: Enterococcus casseliflavus

substrate_name: sn-Glycerol 3-phosphate

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

enzyme: glycerol-3-phosphate oxidase

substrate: sn-Glycerol 3-phosphate


enzyme_display_name: N-acylhexosamine oxidase

organism: Ralstonia solanacearum

substrate_name: chitobiose

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

normalized_value_unit_evidence: Km=19 mM.

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

row_label: A3RXB7 / chitobiose

table_label: Table 1

enzyme: N-acylhexosamine oxidase

substrate: chitobiose


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


organism: Methylovorus sp. MP688

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

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

row_label: Vanillyl alcohol / MetspHMFO


organism: Amycolatopsis orientalis

proof_lines: (S)-mandelate benzoylformate Hmo


enzyme_display_name: prosolanapyrone-II oxidase

organism: Alternaria solani

substrate_name: prosolanapyrone II

assay_conditions_summary: pH 7; buffer 50 mM potassium phosphate

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

raw_value_unit_evidence: Km raw_value=16 raw_unit=uM

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

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

enzyme: prosolanapyrone-II oxidase

substrate: prosolanapyrone II


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


assay_conditions_summary: pH 10

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

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

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


organism: Candida tropicalis

substrate_name: Tetradecanol

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

smiles: CCCCCCCCCCCCCCO

substrate: Tetradecanol


substrate_name: hexadecanol

smiles: CCCCCCCCCCCCCCCCO

substrate: hexadecanol


substrate_name: Dodecanol

proof_lines:
aqueous phase
octane/aqueous phase 99/1

substrate: Dodecanol


substrate_name: Decanol

smiles: CCCCCCCCCCO

substrate: Decanol


substrate_name: Octanol

smiles: CCCCCCCCO

substrate: Octanol


organism: Sus scrofa

substrate_name: glycolate

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

substrate: glycolate


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

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


substrate_name: L-lactate

substrate: L-lactate


substrate_name: DL-beta-phenyllactate

ki_unit: mM

substrate: DL-beta-phenyllactate


organism: Oryza sativa Japonica Group


substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: glycerate

substrate: glycerate


enzyme_display_name: UniProt P13650

organism: Acinetobacter calcoaceticus

substrate_name: cellobiose

source_db: skid

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt P13650

substrate: cellobiose

source: skid


substrate_name: D-galactose

substrate: D-galactose


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


enzyme_display_name: UniProt Q88JH0

organism: Pseudomonas putida

substrate_name: ethanol

smiles: CCO

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

enzyme: UniProt Q88JH0

substrate: ethanol


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


enzyme_display_name: UniProt B8MX95

organism: Aspergillus flavus

substrate_name: D-glucose

enzyme: UniProt B8MX95

substrate: D-glucose


enzyme_display_name: cholesterol oxidase

organism: Streptomyces sp.

substrate_name: dehydroepiandrosterone

enzyme: cholesterol oxidase

substrate: dehydroepiandrosterone


substrate_name: cholesterol

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

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

substrate: cholesterol


enzyme_display_name: glucose 1-dehydrogenase (PQQ, quinone)

organism: Escherichia coli

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

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

enzyme: glucose 1-dehydrogenase (PQQ, quinone)


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


substrate_name: lactose

substrate: lactose


substrate_name: maltose

substrate: maltose


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


enzyme_display_name: alcohol dehydrogenase (quinone)

organism: Komagataeibacter xylinus

substrate_name: acetaldehyde

smiles: CC=O

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

enzyme: alcohol dehydrogenase (quinone)

substrate: acetaldehyde


substrate_name: n-butanol

smiles: CCCCO

substrate: n-butanol


substrate_name: allylic alcohol

smiles: C=CCO

substrate: allylic alcohol


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


substrate_name: 5-(hydroxymethyl)furoic acid

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

substrate: 5-(hydroxymethyl)furoic acid


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


organism: Pseudomonas aeruginosa


substrate_name: citronellol

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

substrate: citronellol


substrate_name: geraniol

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

substrate: geraniol


substrate_name: citral

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

substrate: citral


substrate_name: citronellal

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

substrate: citronellal


enzyme_display_name: glucose 1-dehydrogenase (FAD, quinone)

organism: Pseudomonas sp.

substrate_name: coenzyme Q1

enzyme: glucose 1-dehydrogenase (FAD, quinone)

substrate: coenzyme Q1


substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


assay_conditions_summary: pH 6

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

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


substrate_name: tetramethyl-p-phenylenediamine

substrate: tetramethyl-p-phenylenediamine


substrate_name: ferricyanide

substrate: ferricyanide


organism: Gluconacetobacter diazotrophicus

substrate_name: D-galactose

substrate: D-galactose


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


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


substrate_name: ethanol

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

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

substrate: ethanol


smiles: CCCO


organism: Colletotrichum gloeosporioides

substrate_name: D-xylose

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

substrate: D-xylose


substrate_name: D-glucose

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

substrate: D-glucose


organism: Burkholderia cepacia

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

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

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


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


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

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


substrate_name: lactose

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

substrate: lactose


assay_conditions_summary: pH 6.5; 298.15 K; cofactor FAD

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

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


substrate_name: glucose

assay_conditions_summary: cofactor FAD

substrate: glucose


organism: Aspergillus niger

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


organism: Pyrobaculum aerophilum

substrate_name: maltose

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

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

substrate: maltose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: D-fructose

substrate: D-fructose


organism: Arthrobacter globiformis


substrate_name: N-methylphenazonium methyl sulfate

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

substrate: N-methylphenazonium methyl sulfate


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


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


organism: Pseudomonas taetrolens


substrate_name: sucrose

substrate: sucrose


enzyme_display_name: cyclic alcohol dehydrogenase (quinone)

organism: Gluconobacter frateurii

substrate_name: Cyclopentanol

enzyme: cyclic alcohol dehydrogenase (quinone)

substrate: Cyclopentanol


organism: Aspergillus terreus

proof_lines:
apparent turnover number
apparent KM-value


organism: Mucor circinelloides

assay_conditions_summary: pH 7; 310.15 K; cofactor FAD

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


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


assay_conditions_summary: 313.15 K; cofactor FAD

proof_lines: pH and temperature not specified in the publication


organism: Acinetobacter baumannii


organism: Aspergillus oryzae

assay_conditions_summary: pH 7.4; 310.15 K; cofactor FAD

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


organism: Acidomonas methanolica


organism: Acinetobacter calcoaceticus

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


substrate_name: allose

substrate: allose


organism: Rasamsonia emersonii

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

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


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


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


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


organism: Thermus thermophilus

substrate_name: xylitol

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

substrate: xylitol


substrate_name: mannitol

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

substrate: mannitol


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


substrate_name: methanol

smiles: CO

source_databases_merged: brenda oed

substrate: methanol


substrate_name: D-glucosamine

substrate: D-glucosamine


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


substrate_name: L-arabinose

substrate: L-arabinose


substrate_name: D-galactose

substrate: D-galactose


substrate_name: D-cellobiose

substrate: D-cellobiose


substrate_name: D-glucose 6-phosphate

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

substrate: D-glucose 6-phosphate


substrate_name: D-ribose

substrate: D-ribose


substrate_name: maltotriose

substrate: maltotriose


substrate_name: maltose

substrate: maltose


organism: Thermoascus crustaceus

substrate_name: D-glucose

assay_conditions_summary: pH 7; cofactor FAD

substrate: D-glucose


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

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


enzyme_display_name: quinoprotein glucose dehydrogenase (PQQ, quinone)

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

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

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

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


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

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

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

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

row_label: Y156A / 2-deoxy-D-glucose

enzyme: quinoprotein glucose dehydrogenase (PQQ, quinone)


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

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

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

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

row_label: Y156K / 2-deoxy-D-glucose


substrate_name: alpha-D-lactose

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

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

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

row_label: wild type / alpha-D-lactose

substrate: alpha-D-lactose


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

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

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

row_label: Y156A / alpha-D-lactose


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

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

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

row_label: Y156K / alpha-D-lactose


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

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

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

row_label: wild type / D-cellobiose


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

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

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

row_label: Y156A / D-cellobiose


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

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

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

row_label: Y156K / D-cellobiose


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

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

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

row_label: wild type / D-galactose


enzyme_display_name: Alcohol dehydrogenase (quinone), dehydrogenase subunit

organism: Gluconobacter oxydans (strain 621H)

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

assay_conditions_summary: pH 5

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

raw_value_unit_evidence: Km raw_value=7.7 raw_unit=uM

row_label: G. suboxydans inactive ADH; Q2 column

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


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

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

raw_value_unit_evidence: Km raw_value=13 raw_unit=uM

row_label: G. suboxydans inactive ADH; Q2H2 column

enzyme: Alcohol dehydrogenase (quinone), dehydrogenase subunit


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

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

raw_value_unit_evidence: Km raw_value=170 raw_unit=uM

row_label: G. suboxydans active ADH; Ferricyanide column


enzyme_display_name: Alcohol dehydrogenase (quinone), cytochrome c subunit

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


enzyme: Alcohol dehydrogenase (quinone), cytochrome c subunit

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


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


enzyme_display_name: malate dehydrogenase (quinone)

organism: Plasmodium falciparum

substrate_name: decylubiquinone

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

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

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

row_label: dUQ/decylubiquinone, panel A

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

enzyme: malate dehydrogenase (quinone)

substrate: decylubiquinone


substrate_name: (S)-malate

normalized_value_unit_evidence: Km normalized 5.99 mM.

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

row_label: L-malate, panel B

substrate: (S)-malate


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

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

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

row_label: Y156A / maltose


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

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

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

row_label: Y156K / maltose


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

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

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

row_label: wild type / maltotriose


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

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

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

row_label: Y156A / maltotriose


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

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

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

row_label: Y156K / maltotriose


substrate_name: mannitol

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

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

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

row_label: wild type / mannitol

substrate: mannitol


substrate_name: xylitol

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

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

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

row_label: wild type / xylitol

substrate: xylitol


substrate_name: D-Xylose

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

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

row_label: wild type / D-Xylose

substrate: D-Xylose


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

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

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

row_label: Y156A / D-Xylose


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

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

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

row_label: Y156K / D-Xylose


substrate_name: cellobiose

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

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

row_label: cellobiose

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

substrate: cellobiose


substrate_name: lactose

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

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

row_label: lactose

substrate: lactose


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


substrate_name: L-Arabinose

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

substrate: L-Arabinose


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


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


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


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_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


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


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


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


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


organism: Escherichia coli

substrate_name: pyrroloquinoline quinone

substrate: pyrroloquinoline quinone


substrate_name: D-glucose

substrate: D-glucose


organism: Aspergillus flavus

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.


substrate_name: D-xylose

substrate: D-xylose


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


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


substrate_name: allose

substrate: allose


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


organism: Streptomyces sp.

substrate_name: cholesterol

substrate: cholesterol


enzyme_display_name: (S)-2-hydroxyglutarate dehydrogenase

organism: Homo sapiens

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

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

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

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


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.


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

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


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


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.

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


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)

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

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