enzyme_display_name: Very-long-chain 3-oxoacyl-CoA reductase

organism: Homo sapiens

substrate_name: estrone

column_label: Official OUP Table 1 row '17beta-HSD12', column 'Km (uM)': 3.5 +/- 0.5; Vmax column: 56 +/- 7

raw_value_unit_evidence: Table 1 row 17beta-HSD12: Km raw_value=3.5 +/- 0.5 uM; Vmax=56 +/- 7 nmol product/h/10^6 cells

table_label: OUP full text Table 1. Kinetic parameters of human types 1, 7, and 12 17beta-HSD

enzyme: Very-long-chain 3-oxoacyl-CoA reductase

substrate: estrone


organism: Weissella confusa

source_db: oed

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

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

data_origin: experimental

status: unverified

source: oed


organism: Methanocaldococcus jannaschii

substrate_name: glyoxylate

source_db: brenda

kcat_display: Not reported

kcat_over_km_display: Not reported

sequence_source: multiple

assay_conditions_summary: pH 8

proof_lines:
glyoxylate
lower efficiency

source_databases_merged: brenda uniprot

substrate: glyoxylate

source: brenda


organism: Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)

substrate_name: NAD(+)

source_db: uniprot

assay_conditions_summary: cofactor NAD+

substrate: NAD(+)

source: uniprot


enzyme_display_name: L-sulfolactate dehydrogenase

organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

substrate_name: oxopropanedioate (in the presence of NADH)

assay_conditions_summary: cofactor NADH

proof_lines:
glyoxylate
oxo propanedioic acid
lower efficiency

enzyme: L-sulfolactate dehydrogenase


substrate_name: (2R)-3-sulfolactate (in the presence of NAD(+))

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

assay_conditions_summary: cofactor NADP+


organism: Streptomyces avermitilis

substrate_name: 1-deoxy-11beta-hydroxypentalenic acid

substrate: 1-deoxy-11beta-hydroxypentalenic acid


enzyme_display_name: (1R,2S)-ephedrine 1-dehydrogenase

organism: Arthrobacter sp. TS-15

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

enzyme: (1R,2S)-ephedrine 1-dehydrogenase


km_display: Not reported


substrate_name: isatin

substrate: isatin


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


substrate_name: NADH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

substrate: NADH


enzyme_display_name: phosphogluconate dehydrogenase (NAD(+)-dependent, decarboxylating)

organism: Gluconobacter oxydans


enzyme_display_name: 5'-hydroxyaverantin dehydrogenase

organism: Aspergillus parasiticus

verification_status: verified

assay_conditions_summary: pH 7.5; buffer 60 mM potassium phosphate

column_label: Results prose reports Km and Vmax of the enzyme for HAVN as 83 uM and 2.3 umol mg protein^-1 min^-1.

raw_value_unit_evidence: Km raw_value=83 raw_unit=uM

row_label: partially purified HAVN dehydrogenase from Aspergillus parasiticus NIAH-26 / HAVN substrate

table_label: PMC full text PMID 14602595 HAVN dehydrogenase kinetic prose

enzyme: 5'-hydroxyaverantin dehydrogenase

status: verified


enzyme_display_name: UniProt A0A545BBS8

organism: Arthrobacter sp.

source_db: skid

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt A0A545BBS8

source: skid


enzyme_display_name: pseudoephedrine dehydrogenase

substrate_name: NAD+

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NAD+

column_label: Table 1 explicitly reports Km 3.4 +/- 0.26 mM and kcat 9.22 +/- 0.23 s^-1 for PseDH with NAD+.

row_label: PseDH / NAD+

table_label: Table 1: Kinetic parameters of ephedrine oxidation catalyzed by PseDH and EDH

enzyme: pseudoephedrine dehydrogenase

substrate: NAD+


substrate_name: (S,R)-(+)-ephedrine

column_label: Table 1 explicitly reports Km 0.33 +/- 0.03 mM and kcat 1.45 +/- 0.04 s^-1 for PseDH with (S,R)-(+)-ephedrine.

row_label: PseDH / (S,R)-(+)-Ephedrine

substrate: (S,R)-(+)-ephedrine


organism: Arthrobacter sp. Cr-7

substrate_name: Isopyridoxal

substrate: Isopyridoxal


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


substrate_name: ethyl 2-chlorobenzoylacetate

substrate: ethyl 2-chlorobenzoylacetate


substrate_name: methyl benzoylformate

substrate: methyl benzoylformate


enzyme_display_name: D-apiose dehydrogenase

organism: Klebsiella aerogenes

substrate_name: D-apiitol

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

enzyme: D-apiose dehydrogenase

substrate: D-apiitol


substrate_name: D-apiose

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

substrate: D-apiose


substrate_name: (R,R)-(-)-pseudoephedrine

substrate: (R,R)-(-)-pseudoephedrine


enzyme_display_name: plant 3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating)

organism: Arabidopsis thaliana

proof_lines: isoform 3betaHSD/D2, at 30°C, pH not specified in the publication


proof_lines: isoform 3betaHSD/D1, at 30°C, pH not specified in the publication

enzyme: plant 3beta-hydroxysteroid-4alpha-carboxylate 3-dehydrogenase (decarboxylating)


protein_accession_database: NCBI Protein

sequence_source: GenBank accession TQS88919 (pseudoephedrine dehydrogenase)


verification_status: corrected

assay_conditions_summary: pH 7.8; cofactor NAD+

column_label: Table 1 explicitly reports Km 0.263 +/- 0.03 mM and kcat 3.77 +/- 0.10 s^-1 for PseDH with (S,S)-(+)-pseudoephedrine.

row_label: PseDH / (S,S)-(+)-Pseudoephedrine

status: corrected


organism: Rhizobium rhizogenes (strain K84 / ATCC BAA-868)


organism: Nepeta racemosa

substrate_name: NAD(+) (in the presence of cis-trans-nepetalactol at pH 8.0 and 25 degrees Celsius)

proof_lines: kcat is 0.148 sec(-1) with cis-trans-nepetalactol as substrate (in the presence of NAD(+) at pH 8.0 and 25 degrees Celsius). kcat is 0.32 sec(-1) with cis-cis-nepetalactol as substrate (in the presence of NAD(+) at pH 8.0 and 25 degrees Cel


enzyme_display_name: D-apionate oxidoisomerase

organism: Blautia hydrogenotrophica (strain DSM 10507 / JCM 14656 / S5a33)

substrate_name: D-apionate

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

enzyme: D-apionate oxidoisomerase

substrate: D-apionate


organism: Paraburkholderia graminis (strain ATCC 700544 / DSM 17151 / LMG 18924 / NCIMB 13744 / C4D1M)


organism: Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1)

column_label: Supplementary Table 4 page 5 row F8GV06/CNE_BB1p11570 under Substrate D-Apionate has KM [mM] = 0.27 +/- 0.03 and kcat [s-1] = 0.49 +/- 0.01.

raw_value_unit_evidence: KM raw_value=0.27 raw_unit=mM; kcat raw_value=0.49 raw_unit=s-1.

table_label: Supplementary Table 4, Kinetic parameters for D-apiose dehydrogenase, D-apionate oxidoisomerase, and hydroxypyruvate reductase


organism: Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)


enzyme_display_name: 3alpha-hydroxysteroid 3-dehydrogenase

organism: Comamonas testosteroni

assay_conditions_summary: pH 10.5; 283.15 K; cofactor NAD+

row_label: 2-decalol at 40 C with 3alpha-HSD/CR

table_label: Results text / Supplementary kinetic tables S2-S3

enzyme: 3alpha-hydroxysteroid 3-dehydrogenase


enzyme_display_name: D-galacturonate reductase

organism: Hypocrea jecorina

substrate_name: NADP(+)

proof_lines:
Hypocrea jecorina
d-galacturonic acid reductase
enzyme kinetics

enzyme: D-galacturonate reductase

substrate: NADP(+)


enzyme_display_name: Glucose 1-dehydrogenase

organism: Saccharolobus solfataricus

substrate_name: NADP(+) (at 70 degrees Celsius and pH 8)

assay_conditions_summary: 343.15 K; cofactor NADP+

column_label: Table 4 / Apparent Km values for substrates and coenzymes of glucose dehydrogenase from Sulfolobus solfataricus; Glucose-NADP+ row; coenzyme Km column = 0.03 mM.

normalized_value_unit_evidence: Km=0.03 mM directly reported in Table 4; no unit conversion required.

raw_value_unit_evidence: Glucose-NADP+ / coenzyme Km column reports coenzyme Km = 0.03 mM.

row_label: Glucose-NADP+ / coenzyme Km column

enzyme: Glucose 1-dehydrogenase


enzyme_display_name: D-chiro-inositol 1-dehydrogenase

organism: Thermotoga maritima

proof_lines:
Thermotoga maritima
myo-inositol
myo-inositol dehydrogenase IolG

enzyme: D-chiro-inositol 1-dehydrogenase


enzyme_display_name: aldose 1-dehydrogenase [NAD(P)(+)]

substrate_name: L-Arabinose

enzyme: aldose 1-dehydrogenase [NAD(P)(+)]

substrate: L-Arabinose


organism: Homo sapiens


enzyme_display_name: Aldo-keto reductase family 1 member A1

organism: Mus musculus

substrate_name: D-glucuronate

proof_lines:
D-glucuronate
L-gulonate
aldehyde reductase

enzyme: Aldo-keto reductase family 1 member A1

substrate: D-glucuronate


enzyme_display_name: L-gulonate 5-dehydrogenase

organism: Halomonas elongata

substrate_name: L-gulonate

column_label: Table 1 row HeGulDH(CsGulDH) / L-gulonate gives kcat 1.8 s^-1.

raw_value_unit_evidence: kcat raw_value=1.8 s^-1 raw_unit=s^-1

row_label: HeGulDH / CsGulDH enzyme row with L-gulonate

table_label: Official PMC full-text Table 1: Kinetics of Enzymes Encoded by the CsManD Operon

enzyme: L-gulonate 5-dehydrogenase

substrate: L-gulonate


organism: Methanocaldococcus jannaschii

assay_conditions_summary: pH 9.5; 343.15 K; buffer hydrazine/glycine pH 9; cofactor NADP+

column_label: Table 2 reports (S)-Sulfolactate with NADP+ under MJ0490 (MdhII): Km 4.6 mM, Vmax 3 U/mg, Vmax/Km 1 min^-1 mg^-1.

raw_value_unit_evidence: Km raw_value=4.6 raw_unit=mM

row_label: (S)-Sulfolactate / NADP+ / MJ0490 (MdhII)

table_label: Table 2 - NAD+ and NADP+ dependent enzymatic oxidations of alpha-hydroxy acids by MJ1425/MJ0490/MF malate dehydrogenases


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

organism: Ignisphaera aggregans

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


substrate_name: pyruvate

assay_conditions_summary: pH 6.6; cofactor NADPH

substrate: pyruvate


organism: Rhodococcus sp. (strain AD45)

column_label: Primary-paper PMC Results prose reports HGMB oxidation followed Michaelis-Menten kinetics and the Km for HGMB was 1.4 mM.

raw_value_unit_evidence: HGMB Km 1.4 mM

row_label: HGMB substrate Km sentence

table_label: Results prose: Purification of the HGMB-dependent dehydrogenase


organism: Mediterraneibacter gnavus

assay_conditions_summary: pH 7


enzyme_display_name: D-altritol 5-dehydrogenase

organism: Agrobacterium fabrum

substrate_name: D-Altritol

column_label: PMC4661409 HTML Table 3 row Atu ZnD / D-Altritol columns kcat, Km, and kcat/Km report 1.9 +/- 0.03 s^-1, 1.4 +/- 0.10 mM, and 1.4 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=1.9 s^-1; Km normalized_value=1.4 mM; paper-rounded kcat/Km normalized_value=1.4 s^-1 mM^-1. CatLog stores computed kcat/Km=1.3571428571428572 from the kcat and Km cells.

raw_value_unit_evidence: Table 3 reports Atu ZnD with D-Altritol: kcat raw_value=1.9 s^-1, Km raw_value=1.4 mM, kcat/Km raw_value=1.4 x 10^3 M^-1 s^-1.

row_label: Atu ZnD / D-Altritol

table_label: PMC4661409 HTML Table 3

enzyme: D-altritol 5-dehydrogenase

substrate: D-Altritol


organism: Sulfobacillus thermosulfidooxidans (strain DSM 9293 / VKM B-1269 / AT-1)

smiles: CC(C(C)O)O


enzyme_display_name: sulfoacetaldehyde reductase (NADH)

organism: Bifidobacterium catenulatum subsp. kashiwanohense

substrate_name: NADP+

assay_conditions_summary: pH 10; 303.15 K; cofactor NADP+

proof_lines: pH 10.0, 30°C, recombinant wild-type enzyme

enzyme: sulfoacetaldehyde reductase (NADH)

substrate: NADP+


substrate_name: isethionate

substrate: isethionate


assay_conditions_summary: pH 10

proof_lines: pH 10, temperature not specified in the publication


substrate_name: NAD+

assay_conditions_summary: pH 10; 303.15 K; cofactor NAD+

substrate: NAD+


assay_conditions_summary: pH 10; cofactor NAD+


substrate_name: NADH

assay_conditions_summary: pH 10; 303.15 K; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 7.5; cofactor NADH

proof_lines: pH 7.5, temperature not specified in the publication


substrate_name: NADPH

assay_conditions_summary: pH 10; 303.15 K; cofactor NADPH

substrate: NADPH


enzyme_display_name: L-fucose dehydrogenase

organism: Burkholderia multivorans (strain ATCC 17616 / 249)

proof_lines: kcat is 10 sec(-1) with L-fucose as substrate. kcat is 21.0 sec(-1) with D-arabinose as substrate. kcat is 11 sec(-1) with L-galactose as substrate. kcat is 26 sec(-1) with 4-deoxy-L-fucose as substrate. kcat is 11 sec(-1) with NADP(+) as s

enzyme: L-fucose dehydrogenase


organism: Xanthomonas campestris pv. campestris


organism: Burkholderia multivorans

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

column_label: Table 3 (Catalytic constants for BmulJ_04919 at pH 8.0) prints the column heads `Substrate`, `kcat (s-1)`, `Km (uM)` and `kcat/Km (M-1 s-1)`. In the substrate row `NAD+` the printed cells are kcat 5 +/- 1, Km 28 +/- 4 and kcat/Km 5.3 (0.1) x 10^5.

normalized_value_unit_evidence: Km: printed Table 3 cell 28 uM; 1 uM is 1/1000 mM, so 28 / 1000 = 0.028 mM, which is the value the catalog carries. kcat: printed Table 3 cell 5 s^-1; the printed turnover column head is kcat (s-1), already the canonical unit, so no unit conversion applies and the paper value is 5.0 s^(-1), which the catalog also carries. kcat/Km: printed Table 3 cell 5.3 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.3 x 10^5 / 1000 = 530.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of this line's own two printed component cells is 5 / 0.028 = 178.57142857142856 s^-1 mM^-1, while the paper's own printed catalytic-efficiency cell for the same line is 530.0 s^-1 mM^-1, an independently fitted primary figure carried at the precision of the printed column.

raw_value_unit_evidence: Table 3 (Catalytic constants for BmulJ_04919 at pH 8.0), substrate row `NAD+`: Km = 28 uM; kcat = 5 s^-1; printed kcat/Km = 5.3 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate row `NAD+`

table_label: Table 3: Catalytic constants for BmulJ_04919 at pH 8.0 (Biochemistry 2013, 52(1):239-253)


substrate_name: beta-L-fucose

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

column_label: Table 3 (Catalytic constants for BmulJ_04919 at pH 8.0) prints the column heads `Substrate`, `kcat (s-1)`, `Km (uM)` and `kcat/Km (M-1 s-1)`. In the substrate row `L-fucose (25)` the printed cells are kcat 10 +/- 0.3, Km 6.2 +/- 0.8 and kcat/Km 1.5 (0.2) x 10^6.

normalized_value_unit_evidence: Km: printed Table 3 cell 6.2 uM; 1 uM is 1/1000 mM, so 6.2 / 1000 = 0.0062 mM, which is the value the catalog carries. kcat: printed Table 3 cell 10 s^-1; the printed turnover column head is kcat (s-1), already the canonical unit, so no unit conversion applies and the paper value is 10.0 s^(-1), which the catalog also carries. kcat/Km: printed Table 3 cell 1.5 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.5 x 10^6 / 1000 = 1500.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of this line's own two printed component cells is 10 / 0.0062 = 1612.9032258064517 s^-1 mM^-1, while the paper's own printed catalytic-efficiency cell for the same line is 1500.0 s^-1 mM^-1, an independently fitted primary figure carried at the precision of the printed column.

raw_value_unit_evidence: Table 3 (Catalytic constants for BmulJ_04919 at pH 8.0), substrate row `L-fucose (25)`: Km = 6.2 uM; kcat = 10 s^-1; printed kcat/Km = 1.5 x 10^6 M^-1 s^-1.

row_label: Table 3, substrate row `L-fucose (25)`

substrate: beta-L-fucose


substrate_name: L-galactose

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

column_label: Table 3 (Catalytic constants for BmulJ_04919 at pH 8.0) prints the column heads `Substrate`, `kcat (s-1)`, `Km (uM)` and `kcat/Km (M-1 s-1)`. In the substrate row `L-galactose (26)` the printed cells are kcat 11 +/- 0.5, Km 285 +/- 36 and kcat/Km 3.7 (0.3) x 10^4.

normalized_value_unit_evidence: Km: printed Table 3 cell 285 uM; 1 uM is 1/1000 mM, so 285 / 1000 = 0.285 mM, which is the value the catalog carries. kcat: printed Table 3 cell 11 s^-1; the printed turnover column head is kcat (s-1), already the canonical unit, so no unit conversion applies and the paper value is 11.0 s^(-1), which the catalog also carries. kcat/Km: printed Table 3 cell 3.7 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.7 x 10^4 / 1000 = 37.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of this line's own two printed component cells is 11 / 0.285 = 38.59649122807018 s^-1 mM^-1, while the paper's own printed catalytic-efficiency cell for the same line is 37.0 s^-1 mM^-1, an independently fitted primary figure carried at the precision of the printed column.

raw_value_unit_evidence: Table 3 (Catalytic constants for BmulJ_04919 at pH 8.0), substrate row `L-galactose (26)`: Km = 285 uM; kcat = 11 s^-1; printed kcat/Km = 3.7 x 10^4 M^-1 s^-1.

row_label: Table 3, substrate row `L-galactose (26)`

substrate: L-galactose


column_label: Table 3 (Catalytic constants for BmulJ_04919 at pH 8.0) prints the column heads `Substrate`, `kcat (s-1)`, `Km (uM)` and `kcat/Km (M-1 s-1)`. In the substrate row `NADP+` the printed cells are kcat 11 +/- 0.2, Km 4.0 +/- 0.5 and kcat/Km 3.0 (0.4) x 10^6.

normalized_value_unit_evidence: Km: printed Table 3 cell 4.0 uM; 1 uM is 1/1000 mM, so 4.0 / 1000 = 0.004 mM, which is the value the catalog carries. kcat: printed Table 3 cell 11 s^-1; the printed turnover column head is kcat (s-1), already the canonical unit, so no unit conversion applies and the paper value is 11.0 s^(-1), which the catalog also carries. kcat/Km: printed Table 3 cell 3.0 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.0 x 10^6 / 1000 = 3000.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of this line's own two printed component cells is 11 / 0.004 = 2750.0 s^-1 mM^-1, while the paper's own printed catalytic-efficiency cell for the same line is 3000.0 s^-1 mM^-1, an independently fitted primary figure carried at the precision of the printed column.

raw_value_unit_evidence: Table 3 (Catalytic constants for BmulJ_04919 at pH 8.0), substrate row `NADP+`: Km = 4.0 uM; kcat = 11 s^-1; printed kcat/Km = 3.0 x 10^6 M^-1 s^-1.

row_label: Table 3, substrate row `NADP+`


substrate_name: D-arabinose

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

column_label: Table 3 (Catalytic constants for BmulJ_04919 at pH 8.0) prints the column heads `Substrate`, `kcat (s-1)`, `Km (uM)` and `kcat/Km (M-1 s-1)`. In the substrate row `D-arabinose (29)` the printed cells are kcat 21.0 +/- 0.1, Km 94 +/- 3 and kcat/Km 2.3 (0.1) x 10^5.

normalized_value_unit_evidence: Km: printed Table 3 cell 94 uM; 1 uM is 1/1000 mM, so 94 / 1000 = 0.094 mM, which is the value the catalog carries. kcat: printed Table 3 cell 21.0 s^-1; the printed turnover column head is kcat (s-1), already the canonical unit, so no unit conversion applies and the paper value is 21.0 s^(-1), which the catalog also carries. kcat/Km: printed Table 3 cell 2.3 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.3 x 10^5 / 1000 = 230.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of this line's own two printed component cells is 21.0 / 0.094 = 223.40425531914894 s^-1 mM^-1, while the paper's own printed catalytic-efficiency cell for the same line is 230.0 s^-1 mM^-1, an independently fitted primary figure carried at the precision of the printed column.

raw_value_unit_evidence: Table 3 (Catalytic constants for BmulJ_04919 at pH 8.0), substrate row `D-arabinose (29)`: Km = 94 uM; kcat = 21.0 s^-1; printed kcat/Km = 2.3 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate row `D-arabinose (29)`

substrate: D-arabinose


column_label: Table 3 (Catalytic constants for BmulJ_04919 at pH 8.0) prints the column heads `Substrate`, `kcat (s-1)`, `Km (uM)` and `kcat/Km (M-1 s-1)`. In the substrate row `4-deoxy-L-fucose (47)` the printed cells are kcat 26 +/- 1, Km 786 +/- 92 and kcat/Km 4.0 (0.1) x 10^4.

normalized_value_unit_evidence: Km: printed Table 3 cell 786 uM; 1 uM is 1/1000 mM, so 786 / 1000 = 0.786 mM, which is the value the catalog carries. kcat: printed Table 3 cell 26 s^-1; the printed turnover column head is kcat (s-1), already the canonical unit, so no unit conversion applies and the paper value is 26.0 s^(-1), which the catalog also carries. kcat/Km: printed Table 3 cell 4.0 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.0 x 10^4 / 1000 = 40.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of this line's own two printed component cells is 26 / 0.786 = 33.07888040712468 s^-1 mM^-1, while the paper's own printed catalytic-efficiency cell for the same line is 40.0 s^-1 mM^-1, an independently fitted primary figure carried at the precision of the printed column.

raw_value_unit_evidence: Table 3 (Catalytic constants for BmulJ_04919 at pH 8.0), substrate row `4-deoxy-L-fucose (47)`: Km = 786 uM; kcat = 26 s^-1; printed kcat/Km = 4.0 x 10^4 M^-1 s^-1.

row_label: Table 3, substrate row `4-deoxy-L-fucose (47)`


smiles: O=CCS(=O)(=O)O

column_label: Table 2; row Sulfoacetaldehyde; column kcat (s^-1) raw value 22.83; column KM (mM) raw value 0.50; column kcat/KM (M^-1 s^-1) raw value 4.61 x 10^4

normalized_value_unit_evidence: kcat normalized_value=22.83 normalized_unit=s^-1; KM normalized_value=0.50 normalized_unit=mM; kcat/KM normalized_value=46.1 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=22.83 raw_unit=s^-1; KM raw_value=0.50 raw_unit=mM; kcat/KM raw_value=4.61 x 10^4 raw_unit=M^-1*s^-1

row_label: Sulfoacetaldehyde

table_label: Table 2. Enzyme kinetic parameters


smiles: O=S(=O)(O)CCO

column_label: Table 2; row Isethionate; column kcat (s^-1) raw value 0.97; column KM (mM) raw value 4.44; column kcat/KM (M^-1 s^-1) raw value 2.18 x 10^2

normalized_value_unit_evidence: kcat normalized_value=0.97 normalized_unit=s^-1; KM normalized_value=4.44 normalized_unit=mM; kcat/KM normalized_value=0.218 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.97 raw_unit=s^-1; KM raw_value=4.44 raw_unit=mM; kcat/KM raw_value=2.18 x 10^2 raw_unit=M^-1*s^-1

row_label: Isethionate


column_label: Table 2; row NAD+; column kcat (s^-1) raw value 1.30; column KM (mM) raw value 0.08; column kcat/KM (M^-1 s^-1) raw value 1.58 x 10^4

normalized_value_unit_evidence: kcat normalized_value=1.30 normalized_unit=s^-1; KM normalized_value=0.08 normalized_unit=mM; kcat/KM normalized_value=15.8 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.30 raw_unit=s^-1; KM raw_value=0.08 raw_unit=mM; kcat/KM raw_value=1.58 x 10^4 raw_unit=M^-1*s^-1

row_label: NAD+


column_label: Table 2; row NADH; column kcat (s^-1) raw value 18.67; column KM (mM) raw value 0.06; column kcat/KM (M^-1 s^-1) raw value 3.01 x 10^5

normalized_value_unit_evidence: kcat normalized_value=18.67 normalized_unit=s^-1; KM normalized_value=0.06 normalized_unit=mM; kcat/KM normalized_value=301 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=18.67 raw_unit=s^-1; KM raw_value=0.06 raw_unit=mM; kcat/KM raw_value=3.01 x 10^5 raw_unit=M^-1*s^-1

row_label: NADH


column_label: Table 2; row NADP+; column kcat (s^-1) raw value 0.80; column KM (mM) raw value 0.77; column kcat/KM (M^-1 s^-1) raw value 1.03 x 10^3

normalized_value_unit_evidence: kcat normalized_value=0.80 normalized_unit=s^-1; KM normalized_value=0.77 normalized_unit=mM; kcat/KM normalized_value=1.03 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.80 raw_unit=s^-1; KM raw_value=0.77 raw_unit=mM; kcat/KM raw_value=1.03 x 10^3 raw_unit=M^-1*s^-1

row_label: NADP+


column_label: Table 2; row NADPH; column kcat (s^-1) raw value 18.99; column KM (mM) raw value 0.73; column kcat/KM (M^-1 s^-1) raw value 2.62 x 10^4

normalized_value_unit_evidence: kcat normalized_value=18.99 normalized_unit=s^-1; KM normalized_value=0.73 normalized_unit=mM; kcat/KM normalized_value=26.2 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=18.99 raw_unit=s^-1; KM raw_value=0.73 raw_unit=mM; kcat/KM raw_value=2.62 x 10^4 raw_unit=M^-1*s^-1

row_label: NADPH


enzyme_display_name: L-threonate 2-dehydrogenase

organism: Cupriavidus necator

substrate_name: L-threonate

column_label: Table 1; row Q0KBC7 (ReLtnD) / l-Threonate, NAD+; columns kcat (s^-1), KM (mM), kcat/KM (M^-1 s^-1); cells 29, 0.35, 8.5 x 10^4; normalized kcat/Km 85 s^-1 mM^-1

normalized_value_unit_evidence: kcat=29 s^-1; Km=0.35 mM; kcat/Km=85 s^-1 mM^-1 (explicit table value converted from M^-1 s^-1)

raw_value_unit_evidence: Q0KBC7 (ReLtnD) / l-Threonate, NAD+: kcat=29 s^-1; KM=0.35 mM; kcat/KM=8.5 x 10^4 M^-1 s^-1

row_label: Q0KBC7 (ReLtnD) / l-Threonate, NAD+

table_label: Table 1. Selected kinetic parameters for DtnK, PdxA2, LtnD, and DenD

enzyme: L-threonate 2-dehydrogenase

substrate: L-threonate


enzyme_display_name: A-factor type gamma-butyrolactone 1'-reductase (1S-forming)

organism: Streptomyces virginiae

substrate_name: 6-dehydro-Virginiae butanolide-A

assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: Characterization prose reports the K_m value for (+/-)-6-dehydro-VB-A as 11.1 uM; 11.1 uM equals 0.0111 mM.

raw_value_unit_evidence: Km raw_value=11.1 raw_unit=uM

row_label: purified rBarS1 / (+/-)-6-dehydro-VB-A

table_label: PMC full text PMID 12193632 rBarS1 characterization prose

substrate: 6-dehydro-Virginiae butanolide-A


enzyme_display_name: D-erythronate 2-dehydrogenase

substrate_name: D-erythronate

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

column_label: Table 1; row Q0KBD2 (ReDenD), d-Erythronate, NAD+; columns kcat (s^-1), KM (mM), kcat/KM (M^-1 s^-1); cells 19, 0.59, 3.3 x 10^4; normalized kcat/Km 33 s^-1 mM^-1

normalized_value_unit_evidence: kcat=19 s^-1; Km=0.59 mM; kcat/Km=33 s^-1 mM^-1 (explicit table value converted from 3.3 x 10^4 M^-1 s^-1)

raw_value_unit_evidence: Q0KBD2 (ReDenD), d-Erythronate, NAD+: kcat=19 s^-1; KM=0.59 mM; kcat/KM=3.3 x 10^4 M^-1 s^-1

row_label: Q0KBD2 (ReDenD) / d-Erythronate, NAD+

enzyme: D-erythronate 2-dehydrogenase

substrate: D-erythronate


organism: Pectobacterium atrosepticum

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

column_label: Table 1; row Q6CZ26 (PaLtnD), l-Threonate, NAD+; columns kcat (s^-1), KM (mM), kcat/KM (M^-1 s^-1); cells 54, 0.13, 4.1 x 10^5; normalized kcat/Km 410 s^-1 mM^-1

normalized_value_unit_evidence: kcat=54 s^-1; Km=0.13 mM; kcat/Km=410 s^-1 mM^-1 (explicit table value converted from 4.1 x 10^5 M^-1 s^-1)

raw_value_unit_evidence: Q6CZ26 (PaLtnD), l-Threonate, NAD+: kcat=54 s^-1; KM=0.13 mM; kcat/KM=4.1 x 10^5 M^-1 s^-1

row_label: Q6CZ26 (PaLtnD) / l-Threonate, NAD+


enzyme_display_name: Lactate dehydrogenase (NAD(+),ferredoxin) subunit LctD

organism: Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)

substrate_name: D-lactate

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

assay_conditions_summary: cofactor NAD+

column_label: Weghoff, Bertsch, and Muller, Environmental Microbiology 2015, Results prose on LDH/Etf NAD+ reduction; D-lactate Km raw value 3.6 mM.

normalized_value_unit_evidence: D-lactate Km is reported directly as 3.6 mM, matching exported Km 3.6 mM.

raw_value_unit_evidence: Official Wiley Full Access Results prose states that the growth substrates had Km values of 3.6 mM for D-lactate and 112 mM for L-lactate.

row_label: A. woodii LDH/Etf substrate-affinity prose; D-lactate

table_label: Results prose, LDH/Etf NAD+ reduction section

substrate: D-lactate


substrate_name: L-lactate

column_label: Weghoff, Bertsch, and Muller, Environmental Microbiology 2015, Results prose on LDH/Etf NAD+ reduction; L-lactate Km raw value 112 mM.

normalized_value_unit_evidence: L-lactate Km is reported directly as 112 mM, matching exported Km 112.0 mM.

row_label: A. woodii LDH/Etf substrate-affinity prose; L-lactate

enzyme: Lactate dehydrogenase (NAD(+),ferredoxin) subunit LctD

substrate: L-lactate


enzyme_display_name: Lactate dehydrogenase (NAD(+),ferredoxin) subunit LctB

substrate_name: NAD(+)

substrate: NAD(+)


enzyme_display_name: polyprenol dehydrogenase [NAD(P)H]

organism: Cricetulus griseus

substrate_name: ditrans,polycis-polyprenol

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

proof_lines:
pH 8.0, 37°C, cosubstrate: NAD+
pH 8.0, 37°C, cosubstrate: NADPH

enzyme: polyprenol dehydrogenase [NAD(P)H]

substrate: ditrans,polycis-polyprenol


assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

proof_lines: pH 8.0, 37°C, cosubstrate: ditrans,polycis-polyprenol


assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+


assay_conditions_summary: pH 8; 310.15 K; cofactor NADH


enzyme_display_name: Polyprenol dehydrogenase

organism: Homo sapiens

substrate_name: NADP(+) (with 4 uM of polyprenol)

proof_lines: kcat is 0.44 sec(-1) with polyprenol in presence of NAD(+) (PubMed:38821050). kcat is 0.49 sec(-1) with polyprenol in presence of NADP(+) (PubMed:38821050).

enzyme: Polyprenol dehydrogenase

substrate: NADP(+) (with 4 uM of polyprenol)


substrate_name: NAD(+) (with 4 uM of polyprenol)

substrate: NAD(+) (with 4 uM of polyprenol)


organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

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

assay_conditions_summary: pH 8.5; cofactor NAD+

column_label: Primary PMC HTML Table 3 row IPMDH_Mj, beta-Isopropylmalate group, K_m (uM) column = 24 +/- 3.

normalized_value_unit_evidence: Normalized paper Km: 24 uM = 0.024 mM, matching export Km 0.024 mM.

raw_value_unit_evidence: Table 3 row IPMDH_Mj reports beta-Isopropylmalate K_m 24 +/- 3 uM and kcat/Km 8.8 x 10^4 M^-1 s^-1.

row_label: IPMDH_Mj row; beta-Isopropylmalate K_m column

table_label: Table 3. Kinetic parameters for IPMDH homologs


substrate_name: D-malate

column_label: Primary PMC HTML Table 3 row IPMDH_Mj, d-Malate group, K_m (uM) column = 410 +/- 40.

normalized_value_unit_evidence: Normalized paper Km: 410 uM = 0.410 mM, matching export Km 0.41000000000000003 mM.

raw_value_unit_evidence: Table 3 row IPMDH_Mj reports d-Malate K_m 410 +/- 40 uM and kcat/Km 1.4 x 10^4 M^-1 s^-1.

row_label: IPMDH_Mj row; d-Malate K_m column

substrate: D-malate


enzyme_display_name: (-)-trans-carveol dehydrogenase

organism: Rhodococcus erythropolis

enzyme: (-)-trans-carveol dehydrogenase


enzyme_display_name: Sulfoacetaldehyde reductase

organism: Bilophila wadsworthia (strain 3_1_6)

substrate_name: sulfoacetaldehyde

assay_conditions_summary: cofactor NADH

proof_lines:
Bilophila wadsworthia
SarD
sulfoacetaldehyde reductase

enzyme: Sulfoacetaldehyde reductase

substrate: sulfoacetaldehyde


organism: Arabidopsis thaliana

column_label: Figure 2 defines compound [2] as 4alpha-carboxy-5alpha-cholest-7-en-3beta-ol; Table II reports the Wild type row under the Km, [2] column as 0.13 +/- 0.01 mM.

normalized_value_unit_evidence: Km central normalized_value=0.13 normalized_unit=mM.

raw_value_unit_evidence: Table II reports Km, [2] raw_value=0.13 +/- 0.01 raw_unit=mM for the wild-type enzyme.

row_label: Wild type Arabidopsis 3betaHSD/D

table_label: PMC2663740 Table II


enzyme_display_name: Glyoxylate/succinic semialdehyde reductase 1

substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: succinate semialdehyde

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

enzyme: Glyoxylate/succinic semialdehyde reductase 1

substrate: succinate semialdehyde


substrate_name: NADPH (in the presence of glyoxylate as cosubstrate)


enzyme_display_name: sulfolactaldehyde 3-reductase

organism: Escherichia coli

substrate_name: NADH

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

mutation_type: substitution

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

proof_lines: enzyme mutant T124G, pH and temperature not specified in the publication

enzyme: sulfolactaldehyde 3-reductase

substrate: NADH


proof_lines: enzyme mutant R123G, pH and temperature not specified in the publication


proof_lines: enzyme mutant G122S, pH and temperature not specified in the publication


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


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: 3alpha-hydroxy bile acid-CoA-ester 3-dehydrogenase

organism: [Clostridium] scindens

substrate_name: NADP+

assay_conditions_summary: pH 8.7; 310.15 K; cofactor NADP+

proof_lines: wild type enzyme isoform BaiA2, at pH 8.7 and 37°C

proof_lines: wild type enzyme isoform BaiA1, at pH 8.7 and 37°C

substrate: NADP+


proof_lines: mutantE42A of isoform BaiA2, at pH 8.7 and 37°C

proof_lines: mutant E42A of isoform BaiA2, at pH 8.7 and 37°C

enzyme: 3alpha-hydroxy bile acid-CoA-ester 3-dehydrogenase


substrate_name: chenodeoxycholic acid

substrate: chenodeoxycholic acid


substrate_name: NAD+

assay_conditions_summary: pH 8.7; 310.15 K; cofactor NAD+

substrate: NAD+


substrate_name: cholic acid

substrate: cholic acid


assay_conditions_summary: pH 8.7; 310.15 K; cofactor CoA


substrate_name: glycocholic acid

substrate: glycocholic acid


substrate_name: taurocholic acid

substrate: taurocholic acid


substrate_name: deoxycholoyl-CoA

substrate: deoxycholoyl-CoA


substrate_name: choloyl-CoA

substrate: choloyl-CoA


substrate_name: lithocholoyl-CoA

substrate: lithocholoyl-CoA


substrate_name: chenodeoxycholoyl-CoA

substrate: chenodeoxycholoyl-CoA


enzyme_display_name: Peroxisomal multifunctional enzyme type 2

organism: Drosophila melanogaster

substrate_name: (2E)-butenoyl-CoA (at 22 degrees Celsius)

assay_conditions_summary: cofactor CoA

proof_lines: Catalytic efficiency is similar using full-length protein or the individual (3R)-hydroxyacyl-CoA dehydrogenase and enoyl-CoA hydratase 2 domains in a 1:1 mixture.


substrate_name: (2E)-hexenoyl-CoA (at 22 degrees Celsius)

enzyme: Peroxisomal multifunctional enzyme type 2


substrate_name: (2E)-decenoyl-CoA (at 22 degrees Celsius)


enzyme_display_name: succinic semialdehyde reductase

organism: Mus musculus

assay_conditions_summary: pH 6.6; 298.15 K; cofactor NADPH

column_label: Table 1 row 2-CBA; columns Km (uM), Kcat (min^-1), and Kcat/Km (min^-1 M^-1).

raw_value_unit_evidence: Table 1 row 2-CBA: Km 16 uM; Kcat 78 min^-1; Kcat/Km 4.86e+06 min^-1 M^-1.

table_label: Table 1, Apparent kinetic constants for mouse AKR7A5 for aldehyde and diketone substrates

enzyme: succinic semialdehyde reductase


column_label: Table 1 row 2-NBA; columns Km (uM), Kcat (min^-1), and Kcat/Km (min^-1 M^-1).

raw_value_unit_evidence: Table 1 row 2-NBA: Km 460 uM; Kcat 75 min^-1; Kcat/Km 1.63e+05 min^-1 M^-1.


column_label: PDF page 4 Table 1 row 9,10-PQ under the Km, Kcat, and Kcat/Km columns for mouse AKR7A5.

raw_value_unit_evidence: Table 1 row 9,10-PQ reports Km 8.0 microM, Kcat 62 min^-1, and Kcat/Km 7690000 min^-1 M^-1.

table_label: Table 1. Apparent kinetic constants for mouse AKR7A5 for aldehyde and diketone substrates


substrate_name: Camphorquinone

column_label: Table 1 row Camphorquinone; columns Km (uM), Kcat (min^-1), and Kcat/Km (min^-1 M^-1).

raw_value_unit_evidence: Table 1 row Camphorquinone: Km 4990 uM; Kcat 66 min^-1; Kcat/Km 1.32e+04 min^-1 M^-1.

row_label: Camphorquinone

substrate: Camphorquinone


substrate_name: Dimethylglyoxal

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

column_label: Table 1 row Diacetyl; columns Km (uM), Kcat (min^-1), and Kcat/Km (min^-1 M^-1).

raw_value_unit_evidence: Table 1 row Diacetyl: Km 58420 uM; Kcat 114 min^-1; Kcat/Km 1.96e+03 min^-1 M^-1.

row_label: Diacetyl

substrate: Dimethylglyoxal


substrate_name: Isatin

column_label: Table 1 row Isatin; columns Km (uM), Kcat (min^-1), and Kcat/Km (min^-1 M^-1).

raw_value_unit_evidence: Table 1 row Isatin: Km 109 uM; Kcat 54 min^-1; Kcat/Km 4.99e+05 min^-1 M^-1.

row_label: Isatin

substrate: Isatin


substrate_name: NADH

assay_conditions_summary: pH 6.6; 298.15 K; cofactor NADH

column_label: Table 1 row NADH; columns Km (uM), Kcat (min^-1), and Kcat/Km (min^-1 M^-1).

raw_value_unit_evidence: Table 1 row NADH: Km 1470 uM; Kcat 115 min^-1; Kcat/Km 7.86e+04 min^-1 M^-1.


substrate_name: NADPH

column_label: Table 1 row NADPH; columns Km (uM), Kcat (min^-1), and Kcat/Km (min^-1 M^-1).

raw_value_unit_evidence: Table 1 row NADPH: Km 1.62 uM; Kcat 26 min^-1; Kcat/Km 1.58e+07 min^-1 M^-1.

substrate: NADPH


substrate_name: p-Nitrobenzaldehyde

column_label: Table 1 row 4-NBA; columns Km (uM), Kcat (min^-1), and Kcat/Km (min^-1 M^-1).

raw_value_unit_evidence: Table 1 row 4-NBA: Km 870 uM; Kcat 46 min^-1; Kcat/Km 5.34e+04 min^-1 M^-1.

substrate: p-Nitrobenzaldehyde


substrate_name: Succinate semialdehyde

smiles: O=CCCC(=O)O

substrate: Succinate semialdehyde


substrate_name: Trans, trans-muconaldehyde

smiles: O=C/C=C/C=C/C=O

column_label: PDF page 4 Table 1 row Trans, trans-muconaldehyde under the Km, Kcat, and Kcat/Km columns for mouse AKR7A5.

raw_value_unit_evidence: Table 1 row Trans, trans-muconaldehyde reports Km 7190 microM, Kcat 94 min^-1, and Kcat/Km 13100 min^-1 M^-1.

row_label: Trans, trans-muconaldehyde

substrate: Trans, trans-muconaldehyde


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


proof_lines: could function as both a SSA reductase and a 2-CBA reductase in vivo


assay_conditions_summary: pH 6.7; 298.15 K; cofactor NADPH

proof_lines: hAFAR shows high affinity for succinic semialdehyde


enzyme_display_name: Succinic semialdehyde reductase

organism: Metallosphaera sedula

substrate_name: NADPH; Succinate semialdehyde; H+

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

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

enzyme: Succinic semialdehyde reductase

substrate: NADPH; Succinate semialdehyde; H+


assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADPH


column_label: Table 1 row SSA with fixed substrate NADPH, Km = 8.96 +/- 0.71 mM, kcat = 17.0 +/- 2.2 s^-1, and kcat/Km = 1.89 +/- 0.27 s^-1 mM^-1.

row_label: SSA; fixed substrate NADPH

table_label: Table 1


enzyme_display_name: Glyoxylate/succinic semialdehyde reductase 2, chloroplastic

substrate_name: glyoxylate (check for NADPH)

assay_conditions_summary: pH 7.6; cofactor NADPH

column_label: Table 1 row Glyoxylate with fixed substrate NADPH, Km column = 0.034 +/- 0.003 mM.

row_label: Glyoxylate; fixed substrate NADPH

substrate: glyoxylate (check for NADPH)


substrate_name: succinate semialdehyde

column_label: Table 1 row SSA with fixed substrate NADPH, Km column = 8.96 +/- 0.71 mM.

enzyme: Glyoxylate/succinic semialdehyde reductase 2, chloroplastic

substrate: succinate semialdehyde


substrate_name: NADPH (in the presence of glyoxylate as cosubstrate)

assay_conditions_summary: cofactor NADPH


enzyme_display_name: Aflatoxin B1 aldehyde reductase member 2

substrate_name: succinic semialdehyde

column_label: Table 6 row Succinic semialdehyde / AKR7A2; column Km (uM).

normalized_value_unit_evidence: Km 0.02 mM from 20 uM.

raw_value_unit_evidence: Table 6 row Succinic semialdehyde / AKR7A2: Km 20 +/- 1 uM; kcat 113 +/- 9 min^-1; kcat/Km 5.7 x 10^6 min^-1 M^-1.

row_label: Succinic semialdehyde / AKR7A2

table_label: Table 6. Kinetic properties of recombinant human AKR1A1 and AKR7A2

substrate: succinic semialdehyde


column_label: Table 6 row 2-Carboxybenzaldehyde / AKR7A2; column Km (uM).

normalized_value_unit_evidence: Km 0.017 mM from 17 uM.

raw_value_unit_evidence: Table 6 row 2-Carboxybenzaldehyde / AKR7A2: Km 17 +/- 1 uM; kcat 95 +/- 6 min^-1; kcat/Km 5.8 x 10^6 min^-1 M^-1.

row_label: 2-Carboxybenzaldehyde / AKR7A2

enzyme: Aflatoxin B1 aldehyde reductase member 2


column_label: Table 6 row 9,10-Phenanthrenequinone / AKR7A2; column Km (uM).

normalized_value_unit_evidence: Km 0.008 mM from 8 uM.

raw_value_unit_evidence: Table 6 row 9,10-Phenanthrenequinone / AKR7A2: Km 8 +/- 0.1 uM; kcat 187 +/- 22 min^-1; kcat/Km 2.5 x 10^7 min^-1 M^-1.

row_label: 9,10-Phenanthrenequinone / AKR7A2


column_label: Table 6 row 1,2-Naphthoquinone / AKR7A2; column Km (uM).

normalized_value_unit_evidence: Km 0.102 mM from 102 uM.

raw_value_unit_evidence: Table 6 row 1,2-Naphthoquinone / AKR7A2: Km 102 +/- 10 uM; kcat 435 +/- 27 min^-1; kcat/Km 4.2 x 10^6 min^-1 M^-1.

row_label: 1,2-Naphthoquinone / AKR7A2


organism: Rattus norvegicus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F224W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M77W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V44M to reconstruct the assayed variant sequence.


enzyme_display_name: (3R)-3-hydroxyacyl-CoA dehydrogenase

substrate_name: estradiol

proof_lines:
Ke 6
HSD17B8
estradiol

enzyme: (3R)-3-hydroxyacyl-CoA dehydrogenase

substrate: estradiol


substrate_name: testosterone

proof_lines:
Ke 6
HSD17B8
testosterone

substrate: testosterone


substrate_name: estrone

proof_lines:
Ke 6
HSD17B8
estrone

substrate: estrone


substrate_name: dihydrotestosterone

proof_lines:
Ke 6
HSD17B8
dihydrotestosterone

substrate: dihydrotestosterone


assay_conditions_summary: pH 8.5; cofactor CoA

column_label: Results prose lines 260-266 and Fig. 4; protein DBP; substrate C16:1DC-CoA ((2E)-hexadecenedioyl-CoA); metric apparent Km; raw value 0.9 uM; normalized Km=0.0009 mM.

raw_value_unit_evidence: Results text reports DBP apparent Km 0.9 uM for C16:1DC-CoA (Fig. 4).

table_label: PMID 15060085, Results prose and Fig. 4: kinetic analysis of human DBP and LBP


column_label: Results prose lines 260-266 and Fig. 4; protein DBP; substrate C16:1-CoA ((2E)-hexadecenoyl-CoA); metric apparent Km; raw value 12.8 uM; normalized Km=0.0128 mM.

raw_value_unit_evidence: Results text reports DBP apparent Km 12.8 uM for C16:1-CoA (Fig. 4).


substrate_name: NAD

proof_lines:
HSD17B4
dehydrogenase reactions
Table II

substrate: NAD


substrate: NADH


column_label: Table 2 row AKR7A5 reports Km 19.8 +/- 0.5 uM for SSA.

raw_value_unit_evidence: Km raw_value=19.8 +/- 0.5 uM raw_unit=uM

row_label: Wild-type AKR7A5 / SSA

table_label: Table 2, PMID 16460003 PDF


enzyme_display_name: UniProt P00175

organism: Saccharomyces cerevisiae

substrate_name: FAD

enzyme: UniProt P00175

substrate: FAD


enzyme_display_name: methanol dehydrogenase (cytochrome c)

organism: Methyloversatilis universalis

substrate_name: methanol

smiles: CO

enzyme: methanol dehydrogenase (cytochrome c)

substrate: methanol


substrate_name: ethanol

smiles: CCO

substrate: ethanol


substrate_name: n-Propanol

smiles: CCCO

substrate: n-Propanol


substrate_name: n-butanol

smiles: CCCCO

substrate: n-butanol


organism: Methylibium petroleiphilum


organism: Methylophilus methylotrophus

substrate_name: PQQ; Methanol

substrate: PQQ; Methanol


enzyme_display_name: mannitol dehydrogenase (cytochrome)

organism: Komagataeibacter xylinus

substrate_name: D-mannitol

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

proof_lines: with phenanzine methosulfate as electron acceptor

enzyme: mannitol dehydrogenase (cytochrome)

substrate: D-mannitol


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: D-lactate dehydrogenase (cytochrome c-553)

organism: Nitratidesulfovibrio vulgaris

substrate_name: D-lactate

substrate: D-lactate


enzyme: D-lactate dehydrogenase (cytochrome c-553)


organism: Gluconobacter oxydans

substrate_name: D-arabitol

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

substrate: D-arabitol


substrate_name: D-sorbitol

substrate: D-sorbitol


enzyme_display_name: L-lactate dehydrogenase (cytochrome)

organism: Satureja hortensis

substrate_name: (S)-lactate

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication

enzyme: L-lactate dehydrogenase (cytochrome)

substrate: (S)-lactate


substrate_name: potassium ferricyanide

proof_lines: pH 9.5, temperature not specified in the publication

substrate: potassium ferricyanide


organism: Rhodovulum steppense

proof_lines: pH and temperature not specified in the publication


organism: Crocus sativus

substrate_name: ferricyanide

proof_lines: pH 5.5, isoform with activity maximum at pH 5.5

proof_lines: pH 7.5, isoform with activity maximum at pH 7.5

proof_lines: pH 9.5, isoform with activity maximum at pH 9.5

substrate: ferricyanide


organism: Arabidopsis thaliana


organism: Ogataea angusta

substrate_name: L-lactate

proof_lines: sensor based on the inital Hansenula polymorpha C-105 cells

proof_lines: biosensor based on recombinant yeast FCb2cells

substrate: L-lactate


enzyme_display_name: D-lactate dehydrogenase (cytochrome)

organism: Megasphaera elsdenii

proof_lines:
with ferricyanide
with complete electron transport system

enzyme: D-lactate dehydrogenase (cytochrome)


organism: Helianthus tuberosus


organism: Methylomicrobium sp. HG-1

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

assay_conditions_summary: pH 9

proof_lines: 100 mM Tris-HCl buffer (pH 9.0), 1.1 mM phenazine ethosulfate (initial electron acceptor), 0.04 mM 2,6-dichlorophenol indophenol (terminal electron acceptor), 1 mM KCN and 15 mM NH4Cl, 60°C


substrate_name: Heptanol

smiles: CCCCCCCO

substrate: Heptanol


substrate_name: Hexanol

smiles: CCCCCCO

substrate: Hexanol


substrate_name: Pentanol

smiles: CCCCCO

substrate: Pentanol


substrate_name: Propanol

substrate: Propanol


substrate_name: butanol

substrate: butanol


enzyme_display_name: Quinoprotein ethanol dehydrogenase

organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: ethanol

proof_lines: kcat is 11 sec(-1) for the oxidation of ethanol using artificial electron acceptor (at pH 9). kcat is 15 sec(-1) for the oxidation of 1-propanol using artificial electron acceptor (at pH 9). kcat is 11 sec(-1) for the oxidation of 2-propano

enzyme: Quinoprotein ethanol dehydrogenase

substrate: ethanol


smiles: CC(C)O


smiles: CCC(C)O


substrate_name: ethanal

smiles: CC=O

substrate: ethanal


substrate_name: methanol

substrate: methanol


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D282N with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7

proof_lines: mutant D282N with R289 distal, pH 7.0, 30°C


substrate_name: 1,3-propanediol (at pH 9)

smiles: C(CO)CO

substrate: 1,3-propanediol (at pH 9)


substrate_name: 1-butanol (at pH 9)

substrate: 1-butanol (at pH 9)


substrate_name: FAD

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D72A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; cofactor FAD

proof_lines: pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant D72A

substrate: FAD


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N69K with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant N69K


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K73A with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant K73A


enzyme_display_name: D-lactate dehydrogenase [cytochrome], mitochondrial

substrate_name: D-2-hydroxybutyrate (with cytochrome c as acceptor molecule)

proof_lines: kcat is 88 min(-1) with D-2-hydroxybutyrate as substrate (with cytochrome c as acceptor molecule) (PubMed:19586914). kcat is 65 min(-1) with D-lactate as substrate (with cytochrome c as acceptor molecule) (PubMed:19586914). kcat is 7 min(-1


substrate_name: D-lactate (with cytochrome c as acceptor molecule)

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

enzyme: D-lactate dehydrogenase [cytochrome], mitochondrial


substrate_name: L-lactate (with cytochrome c as acceptor molecule)


substrate_name: D-glycerate (with cytochrome c as acceptor molecule)


substrate_name: glycolate (with cytochrome c as acceptor molecule)

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


substrate_name: L-lactate

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

proof_lines: kcat is 207 sec(-1) with cytochrome c as electron acceptor. kcat is 400 sec(-1) with ferricyanide as electron acceptor.

source_databases_merged: skid uniprot


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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

proof_lines: kcat is 4.0 sec(-1) for (R)-2-hydroxyglutarate oxidation with pyruvate as electron acceptor. kcat is 6.6 sec(-1) for (R)-2-hydroxyglutarate oxidation with DCIP as electron acceptor. kcat is 4.9 sec(-1) for pyruvate reduction with (R)-2-hydr


substrate_name: pyruvate

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

substrate: pyruvate


substrate_name: (R)-lactate

substrate: (R)-lactate


proof_lines: kcat is 0.11 sec(-1) for (R)-2-hydroxyglutarate oxidation with pyruvate as electron acceptor. kcat is 0.18 sec(-1) for (R)-2-hydroxyglutarate oxidation with DCIP as electron acceptor. kcat is 1.31 sec(-1) for (R)-lactate reduction with DCIP


organism: Methylophaga aminisulfidivorans

smiles: CO

proof_lines: type I MDH, pH 9.0, 30°C, with phenazine ethosulfate and 2,6-dichlorophenolindophenol

proof_lines: type II MDH, pH 9.0, 30°C, with phenazine ethosulfate and 2,6-dichlorophenolindophenol

proof_lines: type I MDH, pH 7.0, 30°C, with cytochrome cL


organism: Saccharomyces cerevisiae

substrate_name: Ferricytochrome c

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R289K with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines:
cytochrome c reduction
R289K
k(cat) by a factor of about 10

substrate: Ferricytochrome c


substrate_name: L-Lactate

proof_lines:
L-lactate dehydrogenation
cytochrome c reduction
R289K

substrate: L-Lactate


substrate_name: L-Phenyllactate

substrate: L-Phenyllactate


substrate_name: cytochrome c

proof_lines: pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant A67Q

substrate: cytochrome c


proof_lines: pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant F39A


proof_lines: pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant L65A


proof_lines: pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant P44A


proof_lines: pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant A67L


proof_lines: pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant E63K


proof_lines: pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant P64R


proof_lines: pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant P64Q


proof_lines: pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, mutant V70M


assay_conditions_summary: pH 7; 303.15 K; cofactor FAD


proof_lines: pH 7.0, 30°C, flavin turnover in pre-steady-state flavin reduction, wild-type enzyme


enzyme_display_name: Quinoprotein alcohol dehydrogenase PedE

organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

substrate_name: ethanol

smiles: CCO

column_label: Figure 3 panel D lists ethanol KM=85 +/- 18 uM for PedE.

raw_value_unit_evidence: KM raw_value=85 +/- 18 raw_unit=uM

row_label: PedE, ethanol

table_label: Figure 3, panel D: Kinetic constants of PedE

enzyme: Quinoprotein alcohol dehydrogenase PedE


substrate_name: acetaldehyde

column_label: Figure 3 panel D lists acetaldehyde KM=899 +/- 155 uM for PedE.

raw_value_unit_evidence: KM raw_value=899 +/- 155 raw_unit=uM

row_label: PedE, acetaldehyde

substrate: acetaldehyde


column_label: Figure 3 panel D lists 2-phenylethanol KM=115 +/- 22 uM for PedE.

raw_value_unit_evidence: KM raw_value=115 +/- 22 raw_unit=uM

row_label: PedE, 2-phenylethanol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y143F with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.


enzyme_display_name: alcohol dehydrogenase (cytochrome c)

organism: Methylacidiphilum fumariolicum

substrate_name: methanol

enzyme: alcohol dehydrogenase (cytochrome c)


substrate_name: Phenyllactate

proof_lines:
Y254F mutant enzyme
Y254F mutant

substrate: Phenyllactate


proof_lines:
Y254F mutant enzyme
Y254F mutant
pH 7.0, 25°C, mutant Y254F

substrate: L-lactate


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: (S)-mandelate

substrate: (S)-mandelate


enzyme_display_name: 3-hydroxy acid dehydrogenase

organism: Escherichia coli

substrate_name: L-Glycerate

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

enzyme: 3-hydroxy acid dehydrogenase

substrate: L-Glycerate


substrate_name: D-glycerate

substrate: D-glycerate


substrate_name: D-serine

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

substrate: D-serine


substrate_name: L-allo-threonine

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

substrate: L-allo-threonine


substrate_name: NADP+

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

substrate: NADP+


enzyme_display_name: UniProt Q44467

organism: Aerococcus viridans

substrate_name: glycerate

enzyme: UniProt Q44467

substrate: glycerate


substrate_name: L-lactate

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7
Raw SKiD Env: Temp=4°C, pH=7
Raw SKiD Env: Temp=20°C, pH=6.5


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


substrate_name: (S)-mandelic acid

substrate: (S)-mandelic acid


smiles: O=O

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7
Raw SKiD Env: Temp=37°C, pH=6.5


enzyme_display_name: glucose oxidase

organism: Talaromyces variabilis

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

enzyme: glucose oxidase


organism: Talaromyces funiculosus


substrate_name: D-xylose

substrate: D-xylose


substrate_name: D-maltose

substrate: D-maltose


substrate_name: D-fructose

substrate: D-fructose


enzyme_display_name: Carbohydrate oxidase

organism: Microdochium nivale

substrate_name: cellotriose (at pH 7.2 and 25 degrees Celsius)

enzyme: Carbohydrate oxidase


substrate_name: cellotetraose (at pH 7.2 and 25 degrees Celsius)


organism: Pseudomonas putida

substrate_name: ethanol

substrate: ethanol


smiles: CCCCO


smiles: CC(CO)O

proof_lines:
Pseudomonas putida HK5
ADH IIG
1,2-propanediol induction


organism: Streptomyces coelicolor

substrate_name: D-mannitol

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

substrate: D-mannitol


substrate_name: xylitol

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

substrate: xylitol


enzyme_display_name: L-lactate oxidase

enzyme: L-lactate oxidase


organism: Methylotenera mobilis

smiles: CCCCCCO

proof_lines:
subtype XoxF4-1, at pH 9.0 and 26°C
subtype XoxF4-2, at pH 9.0 and 26°C


smiles: CCCO


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


smiles: CCCC(CO)N


smiles: C=CCCO


smiles: CCC(CO)O


smiles: C=CC(CO)O


smiles: CCCC(CO)O


substrate_name: glycerol

smiles: C(C(CO)O)O

substrate: glycerol


substrate_name: L-arabinose

substrate: L-arabinose


smiles: CCCCC(CO)O


smiles: C(CO)C(CO)O


substrate_name: L-Threitol

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

column_label: Table 1 row L-threitol, columns KM (mM), kcat (s^-1), and kcat/KM (mM^-1 s^-1).

normalized_value_unit_evidence: Table 1 normalized central values: KM=25 mM; kcat=6.3 s^-1; kcat/KM=0.25 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row L-threitol: KM=25 ± 1 mM; kcat=6.3 ± 0.1 s^-1; kcat/KM=0.25 mM^-1 s^-1.

row_label: L-threitol

table_label: Table 1, Steady-state kinetic parameters for m-AldO

substrate: L-Threitol


organism: Phanerodontia chrysosporium

smiles: O=O


substrate_name: beta-D-glucose

substrate: beta-D-glucose


substrate_name: L-sorbose

substrate: L-sorbose


organism: Methylomonas sp. LW13


smiles: CCO


smiles: CCCCO


substrate_name: (S)-lactate

substrate: (S)-lactate


proof_lines:
wild-type, pH 6.5, 37°C
wild-type, pH 7.0, 25°C


proof_lines:
wild-type, pH 6.5, 20°C
wild-type, pH 6.5, 37°C
wild-type, pH 7.0, 25°C


organism: Pleurotus ostreatus


enzyme_display_name: glucoside 3-dehydrogenase (cytochrome c)

organism: Agrobacterium fabrum

substrate_name: cytochrome c

substrate: cytochrome c


substrate_name: methyl alpha-D-glucoside

enzyme: glucoside 3-dehydrogenase (cytochrome c)

substrate: methyl alpha-D-glucoside


organism: Leeuwenhoekiella marinoflava

substrate_name: D-glucose

substrate: D-glucose


substrate_name: L-alpha-hydroxy-beta-methylvalerate

substrate: L-alpha-hydroxy-beta-methylvalerate


substrate_name: methanol

smiles: CO

proof_lines: in the presence of a mixture of La3+, Ce3+, Pr3+, Nd3+, at pH 7.2 and 60°C

proof_lines: pH and temperature not specified in the publication, lanthanide: La3+, Ce3+, Pr3+, Nd3+

substrate: methanol


organism: Methyloversatilis discipulorum

proof_lines: pH and temperature not specified in the publication


organism: Bradyrhizobium diazoefficiens


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R181K with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R181M with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


substrate_name: L-lactate

substrate: L-lactate


organism: Rhodovulum kholense


organism: Sinorhizobium meliloti


organism: Grimontia marina


organism: Tistlia consotensis


proof_lines: pH and temperature not specified in the publication, lanthanide: Ce3+


proof_lines: pH and temperature not specified in the publication, methanol dehydrogenase XoxF4-1


organism: Chlamydomonas reinhardtii


organism: Nostoc sp. PCC 7120 = FACHB-418


organism: Aerococcus viridans

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


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


organism: Gram-negative soil bacterium

substrate_name: (R)-lactate

substrate: (R)-lactate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A95G to reconstruct the assayed variant sequence.

proof_lines:
mutant A95G, pH 6.5, 20°C
mutant A95G, pH 7.0, 25°C


substrate_name: Unknown

substrate: Unknown


organism: Phanerochaete chrysosporium

substrate_name: beta-D-Glucose; O2

substrate: beta-D-Glucose; O2


organism: Goffeauzyma gastrica

proof_lines: 64°C, pH not specified in the publication


organism: Bombyx mori

proof_lines: immobilized enzyme, immobilized membrane with ratio stretching 1.25

proof_lines: immobilized enzyme, immobilized membrane with ratio stretching 3


enzyme_display_name: hexose oxidase

organism: Mazzaella flaccida

enzyme: hexose oxidase


organism: Talaromyces purpureogenus


organism: Penicillium amagasakiense

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K424I with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant K424I, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme

proof_lines: recombinant mutant K424I, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K424E with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant K424E, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme

proof_lines: recombinant mutant K424E, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme


organism: Aspergillus niger

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T30V/I94V/A162T with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T30V/R37K/I94V/V106I/A162T/M556V with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: pH 5.5, temperature not specified in the publication, mutant enzyme T30V/R37K/I94V/V106I/A162T/M556V


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T30V/I94V/A162T/R537K/M556V with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: pH 5.5, temperature not specified in the publication, mutant enzyme T30V/I94V/A162T/R537K/M556V


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


substrate_name: D-xylose

substrate: D-xylose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P81156 and applied mutation signature H520V with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 298.15 K; buffer 0.1 M sodium acetate

column_label: Table 1 (Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6), GOX variant row 'H520V'; column 'Vmax (units/mg)' = 0.01; column 'Km (app) (mM)' = 6.7; column 'kcat (s^-1)' = 0.03; column 'kcat/Km (mM^-1 s^-1)' = 0.004; column '10^3 x Specificity (variant/wild-type)' = 0.01.

normalized_value_unit_evidence: Km: printed Table 1 cell 6.7 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 6.7 mM. kcat: printed Table 1 cell 0.03 s^-1; the printed unit is already s^-1, so no unit conversion applies; the paper value is 0.03 s^(-1). kcat/Km: printed Table 1 cell 0.004 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies; the paper value is 0.004 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GOX variant row 'H520V': Km (app) = 6.7 mM; kcat = 0.03 s^-1; printed kcat/Km = 0.004 mM^-1 s^-1.

row_label: Table 1, GOX variant row 'H520V'

table_label: Table 1: Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6 (Biochemical Journal 2000, 347:553-559)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P81156 and applied mutation signature H520A with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6), GOX variant row 'H520A'; column 'Vmax (units/mg)' = 0.08; column 'Km (app) (mM)' = 5.8; column 'kcat (s^-1)' = 0.16; column 'kcat/Km (mM^-1 s^-1)' = 0.03; column '10^3 x Specificity (variant/wild-type)' = 0.1.

normalized_value_unit_evidence: Km: printed Table 1 cell 5.8 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 5.8 mM. kcat: printed Table 1 cell 0.16 s^-1; the printed unit is already s^-1, so no unit conversion applies; the paper value is 0.16 s^(-1). kcat/Km: printed Table 1 cell 0.03 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies; the paper value is 0.03 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GOX variant row 'H520A': Km (app) = 5.8 mM; kcat = 0.16 s^-1; printed kcat/Km = 0.03 mM^-1 s^-1.

row_label: Table 1, GOX variant row 'H520A'


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

assay_conditions_summary: pH 6


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P81156 and applied mutation signature W430A with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6), GOX variant row 'W430A'; column 'Vmax (units/mg)' = 10.5; column 'Km (app) (mM)' = 27; column 'kcat (s^-1)' = 23; column 'kcat/Km (mM^-1 s^-1)' = 0.8; column '10^3 x Specificity (variant/wild-type)' = 2.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 27 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 27.0 mM. kcat: printed Table 1 cell 23 s^-1; the printed unit is already s^-1, so no unit conversion applies; the paper value is 23.0 s^(-1). kcat/Km: printed Table 1 cell 0.8 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies; the paper value is 0.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GOX variant row 'W430A': Km (app) = 27 mM; kcat = 23 s^-1; printed kcat/Km = 0.8 mM^-1 s^-1.

row_label: Table 1, GOX variant row 'W430A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P81156 and applied mutation signature R516Q with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6), GOX variant row 'R516Q'; column 'Vmax (units/mg)' = 33; column 'Km (app) (mM)' = 733; column 'kcat (s^-1)' = 71; column 'kcat/Km (mM^-1 s^-1)' = 0.1; column '10^3 x Specificity (variant/wild-type)' = 0.3.

normalized_value_unit_evidence: Km: printed Table 1 cell 733 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 733.0 mM. kcat: printed Table 1 cell 71 s^-1; the printed unit is already s^-1, so no unit conversion applies; the paper value is 71.0 s^(-1). kcat/Km: printed Table 1 cell 0.1 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies; the paper value is 0.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GOX variant row 'R516Q': Km (app) = 733 mM; kcat = 71 s^-1; printed kcat/Km = 0.1 mM^-1 s^-1.

row_label: Table 1, GOX variant row 'R516Q'


proof_lines: recombinant wild-type enzyme, pH 7.0, 37°C, with Os-(tpy)(MeCOOH-bpy)Cl2, immobilized enzyme

proof_lines: recombinant wild-type enzyme, pH 7.0, 37°C, with ferrocenemethanol, immobilized enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P81156 and applied mutation signature F418V with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6), GOX variant row 'F418V'; column 'Vmax (units/mg)' = 147; column 'Km (app) (mM)' = 13.3; column 'kcat (s^-1)' = 318; column 'kcat/Km (mM^-1 s^-1)' = 24; column '10^3 x Specificity (variant/wild-type)' = 74.3.

normalized_value_unit_evidence: Km: printed Table 1 cell 13.3 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 13.3 mM. kcat: printed Table 1 cell 318 s^-1; the printed unit is already s^-1, so no unit conversion applies; the paper value is 318.0 s^(-1). kcat/Km: printed Table 1 cell 24 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies; the paper value is 24.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GOX variant row 'F418V': Km (app) = 13.3 mM; kcat = 318 s^-1; printed kcat/Km = 24 mM^-1 s^-1.

row_label: Table 1, GOX variant row 'F418V'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P81156 and applied mutation signature R516K with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6), GOX variant row 'R516K'; column 'Vmax (units/mg)' = 279; column 'Km (app) (mM)' = 513; column 'kcat (s^-1)' = 603; column 'kcat/Km (mM^-1 s^-1)' = 1.2; column '10^3 x Specificity (variant/wild-type)' = 3.7.

normalized_value_unit_evidence: Km: printed Table 1 cell 513 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 513.0 mM. kcat: printed Table 1 cell 603 s^-1; the printed unit is already s^-1, so no unit conversion applies; the paper value is 603.0 s^(-1). kcat/Km: printed Table 1 cell 1.2 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies; the paper value is 1.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GOX variant row 'R516K': Km (app) = 513 mM; kcat = 603 s^-1; printed kcat/Km = 1.2 mM^-1 s^-1.

row_label: Table 1, GOX variant row 'R516K'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P81156 and applied mutation signature Y73F with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6), GOX variant row 'Y73F'; column 'Vmax (units/mg)' = 295; column 'Km (app) (mM)' = 24; column 'kcat (s^-1)' = 639; column 'kcat/Km (mM^-1 s^-1)' = 26; column '10^3 x Specificity (variant/wild-type)' = 80.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 24 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 24.0 mM. kcat: printed Table 1 cell 639 s^-1; the printed unit is already s^-1, so no unit conversion applies; the paper value is 639.0 s^(-1). kcat/Km: printed Table 1 cell 26 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies; the paper value is 26.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GOX variant row 'Y73F': Km (app) = 24 mM; kcat = 639 s^-1; printed kcat/Km = 26 mM^-1 s^-1.

row_label: Table 1, GOX variant row 'Y73F'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P81156 and applied mutation signature N518T with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6), GOX variant row 'N518T'; column 'Vmax (units/mg)' = 539; column 'Km (app) (mM)' = 36; column 'kcat (s^-1)' = 1166; column 'kcat/Km (mM^-1 s^-1)' = 33; column '10^3 x Specificity (variant/wild-type)' = 102.2.

normalized_value_unit_evidence: Km: printed Table 1 cell 36 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 36.0 mM. kcat: printed Table 1 cell 1166 s^-1; the printed unit is already s^-1, so no unit conversion applies; the paper value is 1166.0 s^(-1). kcat/Km: printed Table 1 cell 33 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies; the paper value is 33.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GOX variant row 'N518T': Km (app) = 36 mM; kcat = 1166 s^-1; printed kcat/Km = 33 mM^-1 s^-1.

row_label: Table 1, GOX variant row 'N518T'


organism: Methylorubrum extorquens

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

proof_lines: in the presence of Nd3+, at pH 7.0 and 30°C

proof_lines: Nd-XoxF, pH 7.0, 30°C, determined using the dye-linked activity, DCPIP reduction

proof_lines: in the presence of Ce3+, at pH 7.0 and 30°C

source_databases_merged: brenda skid


organism: Penicillium adametzii

assay_conditions_summary: pH 5

proof_lines:
pH 5.0, 25°C, enzyme fraction 1
pH 5.0, 25°C, enzyme fraction 2
pH 5.0, 25°C


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


substrate_name: formaldehyde

proof_lines: XoxF1, in the absence of lanthanides, pH and temperature not specified in the publication

proof_lines: XoxF1, in the presence of La3+, pH and temperature not specified in the publication

substrate: formaldehyde


substrate_name: ethanol

substrate: ethanol


proof_lines: recombinant enzyme yGOXpenag, using ferrocinium-methanol as cosubstrate, pH 6.0, 50°C

proof_lines: recombinant enzyme yGOXpenag, using O2 as cosubstrate, pH 6.0, 50°C

source_databases_merged: brenda skid uniprot


organism: Chondrus crispus

proof_lines: pH 7.0, temperature not specified in the publication


organism: Talaromyces variabilis

proof_lines:
pH 5.0, 28°C, native enzyme
pH 5.0, 28°C, recombinant enzyme


enzyme_display_name: Transferred entry: 1.13.12.4

enzyme: Transferred entry: 1.13.12.4


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y215F with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y215H with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P81156 and applied mutation signature F418V with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6; row F418V; columns Km(app) (mM), kcat (s^-1), and kcat/Km (mM^-1*s^-1); F418V: Km(app) 13.3 +/- 0.7 mM; kcat 318 s^-1; kcat/Km 24 mM^-1*s^-1. The printed central Km value is 13.3 mM and the independently printed efficiency is 24 mM^-1*s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P81156 and applied mutation signature H520A with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6; row H520A; columns Km(app) (mM), kcat (s^-1), and kcat/Km (mM^-1*s^-1); H520A: Km(app) 5.8 +/- 0.7 mM; kcat 0.16 s^-1; kcat/Km 0.03 mM^-1*s^-1. The printed central Km value is 5.8 mM and the independently printed efficiency is 0.03 mM^-1*s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P81156 and applied mutation signature N518T with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6; row N518T; columns Km(app) (mM), kcat (s^-1), and kcat/Km (mM^-1*s^-1); N518T: Km(app) 36 +/- 2 mM; kcat 1166 s^-1; kcat/Km 33 mM^-1*s^-1. The printed central Km value is 36 mM and the independently printed efficiency is 33 mM^-1*s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P81156 and applied mutation signature R516K with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6; row R516K; columns Km(app) (mM), kcat (s^-1), and kcat/Km (mM^-1*s^-1); R516K: Km(app) 513 +/- 90 mM; kcat 603 s^-1; kcat/Km 1.2 mM^-1*s^-1. The printed central Km value is 513 mM and the independently printed efficiency is 1.2 mM^-1*s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P81156 and applied mutation signature W430A with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6; row W430A; columns Km(app) (mM), kcat (s^-1), and kcat/Km (mM^-1*s^-1); W430A: Km(app) 27 +/- 4 mM; kcat 23 s^-1; kcat/Km 0.8 mM^-1*s^-1. The printed central Km value is 27 mM and the independently printed efficiency is 0.8 mM^-1*s^-1.


column_label: Primary-paper Table 1 lists Wild type kcat 2003, Km 6.2 +/- 0.5, and kcat/Km 323; export kcat/Km is 323.06451612903226.

row_label: Wild type row

table_label: Table 1: Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P81156 and applied mutation signature Y73F with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of P. amagasakiense GOX variants for the oxidation of beta-D-glucose at pH 6; row Y73F; columns Km(app) (mM), kcat (s^-1), and kcat/Km (mM^-1*s^-1); Y73F: Km(app) 24 +/- 2 mM; kcat 639 s^-1; kcat/Km 26 mM^-1*s^-1. The printed central Km value is 24 mM and the independently printed efficiency is 26 mM^-1*s^-1.


column_label: Primary-paper PMC Table 4 reports 2-Deoxy-D-glucose columns Km 8.3 +/- 0.7 mM, kcat 83 s^-1, and kcat/Km 10.0 s^-1 mM^-1.

raw_value_unit_evidence: 2-Deoxy-D-glucose Km 8.3 +/- 0.7 mM; kcat 83 s^-1; kcat/Km 10.0 s^-1 mM^-1

row_label: 2-Deoxy-D-glucose row

table_label: Table 4: Kinetic parameters of recombinant GOX for different sugars


substrate_name: D-Galactose

column_label: Primary-paper PMC Table 4 reports D-Galactose columns Km 952 +/- 9 mM, kcat 159 s^-1, and kcat/Km 0.2 s^-1 mM^-1.

raw_value_unit_evidence: D-Galactose Km 952 +/- 9 mM; kcat 159 s^-1; kcat/Km 0.2 s^-1 mM^-1

row_label: D-Galactose row

substrate: D-Galactose


substrate_name: D-Mannose

column_label: Primary-paper PMC Table 4 reports D-Mannose columns Km 106 +/- 8 mM, kcat 401 s^-1, and kcat/Km 3.8 s^-1 mM^-1.

raw_value_unit_evidence: D-Mannose Km 106 +/- 8 mM; kcat 401 s^-1; kcat/Km 3.8 s^-1 mM^-1

row_label: D-Mannose row

substrate: D-Mannose


substrate_name: D-Xylose

column_label: Primary-paper PMC Table 4 reports D-Xylose columns Km 384 +/- 27 mM, kcat 72 s^-1, and kcat/Km 0.2 s^-1 mM^-1.

normalized_value_unit_evidence: Km 384 mM = 384 mM; kcat 72 s^-1 = 72 s^-1; table kcat/Km 0.2 is a one-decimal display of 72/384 = 0.1875 s^-1 mM^-1

row_label: D-Xylose row

substrate: D-Xylose


organism: Penicillium sp. MX3343

substrate_name: beta-D-glucose

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

substrate: beta-D-glucose


column_label: Table 2 GOxP5 row lists Km / kcat / kcat/Km as 0.0657 mol L^-1 / 137.1 s^-1 / 2086.758 mol^-1 L s^-1

row_label: GOxP5 row

table_label: Frontiers PDF Table 2


proof_lines:
hexose oxidase
Chondrus crispus
Km(O2)


substrate_name: lactose

proof_lines:
hexose oxidase
Chondrus crispus
lactose

substrate: lactose


enzyme_display_name: 1-butanol dehydrogenase (cytochrome c)

organism: Thauera butanivorans (strain ATCC 43655 / DSM 2080 / JCM 20651 / CCUG 51053 / NBRC 103042 / IAM 12574 / Bu B1211)

substrate_name: butyraldehyde

smiles: CCCC=O

column_label: Catalytic-properties prose reports butyraldehyde Km 535 +/- 13 uM and states that BDH affinity for 1-butanol is 76-fold higher.

raw_value_unit_evidence: Km=535 +/- 13 uM for butyraldehyde.

row_label: butyraldehyde

table_label: Primary article PDF page 9 / printed page 753, Catalytic properties prose

enzyme: 1-butanol dehydrogenase (cytochrome c)

substrate: butyraldehyde


organism: Microdochium nivale

substrate_name: cellobiose (at pH 6 and 30 degrees Celsius)


substrate_name: glucose (at pH 6 and 40 degrees Celsius)

column_label: Results prose reports Km values of 42, 11, and 59 mM for Glc, maltose, and cellobiose, respectively.

raw_value_unit_evidence: Km raw_value=42 raw_unit=mM

row_label: r-MnCO / Glc

table_label: Wiley full-text results prose, enzymatic properties of r-MnCO


organism: Thauera butanivorans

column_label: The abstract reports BDH exhibited its lowest Km, 7+/-1 microM, towards 1-butanol.

raw_value_unit_evidence: Km raw_value=7 microM raw_unit=microM

row_label: Prose segment: 1-butanol Km

table_label: PubMed PMID 11238982 abstract


substrate_name: acetaldehyde

column_label: Fig. 3D two-carbon-substrate table lists acetaldehyde Km 285 uM.

raw_value_unit_evidence: Km raw_value=285 raw_unit=uM

row_label: ExaF-La / acetaldehyde row

table_label: Fig. 3D, ExaF kinetic parameters with two-carbon substrates

substrate: acetaldehyde


substrate_name: methanol


substrate_name: Acceptor

smiles: [At]

substrate: Acceptor


enzyme_display_name: UniProt P13006

proof_lines:
Raw SKiD Env: Temp=37°C, pH=5.1
Raw SKiD Env: Temp=25°C, pH=6
Raw SKiD Env: Temp=25°C, pH=7.4

enzyme: UniProt P13006


enzyme_display_name: Glucose oxidase

proof_lines: kinetic analysis of a yeast-derived enzyme

enzyme: Glucose oxidase


organism: Penicillium chrysogenum

column_label: OUP full text reports Km,xylose = 690 mmol l^-1 for Penicillium chrysogenum GOX.

raw_value_unit_evidence: Km raw_value=690 mmol l^-1 raw_unit=mmol l^-1

row_label: Penicillium chrysogenum GOX / D-xylose

table_label: Results prose: GOX kinetic parameters


substrate_name: oxygen

column_label: Abstract reports K(m) for oxygen was 0.97 mM.

raw_value_unit_evidence: Km raw_value=0.97 mM raw_unit=mM

row_label: Microdochium nivale carbohydrate oxidase / oxygen

table_label: PubMed XML abstract PMID 17154316

substrate: oxygen


enzyme_display_name: L-lactate dehydrogenase (cytochrome)

organism: Saccharomyces cerevisiae

substrate_name: L-lactate

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

proof_lines: influence of anions (400 mM KBr) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration

proof_lines: influence of anions (400 mM potassium acetate) on mutant R289K steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 2 mM ferricyanide and variable L-lactate concentration

enzyme: L-lactate dehydrogenase (cytochrome)


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

proof_lines: influence of anions (400 mM KBr) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration

proof_lines: influence of anions (400 mM KCl) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration

proof_lines: influence of anions (400 mM potassium acetate) on the FDH domain steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, constant 10 mM ferricyanide and variable L-lactate concentration


assay_conditions_summary: pH 7; 278.15 K; cofactor FMN

proof_lines: influence of anions (400 mM KBr) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration

proof_lines: influence of anions (200 mM phsophate) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration

proof_lines: influence of anions (400 mM KCl) on the wild-type steady-state kinetic. Reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, 1.5 mM ferricyanide and variable L-lactate concentration


mutation_signature: stopped-flow kinetic parameters for flavin reduction by L-lactate using holo- , reaction conditions: 100 mM phosphate , 1 mM EDTA, , , in the absence of ferrocy

mutation_type: truncation

proof_lines: stopped-flow kinetic parameters for flavin reduction by L-lactate using holo-enzyme, reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, in the absence of ferrocyanide


mutation_signature: stopped-flow kinetic parameters for flavin reduction by L-lactate using FDH domain, reaction conditions: 100 mM phosphate , 1 mM EDTA, , , in the absence of fer

proof_lines: stopped-flow kinetic parameters for flavin reduction by L-lactate using FDH domain, reaction conditions: 100 mM phosphate buffer, 1 mM EDTA, pH 7, 5°C, in the absence of ferrocyanide


enzyme_display_name: D-lactate dehydrogenase (cytochrome)

organism: Arabidopsis thaliana

substrate_name: glycolate

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

enzyme: D-lactate dehydrogenase (cytochrome)

substrate: glycolate


substrate_name: D-glycerate

substrate: D-glycerate


substrate: L-lactate


substrate_name: D-lactate

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

substrate: D-lactate


enzyme_display_name: aryl-alcohol oxidase

organism: Bjerkandera adusta

substrate_name: anisyl alcohol

enzyme: aryl-alcohol oxidase

substrate: anisyl alcohol


organism: Sphingobacterium sp.

substrate_name: veratryl alcohol

substrate: veratryl alcohol


substrate_name: 3,4-dimethoxybenzyl alcohol

substrate: 3,4-dimethoxybenzyl alcohol


enzyme_display_name: UniProt G2PZJ2

organism: Thermothelomyces thermophilus

enzyme: UniProt G2PZJ2


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


organism: Colletotrichum graminicola

substrate_name: 3-anisyl alcohol

substrate: 3-anisyl alcohol


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


substrate_name: 4-anisyl alcohol

substrate: 4-anisyl alcohol


substrate_name: 4-Hydroxybenzyl alcohol

substrate: 4-Hydroxybenzyl alcohol


sequence_variant_note: Mutation signature Y334W could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: benzyl alcohol

substrate: benzyl alcohol


enzyme_display_name: pyranose oxidase

organism: Irpex lacteus

substrate_name: D-fructose

enzyme: pyranose oxidase

substrate: D-fructose


substrate_name: cellobiose

substrate: cellobiose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: D-xylose

substrate: D-xylose


substrate_name: sucrose

substrate: sucrose


organism: Trametes versicolor

substrate_name: beta-D-glucose

substrate: beta-D-glucose


organism: Trametes hirsuta

substrate_name: D-glucose

substrate: D-glucose


enzyme_display_name: UniProt Q7ZA32

organism: Trametes ochracea

substrate_name: D-melibiose

enzyme: UniProt Q7ZA32

substrate: D-melibiose


enzyme_display_name: Pyranose 2-oxidase

enzyme: Pyranose 2-oxidase


enzyme_display_name: UniProt Q5NT46

organism: Mesorhizobium loti

substrate_name: pyridoxine

enzyme: UniProt Q5NT46

substrate: pyridoxine


enzyme_display_name: alcohol oxidase

organism: Phanerodontia chrysosporium

substrate_name: n-butanol

enzyme: alcohol oxidase

substrate: n-butanol


enzyme_display_name: UniProt P04842

organism: Komagataella pastoris

substrate_name: methanol

enzyme: UniProt P04842

substrate: methanol


enzyme_display_name: UniProt Q7X2H8

organism: Arthrobacter globiformis

smiles: CCCCCCO

enzyme: UniProt Q7X2H8


enzyme_display_name: UniProt T2M2J4

proof_lines:
Raw SKiD Env: Temp=23°C, pH=7.5
Raw SKiD Env: Temp=50°C, pH=9

enzyme: UniProt T2M2J4


substrate_name: diethylene glycol

smiles: C(COCCO)O

substrate: diethylene glycol


smiles: CC(CO)O


substrate_name: ethanol

substrate: ethanol


smiles: CC(CCCO)O


smiles: CCCO


smiles: C(CCO)CCO


smiles: C(CCCO)CCO


smiles: C(CCO)CO


smiles: C(CSCCO)O


substrate_name: n-Pentanol

smiles: CCCCCO

substrate: n-Pentanol


smiles: CCCCCCCCCCO


smiles: CCCCCCCO


smiles: CCCCCCCCO


enzyme_display_name: scyllo-inositol 2-dehydrogenase (NADP+)

organism: Bacillus subtilis

substrate_name: NADPH

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

enzyme: scyllo-inositol 2-dehydrogenase (NADP+)

substrate: NADPH


substrate_name: NADP+

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

substrate: NADP+


substrate_name: scyllo-Inositol

substrate: scyllo-Inositol


enzyme_display_name: 3alpha-hydroxysteroid 3-dehydrogenase

organism: Homo sapiens

substrate_name: allopregnanolone

proof_lines: in 100 mM potassium phosphate, pH 7.0, at 25°C

enzyme: 3alpha-hydroxysteroid 3-dehydrogenase

substrate: allopregnanolone


assay_conditions_summary: pH 7; cofactor NADPH


assay_conditions_summary: pH 7; cofactor NADP+


enzyme_display_name: cholesterol oxidase

organism: Rhodococcus erythropolis

substrate_name: cholesterol

enzyme: cholesterol oxidase

substrate: cholesterol


organism: Coprinopsis cinerea

substrate_name: benzyl alcohol

substrate: benzyl alcohol


substrate_name: isovanillyl alcohol

substrate: isovanillyl alcohol


substrate_name: 4-Hydroxybenzyl alcohol

substrate: 4-Hydroxybenzyl alcohol


substrate_name: 3-Hydroxybenzyl alcohol

substrate: 3-Hydroxybenzyl alcohol


substrate_name: 3-anisyl alcohol

substrate: 3-anisyl alcohol


substrate_name: veratryl alcohol

substrate: veratryl alcohol


substrate_name: 4-anisyl alcohol

substrate: 4-anisyl alcohol


substrate_name: Vanillyl alcohol

substrate: Vanillyl alcohol


smiles: CC=CC=CCO


smiles: C/C=C/C=C/CO


organism: Nocardia erythropolis


proof_lines: Km increases when enzyme is entrapped in reverse micelles of the synthetic surfactant aerosol-OT-isooctane


organism: Pimelobacter simplex

substrate_name: stigmasterol

sequence_source: GenBank protein WP_052138420.1 translated from CP009896.1 (Pimelobacter simplex PsChO)

sequence_variant_note: Mutation signature F70V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.5, temperature not specified in the publication, mutant enzyme F70V

substrate: stigmasterol


assay_conditions_summary: pH 7.5; buffer phosphate

normalized_value_unit_evidence: Km normalized_value=0.78961 normalized_unit=mM; kcat normalized_value=1.58 normalized_unit=s^-1; kcat/Km normalized_value=2.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=789.61 +/- 4.71 raw_unit=uM; kcat raw_value=1.58 +/- 0.07 raw_unit=s^-1; kcat/Km raw_value=0.002 +/- 0.0001 raw_unit=uM^-1 s^-1

row_label: stigmasterol; WT

table_label: Table 1. Kinetic parameters of PsChO WT and variants toward five substrates


sequence_variant_note: Mutation signature V64C could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.5, temperature not specified in the publication, mutant enzyme V64C


substrate_name: dehydroepiandrosterone

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

column_label: Table 1 row dehydroepiandrosterone, column WT, lists K_m 341.21 +/- 3.79 uM, kcat 6.82 +/- 0.14 s^-1, and kcat/K_m 0.02 +/- 0.0004 uM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.34121 normalized_unit=mM; kcat normalized_value=6.82 normalized_unit=s^-1; kcat/Km normalized_value=20.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=341.21 +/- 3.79 raw_unit=uM; kcat raw_value=6.82 +/- 0.14 raw_unit=s^-1; kcat/Km raw_value=0.02 +/- 0.0004 raw_unit=uM^-1 s^-1

row_label: dehydroepiandrosterone; WT

substrate: dehydroepiandrosterone


substrate_name: beta-sitosterol

column_label: Table 1 row beta-sitosterol, column WT, lists K_m 328.61 +/- 3.60 uM, kcat 9.86 +/- 0.35 s^-1, and kcat/K_m 0.03 +/- 0.0005 uM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.32861 normalized_unit=mM; kcat normalized_value=9.86 normalized_unit=s^-1; kcat/Km normalized_value=30.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=328.61 +/- 3.60 raw_unit=uM; kcat raw_value=9.86 +/- 0.35 raw_unit=s^-1; kcat/Km raw_value=0.03 +/- 0.0005 raw_unit=uM^-1 s^-1

row_label: beta-sitosterol; WT

substrate: beta-sitosterol


substrate_name: pregnenolone

normalized_value_unit_evidence: Km normalized_value=0.29455 normalized_unit=mM; kcat normalized_value=11.78 normalized_unit=s^-1; kcat/Km normalized_value=40.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=294.55 +/- 2.97 raw_unit=uM; kcat raw_value=11.78 +/- 0.34 raw_unit=s^-1; kcat/Km raw_value=0.04 +/- 0.0005 raw_unit=uM^-1 s^-1

row_label: pregnenolone; WT

substrate: pregnenolone


normalized_value_unit_evidence: Km normalized_value=0.20485 normalized_unit=mM; kcat normalized_value=12.29 normalized_unit=s^-1; kcat/Km normalized_value=60.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=204.85 +/- 3.14 raw_unit=uM; kcat raw_value=12.29 +/- 0.32 raw_unit=s^-1; kcat/Km raw_value=0.06 +/- 0.0003 raw_unit=uM^-1 s^-1

row_label: cholesterol; WT


organism: Mycolicibacterium neoaurum

proof_lines:
pH 7.5, 37°C, full-length isozyme ChoM2
pH 7.5, 37°C


mutation_signature: truncated isozyme ChoM2


substrate_name: dehydroandrosterone

substrate: dehydroandrosterone


substrate_name: diosgenin

proof_lines:
pH 7.5, 37°C
pH 7.5, 37°C, full-length isozyme ChoM2

substrate: diosgenin


sequence_source: UniProtKB E3Q9X3 (CgrAAO; GLRG_02805)

sequence_variant_note: Resolved canonical sequence from UniProtKB E3Q9X3 (CgrAAO; GLRG_02805) and applied mutation signature Y334F with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB E3Q9X3 (CgrAAO; GLRG_02805) and applied mutation signature Y334W with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


organism: Cornu aspersum

substrate_name: Octanol

substrate: Octanol


substrate_name: Tetradecanol

smiles: CCCCCCCCCCCCCCO

substrate: Tetradecanol


substrate_name: Decanol

substrate: Decanol


substrate_name: hexadecanol

smiles: CCCCCCCCCCCCCCCCO

substrate: hexadecanol


substrate_name: Hexanol

smiles: CCCCCCO

substrate: Hexanol


substrate_name: Dodecanol

smiles: CCCCCCCCCCCCO

substrate: Dodecanol


substrate_name: Propanol

substrate: Propanol


substrate_name: butanol

smiles: CCCCO

substrate: butanol


smiles: CCC=CCCCO


organism: Fusarium oxysporum f. sp. lycopersici


substrate_name: veratryl alcohol

substrate: veratryl alcohol


substrate_name: benzyl alcohol

substrate: benzyl alcohol


substrate_name: 4-methoxybenzyl alcohol

substrate: 4-methoxybenzyl alcohol


substrate_name: 3-Methoxybenzyl alcohol

substrate: 3-Methoxybenzyl alcohol


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


organism: Fusarium graminearum


organism: Poria contigua

substrate_name: methanol

smiles: CO

substrate: methanol


substrate_name: ethanol

smiles: CCO

substrate: ethanol


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: n-Propanol

smiles: CCCO

substrate: n-Propanol


substrate_name: n-butanol

substrate: n-butanol


substrate_name: Isopropanol

smiles: CC(C)O

substrate: Isopropanol


smiles: C(CS)O


organism: Ogataea angusta

substrate_name: p-benzoquinone

substrate: p-benzoquinone


smiles: O=O


substrate_name: allyl alcohol

smiles: C=CCO

substrate: allyl alcohol


organism: Mycosarcoma maydis

substrate_name: 2,4-Dimethoxybenzyl alcohol

substrate: 2,4-Dimethoxybenzyl alcohol


substrate_name: anisyl alcohol

substrate: anisyl alcohol


substrate_name: 4-Hydroxybenzyl alcohol

substrate: 4-Hydroxybenzyl alcohol


organism: Ochrobactrum sp.

smiles: CCCCCCCCCCO


smiles: CCCCCCCCO


smiles: CCCCCO


substrate_name: Lactate

substrate: Lactate


substrate_name: glycolate

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

substrate: glycolate


organism: Colletotrichum graminicola


smiles: CCCCCCCO

column_label: PDF Table 1 CgrAlcOx row 1-Heptanol; paper tuple kcat=100 s^-1, Km=0.19 mM, kcat/Km=530 s^-1*mM^-1 differs from export tuple kcat=85.8, Km=0.19, kcat/Km=451.57894736842104.

normalized_value_unit_evidence: kcat normalized_value=100 normalized_unit=s^-1; Km normalized_value=0.19 normalized_unit=mM; kcat/Km normalized_value=530 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: kcat raw_value=100 raw_unit=s^-1; Km raw_value=0.19 raw_unit=mM; kcat/Km raw_value=5.3e5 raw_unit=s^-1*M^-1.

table_label: Table 1. Substrate specificity of CgrAlcOx and CglAlcOx


organism: Phlebiopsis gigantea


substrate_name: D-ribose

substrate: D-ribose


substrate_name: ribitol

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

substrate: ribitol


substrate_name: erythritol

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

substrate: erythritol


organism: Schizophyllum commune

substrate_name: beta-sitosterol

substrate: beta-sitosterol


substrate_name: stigmasterol

substrate: stigmasterol


substrate_name: pregnenolone

substrate: pregnenolone


substrate_name: dehydroepiandrosterone

proof_lines: in the presence and absence of undecanol

substrate: dehydroepiandrosterone


enzyme_display_name: galactose oxidase

organism: Polyporus circinatus

substrate_name: ganglioside

proof_lines: gangliosides in aqueous solution from Tay Sachs disease, competitive non-substrate inhibition

proof_lines: bovine brain gangliosides in aqueous solution, competitive non-substrate inhibition

proof_lines: bovine brain gangliosides in 70% n-propanol, competitive substrate inhibition

enzyme: galactose oxidase

substrate: ganglioside


substrate_name: N-acetyl-D-galactosamine

substrate: N-acetyl-D-galactosamine


substrate_name: D-galactosamine

substrate: D-galactosamine


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


organism: Aspergillus terreus

substrate_name: n-Heptanol

substrate: n-Heptanol


substrate_name: n-dodecanol

smiles: CCCCCCCCCCCCO

substrate: n-dodecanol


proof_lines:
substrate: R-(-)-2-octanol
substrate: n-dodecanol
substrate: n-heptanol


smiles: CCCCCCC(C)O


organism: Basidiomycota

substrate_name: methanol

smiles: CO

substrate: methanol


substrate_name: ethanol

smiles: CCO

substrate: ethanol


substrate_name: n-Propanol

smiles: CCCO

substrate: n-Propanol


substrate_name: n-butanol

smiles: CCCCO

substrate: n-butanol


organism: Thermothelomyces thermophilus

assay_conditions_summary: pH 6; buffer pH 6

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

table_label: Table 1. MtAAOx substrate specificity and kinetic parameters


substrate_name: veratryl alcohol

column_label: Table 1; row veratryl alcohol; KM, kcat, and kcat/KM columns.

row_label: veratryl alcohol

substrate: veratryl alcohol


substrate_name: cinnamyl alcohol

column_label: Table 1; row cinnamyl alcohol; KM, kcat, and kcat/KM columns.

row_label: cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: anisyl alcohol

column_label: Table 1; row anisyl alcohol; KM, kcat, and kcat/KM columns.

row_label: anisyl alcohol

substrate: anisyl alcohol


organism: Pseudomonas sp. 11/12A


organism: Nocardia erythropolis


substrate_name: sitosterol

substrate: sitosterol


substrate_name: fucosterol

substrate: fucosterol


organism: Aspergillus oryzae

substrate_name: D-galactose

substrate: D-galactose


substrate_name: D-xylose

column_label: Table 2; row D-Xylose; AoPOx columns Km, kcat, and kcat/Km.

row_label: D-Xylose / AoPOx

table_label: Table 2

substrate: D-xylose


substrate_name: L-sorbose

column_label: Table 2; row L-Sorbose; AoPOx columns Km, kcat, and kcat/Km.

row_label: L-Sorbose / AoPOx

substrate: L-sorbose


substrate_name: ferricenium hexafluorophosphate

column_label: Table 3; row AoPOx Fc+PF6-; columns Km, kcat, and kcat/Km; footnote b pH 8.0.

row_label: Fc+PF6- / AoPOx

table_label: Table 3

substrate: ferricenium hexafluorophosphate