sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31A to reconstruct the assayed variant sequence.


enzyme_display_name: 2-dehydropantoate 2-reductase

organism: Escherichia coli

substrate_name: NADPH

source_db: oed

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S244A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NADPH

proof_lines: NADPH-dependent reduction of ketopantoate to pantoate

proof_lines: steady-state kinetics of active site mutants R31A, K72A, N98A

data_origin: experimental

enzyme: 2-dehydropantoate 2-reductase

substrate: NADPH

status: unverified

source: oed


mutation_signature: Unknown

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


organism: Thermococcus kodakarensis

source_db: brenda

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

sequence_source: multiple

assay_conditions_summary: pH 6.4; 343.15 K; cofactor NADPH

proof_lines: kcat is 23.1 sec(-1) toward ketopantoate (in the presence of NADH). kcat is 19.7 sec(-1) toward NADH. kcat is 2.22 sec(-1) toward NADPH.

source_databases_merged: brenda skid uniprot

source: brenda


substrate_name: NAD+

assay_conditions_summary: pH 6.4; 343.15 K; cofactor NAD+

substrate: NAD+


substrate_name: (R)-pantoate

assay_conditions_summary: pH 6.4; 343.15 K; cofactor CoA

substrate: (R)-pantoate


substrate_name: NADH

assay_conditions_summary: pH 6.4; 343.15 K; cofactor NADH

substrate: NADH


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

proof_lines:
2-oxopantoate reduction
NADH preference
Thermococcus kodakarensis KPR


proof_lines:
2-oxopantoate reduction
pantoate formation
Thermococcus kodakarensis KPR


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E256A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K176A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K72A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N98A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


proof_lines:
ketopantoate reductase
Escherichia coli
active-site mutants


organism: Candida dubliniensis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H128A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T30A to reconstruct the assayed variant sequence.

column_label: ScienceDirect full text Table 3 row T30A has the exact kcat and Km cells and the rounded explicit kcat/Km cell.

normalized_value_unit_evidence: kcat normalized_value=15.5 normalized_unit=s^-1; Km normalized_value=3.5 normalized_unit=mM; paper explicit kcat/Km=4.43 s^-1 mM^-1 while CatLog stores computed 4.428571428571429.

raw_value_unit_evidence: Table 3 row T30A reports kcat=15.5 s^-1, Km=3.5 mM, and kcat/Km=4.43 s^-1 mM^-1.

row_label: T30A mutant form of CduCPR

table_label: ScienceDirect full text Table 3: Kinetic comparisons between wild-type and mutant forms of CduCPR

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H128A to reconstruct the assayed variant sequence.


organism: Escherichia coli (strain K12)

substrate_name: pantoate

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

assay_conditions_summary: cofactor NADPH

substrate: pantoate

source: uniprot


substrate_name: NADP(+)

assay_conditions_summary: cofactor NADP+

substrate: NADP(+)


organism: Homo sapiens

assay_conditions_summary: cofactor NADH


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

verification_status: verified

assay_conditions_summary: pH 6.25; 315.15 K; cofactor NADPH

column_label: Abstract reports apparent Km constants for NADPH and ketopantoic acid were 0.776 +/- 0.09 mM and 0.742 +/- 0.01 mM respectively.

raw_value_unit_evidence: Km raw_value=0.776 mM raw_unit=mM

row_label: Salmonella typhimurium ApbA ketopantoic acid reductase / NADPH

table_label: PubMed XML abstract PMID 9488683

status: verified


raw_value_unit_evidence: Km raw_value=0.742 mM raw_unit=mM

row_label: Salmonella typhimurium ApbA ketopantoic acid reductase / ketopantoic acid


enzyme_display_name: UniProt P0A9J4

source_db: skid

assay_conditions_summary: pH 7.5; 300.15 K; cofactor NADPH

proof_lines:
Raw SKiD Env: Temp=27°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

source_databases_merged: skid uniprot

enzyme: UniProt P0A9J4

source: skid


enzyme_display_name: 12alpha-hydroxysteroid dehydrogenase

organism: [Clostridium] scindens

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

assay_conditions_summary: pH 7; cofactor NADPH

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

enzyme: 12alpha-hydroxysteroid dehydrogenase


substrate_name: 12-oxolithocholic acid

assay_conditions_summary: pH 7

substrate: 12-oxolithocholic acid


substrate_name: NADP+

assay_conditions_summary: pH 7.5; cofactor NADP+

proof_lines: at pH 7.5, temperature not specified in the publication

substrate: NADP+


substrate_name: deoxycholic acid

substrate: deoxycholic acid


organism: Archaeoglobus fulgidus

assay_conditions_summary: pH 6.6; 343.15 K; cofactor NADP+


substrate_name: L-alpha-glycerol 3-phosphate

substrate: L-alpha-glycerol 3-phosphate


substrate_name: D-glyceraldehyde 3-phosphate

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

substrate: D-glyceraldehyde 3-phosphate


organism: Peptacetobacter hiranonis


assay_conditions_summary: pH 7; cofactor NADP+


enzyme_display_name: 2-oxoadipate reductase

enzyme: 2-oxoadipate reductase


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


organism: [Clostridium] hylemonae


assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: at pH 8.0, temperature not specified in the publication


assay_conditions_summary: pH 8


organism: Eggerthella sp. CAG:298

substrate_name: 12-oxo-deoxycholic acid

proof_lines: coenzyme: NADPH, pH 7.0, temperature not specified in the publication

substrate: 12-oxo-deoxycholic acid


proof_lines: coenzyme: NADP+, pH 7.0, temperature not specified in the publication


enzyme_display_name: L-rhamnose 1-dehydrogenase

organism: Aureobasidium pullulans

assay_conditions_summary: cofactor NAD+

enzyme: L-rhamnose 1-dehydrogenase


substrate_name: L-rhamnose

substrate: L-rhamnose


organism: Eggerthella lenta

proof_lines: with NADH as cosubstrate, pH and temperature not specified in the publication


proof_lines: with NAD+ as cosubstrate, pH and temperature not specified in the publication


enzyme_display_name: D-xylose 1-dehydrogenase

organism: Arthrobacter sp.

substrate_name: D-xylose

enzyme: D-xylose 1-dehydrogenase

substrate: D-xylose


organism: Debaryomyces hansenii


enzyme_display_name: D-xylose 1-dehydrogenase (NADP+, D-xylono-1,5-lactone-forming)

organism: Haloarcula marismortui

substrate_name: D-glucose

substrate: D-glucose


enzyme: D-xylose 1-dehydrogenase (NADP+, D-xylono-1,5-lactone-forming)


organism: Bifidobacterium sp.

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


organism: Clostridium perfringens


organism: [Clostridium] leptum


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

substrate_name: acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 7.0 and 25 degrees Celsius)

assay_conditions_summary: pH 7; cofactor NADH

proof_lines: kcat is 458 min(-1) for DL-3-hydroxybutyryl-CoA (PubMed:28888424). kcat is 706 min(-1) for allopregnanolone (PubMed:28888424).

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


substrate_name: beta-hydroxybutyryl-CoA (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

assay_conditions_summary: pH 9.3; cofactor CoA


substrate_name: androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: isoursodeoxycholic acid (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: dehydrocorticosterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: NADH (in the presence of acetoacetyl-CoA, at pH 7.0 and 25 degrees Celsius)


substrate_name: NAD (in the presence of beta-hydroxybutyryl-CoA, at pH 9.3 and 25 degrees Celsius)


organism: Scheffersomyces stipitis

substrate_name: L-Lyxose

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

source_databases_merged: brenda uniprot

substrate: L-Lyxose


substrate_name: L-Mannose

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

substrate: L-Mannose


organism: Macaca fuscata

substrate_name: NADPH

substrate: NADPH


substrate_name: NADP+


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


substrate_name: Camphorquinone

substrate: Camphorquinone


organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15)

substrate_name: D-xylose (at pH 9)

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

assay_conditions_summary: pH 9

proof_lines: kcat is 1360 min(-1) with D-xylose as substrate (at pH 9). kcat is 1455 min(-1) with L-arabinose as substrate (at pH 9). kcat is 1860 min(-1) with NAD(+) as substrate (at pH 9).

substrate: D-xylose (at pH 9)


substrate_name: NAD(+) (at pH 9)

substrate: NAD(+) (at pH 9)


organism: Paenarthrobacter nicotinovorans

substrate_name: NAD+

assay_conditions_summary: pH 7.8; cofactor NAD+

substrate: NAD+


substrate_name: D-xylose

assay_conditions_summary: pH 7.8; cofactor NADP+

proof_lines:
28°C, pH 7.8, with NADP+ as cofactor
kcat is 14.9 sec(-1).


enzyme_display_name: D-xylose dehydrogenase

substrate_name: NADP(+)

enzyme: D-xylose dehydrogenase

substrate: NADP(+)


organism: Homo sapiens

assay_conditions_summary: cofactor CoA


substrate_name: tetramyristoyl cardiolipin

substrate: tetramyristoyl cardiolipin


substrate_name: tetralinoleoyl cardiolipin

substrate: tetralinoleoyl cardiolipin


substrate_name: L-rhamnose

proof_lines:
pH 9.0, 30°C, recombinant enzyme
pH 8.0, 30°C, recombinant enzyme


organism: Macaca fuscata fuscata

substrate_name: naphthalene dihydrodiol (at pH 10.0)

assay_conditions_summary: pH 10

substrate: naphthalene dihydrodiol (at pH 10.0)


substrate_name: benzene dihydrodiol (at pH 10.0)

substrate: benzene dihydrodiol (at pH 10.0)


substrate_name: 3-deoxyglucosone (at pH 7.5)

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

substrate: 3-deoxyglucosone (at pH 7.5)


substrate_name: methylglyoxal (at pH 7.5)

smiles: CC(=O)C=O

substrate: methylglyoxal (at pH 7.5)


substrate_name: D-glucose (at pH 7.5)

substrate: D-glucose (at pH 7.5)


organism: Clostridium sp. (strain ATCC 29733 / VPI C48-50)

substrate_name: NADP(+) (at pH 8.0 and 25 degrees Celsius)

column_label: Wiley full-text abstract kinetic constants paragraph | row NADP(+) | column Km, NADP = 35 uM NADP

raw_value_unit_evidence: Km 35 uM NADP

row_label: NADP(+)


substrate_name: cholate (at pH 8.0 and 25 degrees Celsius)

column_label: Wiley full-text abstract kinetic constants paragraph | row cholate | column Km, cholic acid = 72 uM cholic acid

raw_value_unit_evidence: Km 72 uM cholic acid

row_label: cholate


substrate_name: deoxycholate (at pH 8.0 and 25 degrees Celsius)

column_label: Wiley full-text abstract kinetic constants paragraph | row deoxycholate | column Km, deoxycholic acid = 45 uM deoxycholic acid

raw_value_unit_evidence: Km 45 uM deoxycholic acid

row_label: deoxycholate


substrate_name: 3alpha,7alpha-dihydroxy-12-oxo-5beta-cholanate (12-oxochenodeoxycholate) (at pH 8.0 and 25 degrees Celsius)

column_label: Abstract reports 12-oxochenodeoxylic acid, Km = 12 microns, under conditions of 0.1 M potassium phosphate, pH 8.0, 25 degrees C.

raw_value_unit_evidence: Km raw_value=12 microns raw_unit=microM

row_label: Clostridium group P strain C48-50 12 alpha-HSDH / 12-oxochenodeoxylic acid

table_label: PubMed XML abstract PMID 2007406


organism: Clostridium sp.

substrate_name: 12-oxochenodeoxycholic acid

column_label: Wiley full-text abstract kinetic constants paragraph | row 12-oxochenodeoxycholic acid | column Km, 12-oxochenodeoxycholic acid = 12 uM 12-oxochenodeoxycholic acid

raw_value_unit_evidence: Km 12 uM 12-oxochenodeoxycholic acid

row_label: 12-oxochenodeoxycholic acid

substrate: 12-oxochenodeoxycholic acid


substrate_name: NADPH

assay_conditions_summary: pH 8; cofactor NADPH

column_label: Wiley full-text abstract kinetic constants paragraph | row NADPH | column Km, NADPH = 8.5 uM NADPH

raw_value_unit_evidence: Km 8.5 uM NADPH

row_label: NADPH


substrate_name: NADP+

column_label: Wiley full-text abstract kinetic constants paragraph | row NADP+ | column Km, NADP = 35 uM NADP

row_label: NADP+

substrate: NADP+


substrate_name: deoxycholic acid

column_label: Wiley full-text abstract kinetic constants paragraph | row deoxycholic acid | column Km, deoxycholic acid = 45 uM deoxycholic acid

row_label: deoxycholic acid

substrate: deoxycholic acid


substrate_name: cholic acid

column_label: Wiley full-text abstract kinetic constants paragraph | row cholic acid | column Km, cholic acid = 72 uM cholic acid

row_label: cholic acid

substrate: cholic acid


organism: Canis lupus familiaris

substrate_name: naphthalene dihydrodiol (at pH 7.5)

substrate: naphthalene dihydrodiol (at pH 7.5)


substrate_name: benzene dihydrodiol (at pH 7.5)

substrate: benzene dihydrodiol (at pH 7.5)


substrate_name: D-xylose

substrate: D-xylose


substrate_name: camphorquinone (at pH 7.5)

substrate: camphorquinone (at pH 7.5)


enzyme_display_name: D-xylose 1-dehydrogenase (NADP(+), D-xylono-1,5-lactone-forming)

substrate_name: D-glucose

substrate: D-glucose


substrate_name: D-ribose

enzyme: D-xylose 1-dehydrogenase (NADP(+), D-xylono-1,5-lactone-forming)

substrate: D-ribose


substrate_name: D-Xylose

substrate: D-Xylose


organism: Trichoderma reesei

substrate_name: D-Arabinose

assay_conditions_summary: pH 8.1; 303.15 K; buffer 100 mM Tris/HCl pH 8; cofactor NADP+

column_label: Official PMC Table 2 row D-Arabinose: Vmax 100 nkat mg^-1 | kcat 4.4 s^-1 | Km 390.0 mM | Efficacy 11.0 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=4.4 normalized_unit=s^-1; Km normalized_value=390 normalized_unit=mM; kcat/Km ratio normalized_value=0.011282051282051283 normalized_unit=s^-1*mM^-1; printed efficacy normalized_value=0.011 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 D-Arabinose cells: Vmax raw_value=100 raw_unit=nkat mg^-1; kcat raw_value=4.4 raw_unit=s^-1; Km raw_value=390.0 raw_unit=mM; efficacy raw_value=11.0 raw_unit=s^-1 M^-1.

row_label: D-Arabinose

table_label: Table 2. The kinetic properties of the histidine-tagged and purified XYD1 with respect to different sugars: the NADP+ concentration was 0.8 mM.

substrate: D-Arabinose


substrate_name: D-Galactose

column_label: Official PMC Table 2 row D-Galactose: Vmax 205 nkat mg^-1 | kcat 8.9 s^-1 | Km 100.0 mM | Efficacy 89.0 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=8.9 normalized_unit=s^-1; Km normalized_value=100 normalized_unit=mM; kcat/Km ratio normalized_value=0.08900000000000001 normalized_unit=s^-1*mM^-1; printed efficacy normalized_value=0.089 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 D-Galactose cells: Vmax raw_value=205 raw_unit=nkat mg^-1; kcat raw_value=8.9 raw_unit=s^-1; Km raw_value=100.0 raw_unit=mM; efficacy raw_value=89.0 raw_unit=s^-1 M^-1.

row_label: D-Galactose

substrate: D-Galactose


substrate_name: D-Glucose

column_label: Official PMC Table 2 row D-Glucose: Vmax 130 nkat mg^-1 | kcat 5.7 s^-1 | Km 24.0 mM | Efficacy 240.0 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=5.7 normalized_unit=s^-1; Km normalized_value=24 normalized_unit=mM; kcat/Km ratio normalized_value=0.23750000000000002 normalized_unit=s^-1*mM^-1; printed efficacy normalized_value=0.24 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 D-Glucose cells: Vmax raw_value=130 raw_unit=nkat mg^-1; kcat raw_value=5.7 raw_unit=s^-1; Km raw_value=24.0 raw_unit=mM; efficacy raw_value=240.0 raw_unit=s^-1 M^-1.

row_label: D-Glucose

substrate: D-Glucose


substrate_name: D-Ribose

column_label: Official PMC Table 2 row D-Ribose: Vmax 141 nkat mg^-1 | kcat 6.2 s^-1 | Km 145.0 mM | Efficacy 43.0 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=6.2 normalized_unit=s^-1; Km normalized_value=145 normalized_unit=mM; kcat/Km ratio normalized_value=0.04275862068965517 normalized_unit=s^-1*mM^-1; printed efficacy normalized_value=0.043 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 D-Ribose cells: Vmax raw_value=141 raw_unit=nkat mg^-1; kcat raw_value=6.2 raw_unit=s^-1; Km raw_value=145.0 raw_unit=mM; efficacy raw_value=43.0 raw_unit=s^-1 M^-1.

row_label: D-Ribose

substrate: D-Ribose


column_label: Official PMC Table 2 row D-Xylose: Vmax 500 nkat mg^-1 | kcat 21.8 s^-1 | Km 43.0 mM | Efficacy 510.0 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=21.8 normalized_unit=s^-1; Km normalized_value=43 normalized_unit=mM; kcat/Km ratio normalized_value=0.5069767441860465 normalized_unit=s^-1*mM^-1; printed efficacy normalized_value=0.51 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 D-Xylose cells: Vmax raw_value=500 raw_unit=nkat mg^-1; kcat raw_value=21.8 raw_unit=s^-1; Km raw_value=43.0 raw_unit=mM; efficacy raw_value=510.0 raw_unit=s^-1 M^-1.

row_label: D-Xylose


substrate_name: L-Arabinose

column_label: Official PMC Table 2 row L-Arabinose: Vmax 117 nkat mg^-1 | kcat 5.1 s^-1 | Km 60.0 mM | Efficacy 85.0 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=5.1 normalized_unit=s^-1; Km normalized_value=60 normalized_unit=mM; kcat/Km ratio normalized_value=0.08499999999999999 normalized_unit=s^-1*mM^-1; printed efficacy normalized_value=0.085 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 L-Arabinose cells: Vmax raw_value=117 raw_unit=nkat mg^-1; kcat raw_value=5.1 raw_unit=s^-1; Km raw_value=60.0 raw_unit=mM; efficacy raw_value=85.0 raw_unit=s^-1 M^-1.

row_label: L-Arabinose

substrate: L-Arabinose


enzyme_display_name: D-xylose 1-dehydrogenase (NADP(+))

organism: Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30)

substrate_name: NADP(+)

assay_conditions_summary: pH 8.1; buffer 100 mM Tris/HCl pH 8; cofactor NADP+

column_label: Official PMC article line 1432: NADP+ Km 250 +/- 90 uM and Vmax 510 +/- 20 nkat mg^-1.

normalized_value_unit_evidence: Km normalized_value=0.25 normalized_unit=mM; Vmax raw context preserved but not used as exported kcat.

raw_value_unit_evidence: Text line 1432 reports Km for NADP+ raw_value=250 +/- 90 raw_unit=uM and Vmax raw_value=510 +/- 20 raw_unit=nkat mg^-1.

table_label: Text kinetic constants paragraph

enzyme: D-xylose 1-dehydrogenase (NADP(+))

substrate: NADP(+)


substrate_name: D-arabinose

substrate: D-arabinose


organism: Sus scrofa

assay_conditions_summary: pH 7.5; 303.15 K; buffer pH 7; cofactor NADP+

column_label: Table 2: Substrate-specificity of D-xylose dehydrogenase (Biochem. J. 1990, volume 266, pages 637-644); printed column heads Sugar | Vmax. (units/mg of protein) | Km(app.) (M) | kcat. (s^-1) | Ksp. (M^-1 s^-1). Table 2, sugar row 2-Deoxy-D-glucose; column Km(app.) (M) = 0.054; column kcat. (s^-1) = 22; column Ksp. (M^-1 s^-1) = 407; column Vmax. (units/mg of protein) = 2.9. captured primary segment: 2-Deoxy-D-glucose | Km 0.054 M | kcat 22 s^-1 | kcat/Km 407 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 0.054 M; 1 M is 1000 mM, so 0.054 x 1000 = 54.0 mM; the exported value is 54.0 mM. kcat: printed Table 2 cell 22 s^-1; already in s^-1, so no unit conversion applies (this table prints no min^-1 kinetic cell); the exported value is 22.0 s^(-1). kcat/Km: printed Table 2 Ksp. cell 407 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 407 / 1000 = 0.407 s^(-1)*mM^(-1). Quotient disclosure for this row: 22.0 / 54.0 = 0.4074074074074074 s^-1 mM^-1, the exported value, and 22 / 0.054 = 407.41 M^-1 s^-1 rounds to the printed Ksp. cell 407 M^-1 s^-1.

raw_value_unit_evidence: Table 2, sugar row 2-Deoxy-D-glucose: Km(app.) = 0.054 M; kcat = 22 s^-1; printed Ksp (kcat/Km) = 407 M^-1 s^-1; Vmax = 2.9 units/mg of protein.

row_label: Table 2, sugar row 2-Deoxy-D-glucose


column_label: Table 2: Substrate-specificity of D-xylose dehydrogenase (Biochem. J. 1990, volume 266, pages 637-644); printed column heads Sugar | Vmax. (units/mg of protein) | Km(app.) (M) | kcat. (s^-1) | Ksp. (M^-1 s^-1). Table 2, sugar row D-Arabinose; column Km(app.) (M) = 0.13; column kcat. (s^-1) = 9; column Ksp. (M^-1 s^-1) = 69; column Vmax. (units/mg of protein) = 1.2. captured primary segment: D-Arabinose | Km 0.13 M | kcat 9 s^-1 | kcat/Km 69 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 0.13 M; 1 M is 1000 mM, so 0.13 x 1000 = 130.0 mM; the exported value is 130.0 mM. kcat: printed Table 2 cell 9 s^-1; already in s^-1, so no unit conversion applies (this table prints no min^-1 kinetic cell); the exported value is 9.0 s^(-1). kcat/Km: printed Table 2 Ksp. cell 69 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 69 / 1000 = 0.069 s^(-1)*mM^(-1). Quotient disclosure for this row: 9.0 / 130.0 = 0.06923076923076923 s^-1 mM^-1, the exported value, and 9 / 0.13 = 69.23 M^-1 s^-1 rounds to the printed Ksp. cell 69 M^-1 s^-1.

raw_value_unit_evidence: Table 2, sugar row D-Arabinose: Km(app.) = 0.13 M; kcat = 9 s^-1; printed Ksp (kcat/Km) = 69 M^-1 s^-1; Vmax = 1.2 units/mg of protein.

row_label: Table 2, sugar row D-Arabinose


column_label: Table 2: Substrate-specificity of D-xylose dehydrogenase (Biochem. J. 1990, volume 266, pages 637-644); printed column heads Sugar | Vmax. (units/mg of protein) | Km(app.) (M) | kcat. (s^-1) | Ksp. (M^-1 s^-1). Table 2, sugar row D-Galactose; column Km(app.) (M) = 0.14; column kcat. (s^-1) = 12; column Ksp. (M^-1 s^-1) = 86; column Vmax. (units/mg of protein) = 1.5. captured primary segment: D-Galactose | Km 0.14 M | kcat 12 s^-1 | kcat/Km 86 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 0.14 M; 1 M is 1000 mM, so 0.14 x 1000 = 140.0 mM; the exported value is 140.0 mM. kcat: printed Table 2 cell 12 s^-1; already in s^-1, so no unit conversion applies (this table prints no min^-1 kinetic cell); the exported value is 12.0 s^(-1). kcat/Km: printed Table 2 Ksp. cell 86 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 86 / 1000 = 0.086 s^(-1)*mM^(-1). Quotient disclosure for this row: 12.0 / 140.0 = 0.08571428571428572 s^-1 mM^-1, the exported value, and 12 / 0.14 = 85.71 M^-1 s^-1 rounds to the printed Ksp. cell 86 M^-1 s^-1.

raw_value_unit_evidence: Table 2, sugar row D-Galactose: Km(app.) = 0.14 M; kcat = 12 s^-1; printed Ksp (kcat/Km) = 86 M^-1 s^-1; Vmax = 1.5 units/mg of protein.

row_label: Table 2, sugar row D-Galactose


column_label: Table 2: Substrate-specificity of D-xylose dehydrogenase (Biochem. J. 1990, volume 266, pages 637-644); printed column heads Sugar | Vmax. (units/mg of protein) | Km(app.) (M) | kcat. (s^-1) | Ksp. (M^-1 s^-1). Table 2, sugar row D-Glucose; column Km(app.) (M) = 0.049; column kcat. (s^-1) = 16; column Ksp. (M^-1 s^-1) = 326; column Vmax. (units/mg of protein) = 1.1. captured primary segment: D-Glucose | Km 0.049 M | kcat 16 s^-1 | kcat/Km 326 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 0.049 M; 1 M is 1000 mM, so 0.049 x 1000 = 49.0 mM; the exported value is 49.0 mM. kcat: printed Table 2 cell 16 s^-1; already in s^-1, so no unit conversion applies (this table prints no min^-1 kinetic cell); the exported value is 16.0 s^(-1). kcat/Km: the paper prints its own Table 2 Ksp. cell 326 M^-1 s^-1, defined by the paper as the ratio kcat./Km(app); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 326 / 1000 = 0.326 s^(-1)*mM^(-1). Quotient disclosure for this row: 16 / 0.049 = 326.53 M^-1 s^-1 in the printed unit.

raw_value_unit_evidence: Table 2, sugar row D-Glucose: Km(app.) = 0.049 M; kcat = 16 s^-1; printed Ksp (kcat/Km) = 326 M^-1 s^-1; Vmax = 1.1 units/mg of protein.

row_label: Table 2, sugar row D-Glucose


column_label: Table 2: Substrate-specificity of D-xylose dehydrogenase (Biochem. J. 1990, volume 266, pages 637-644); printed column heads Sugar | Vmax. (units/mg of protein) | Km(app.) (M) | kcat. (s^-1) | Ksp. (M^-1 s^-1). Table 2, sugar row D-Ribose; column Km(app.) (M) = 0.027; column kcat. (s^-1) = 40; column Ksp. (M^-1 s^-1) = 1481; column Vmax. (units/mg of protein) = 5.2. captured primary segment: D-Ribose | Km 0.027 M | kcat 40 s^-1 | kcat/Km 1481 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 0.027 M; 1 M is 1000 mM, so 0.027 x 1000 = 27.0 mM; the exported value is 27.0 mM. kcat: printed Table 2 cell 40 s^-1; already in s^-1, so no unit conversion applies (this table prints no min^-1 kinetic cell); the exported value is 40.0 s^(-1). kcat/Km: printed Table 2 Ksp. cell 1481 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1481 / 1000 = 1.481 s^(-1)*mM^(-1). Quotient disclosure for this row: 40.0 / 27.0 = 1.4814814814814814 s^-1 mM^-1, the exported value, and 40 / 0.027 = 1481.48 M^-1 s^-1 rounds to the printed Ksp. cell 1481 M^-1 s^-1.

raw_value_unit_evidence: Table 2, sugar row D-Ribose: Km(app.) = 0.027 M; kcat = 40 s^-1; printed Ksp (kcat/Km) = 1481 M^-1 s^-1; Vmax = 5.2 units/mg of protein.

row_label: Table 2, sugar row D-Ribose


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADP+


proof_lines: L-arabinose D-xylose D-ribose


organism: Caulobacter vibrioides

substrate_name: NAD+

assay_conditions_summary: pH 6.8; 298.15 K; cofactor NAD+

substrate: NAD+


organism: Pseudomonas putida


organism: Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)

substrate_name: NAD

substrate: NAD


substrate_name: D-xylose (at pH 7.5)

assay_conditions_summary: pH 7.5; cofactor NADP+

column_label: Table 2. Kinetic constants of dimeric DDs and pig liver XDH for monosaccharides; row label: d-xylose; column label: Pig DD column Km; raw value 0.8 mM; normalized value 0.8 mM.

raw_value_unit_evidence: Table 2. Kinetic constants of dimeric DDs and pig liver XDH for monosaccharides; d-xylose row / Pig DD column; Km=0.8 mM.

row_label: d-xylose row / Pig DD column

substrate: D-xylose (at pH 7.5)


organism: Arthrobacter nicotinovorans

assay_conditions_summary: pH 7.8; 301.15 K; cofactor NADP+

column_label: XDH prose paragraph; ORF40 coenzyme preference; metrics named in prose: Km, kcat, kcat/Km for NAD+.

normalized_value_unit_evidence: kcat paper=1.5 s^-1; Km paper=5.03 mM; kcat/Km paper=0.298 s^-1 mM^-1

row_label: ORF40/XDH NAD+ coenzyme row

table_label: XDH prose kinetics


substrate_name: NADP+

column_label: XDH prose paragraph; ORF40 coenzyme preference; metrics named in prose: Km, kcat, kcat/Km for NADP+.

normalized_value_unit_evidence: kcat paper=10.5 s^-1; Km paper=0.32 mM; kcat/Km paper=32 s^-1 mM^-1

row_label: ORF40/XDH NADP+ coenzyme row

substrate: NADP+


enzyme_display_name: D-xylose 1-dehydrogenase (NADP(+)) 2

organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)

assay_conditions_summary: cofactor NADP+

column_label: apparent Km for D-xylose

normalized_value_unit_evidence: HVO_B0029 paragraph supports Km 89 mM for D-xylose.

raw_value_unit_evidence: HVO_B0029 paragraph reports apparent Km for D-xylose of 89 +/- 1 mM.

row_label: HVO_B0029 gene product; D-xylose substrate

table_label: Prose immediately after Table 4: HVO_B0029 reactivated enzyme

enzyme: D-xylose 1-dehydrogenase (NADP(+)) 2


substrate_name: NADP

column_label: apparent Km for NADP+

normalized_value_unit_evidence: HVO_B0029 paragraph supports Km 0.75 mM for NADP+.

raw_value_unit_evidence: HVO_B0029 paragraph reports apparent Km for NADP+ of 0.75 +/- 0.06 mM.

row_label: HVO_B0029 gene product; NADP+ cosubstrate

substrate: NADP


substrate_name: Camphorquinone

proof_lines:
Cynomolgus and Japanese monkey kidneys
dimeric dihydrodiol dehydrogenase

substrate: Camphorquinone


substrate_name: D-xylose

proof_lines: Mammalian dimeric dihydrodiol dehydrogenase

substrate: D-xylose


organism: Oryctolagus cuniculus

proof_lines:
dimeric dihydrodiol dehydrogenase
D-xylose dehydrogenase
rabbit lens


enzyme_display_name: geraniol dehydrogenase (NADP(+))

organism: Zingiber officinale

substrate_name: geraniol

smiles: CC(C)=CCC/C(C)=C/CO

enzyme: geraniol dehydrogenase (NADP(+))

substrate: geraniol


substrate_name: nerol

smiles: CC(C)=CCC/C(C)=C\CO

substrate: nerol


enzyme_display_name: carbonyl reductase (NADPH)

organism: Bacillus subtilis

substrate_name: NADPH

enzyme: carbonyl reductase (NADPH)

substrate: NADPH


substrate_name: ethyl 4-chloroacetoacetate

smiles: CCOC(=O)CC(=O)CCl

substrate: ethyl 4-chloroacetoacetate


enzyme_display_name: UniProt B2KJ46

organism: Candida parapsilosis

source_license: CC BY-NC-ND 4.0

enzyme: UniProt B2KJ46


proof_lines:
Raw SKiD Env: Temp=35°C, pH=5
Raw SKiD Env: Temp=-----, pH=-----


substrate_name: NADH

substrate: NADH


enzyme_display_name: UniProt F1N9C1

organism: Gallus gallus

substrate_name: testosterone

enzyme: UniProt F1N9C1

substrate: testosterone


substrate_name: estrone

substrate: estrone


substrate_name: prostaglandin E2

substrate: prostaglandin E2


substrate_name: acetone

smiles: CC(=O)C

substrate: acetone


substrate_name: p-toluquinone

substrate: p-toluquinone


substrate_name: menadione

substrate: menadione


substrate_name: isatin

substrate: isatin


enzyme_display_name: UniProt P16152

organism: Homo sapiens

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

enzyme: UniProt P16152


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


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


enzyme_display_name: UniProt Q28960

enzyme: UniProt Q28960


enzyme_display_name: UniProt Q5FQJ0

organism: Gluconobacter oxydans

substrate_name: methylglyoxal

enzyme: UniProt Q5FQJ0

substrate: methylglyoxal


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


enzyme_display_name: UniProt Q9X265

organism: Thermotoga maritima

substrate_name: ethyl 2-methylacetoacetate

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

enzyme: UniProt Q9X265

substrate: ethyl 2-methylacetoacetate


substrate_name: ethyl 2-oxo-4-phenylbutyrate

substrate: ethyl 2-oxo-4-phenylbutyrate


enzyme_display_name: UniProt Q9Y8Y1

organism: Aeropyrum pernix

enzyme: UniProt Q9Y8Y1


substrate_name: ethyl 4-chloro-3-oxobutanoate

substrate: ethyl 4-chloro-3-oxobutanoate


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


substrate_name: doxorubicin

substrate: doxorubicin


substrate_name: oracin

substrate: oracin


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


organism: Methanobacterium palustre

substrate_name: acetoin

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

substrate: acetoin


smiles: CC(C)O


substrate_name: NADP+

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

substrate: NADP+


substrate_name: diacetyl

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

substrate: diacetyl


km_display: Not reported

smiles: CCCC(C)O


substrate_name: Cyclohexanol

substrate: Cyclohexanol


substrate_name: Cycloheptanone

substrate: Cycloheptanone


smiles: CCCC(=O)C


smiles: CC(C(C)O)O


substrate_name: Cyclopentanone

substrate: Cyclopentanone


smiles: CCC(=O)C


substrate_name: cyclohexanone

substrate: cyclohexanone


substrate_name: Cyclopentanol

substrate: Cyclopentanol


smiles: CCC(C)O


substrate_name: propanone

substrate: propanone


substrate_name: NADPH

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

substrate: NADPH


organism: Starmerella magnoliae

assay_conditions_summary: cofactor NADPH


substrate_name: ethyl 2-chloro-3-oxobutanoate

smiles: CCOC(=O)C(C(=O)C)Cl

substrate: ethyl 2-chloro-3-oxobutanoate


substrate_name: methyl 4-chloro-3-oxobutanoate

smiles: COC(=O)CC(=O)CCl

substrate: methyl 4-chloro-3-oxobutanoate


substrate_name: ketopantoyl lactone

substrate: ketopantoyl lactone


substrate_name: ethyl pyruvate

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

substrate: ethyl pyruvate


substrate_name: methyl 2-chloro-3-oxobutanoate

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

substrate: methyl 2-chloro-3-oxobutanoate


substrate_name: ethyl 2-oxobutanoate

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

substrate: ethyl 2-oxobutanoate


enzyme_display_name: geraniol dehydrogenase (NADP+)

organism: Cymbopogon flexuosus

substrate_name: geranial

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

enzyme: geraniol dehydrogenase (NADP+)

substrate: geranial


substrate_name: geraniol

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

substrate: geraniol


substrate_name: NADP+

substrate: NADP+


organism: Persicaria minor

assay_conditions_summary: pH 9.5; 310.15 K; cofactor NADP+

proof_lines: isoform geraniol-DH I, in 100 mM glycine-NaOH, pH 9.5, at 37°C

proof_lines: isoform geraniol-DH II, in 100 mM glycine-NaOH, pH 9.5, at 37°C


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: linalool

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

substrate: linalool


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


substrate_name: NADH

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

assay_conditions_summary: pH 7.5; 308.15 K; cofactor NADPH

substrate: NADH


mutation_type: deletion

proof_lines: deletion mutant lacking 31 N-terminal amino acids, pH 7.5, 35°C


mutation_signature: deletion mutant lacking 31 N-terminal amino acids


substrate_name: NADPH; 4-Oxonon-2-enal

substrate: NADPH; 4-Oxonon-2-enal


substrate_name: 4-Oxonon-2-enal; NADPH

substrate: 4-Oxonon-2-enal; NADPH


substrate_name: menadione

substrate: menadione


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


smiles: CCCCCC(=O)/C=C/C=O

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH


organism: Mus musculus

substrate_name: doxorubicin

substrate: doxorubicin


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


substrate_name: NADPH

assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH

substrate: NADPH


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


assay_conditions_summary: pH 5; 308.15 K; buffer 100 mM acetate; cofactor NADPH

proof_lines: mutant S67D/H68D, with NADPH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)


assay_conditions_summary: pH 5; 308.15 K; buffer 100 mM acetate; cofactor NADH

proof_lines: wild-type, with NADH as cofactor, at 35°C in 100 mM acetate buffer (pH 5.0)


proof_lines:
mutant H68D/P69D, NADPH as cofactor
mutant H68D/P69D, NADH as cofactor


proof_lines:
mutant H68D, NADPH as cofactor
mutant H68D, NADH as cofactor


proof_lines:
mutant P69D, NADPH as cofactor
mutant P69D, NADH as cofactor


proof_lines:
mutant S67D/P69D, NADPH as cofactor
mutant S67D/P69D, NADH as cofactor


proof_lines:
mutant S67D, NADPH as cofactor
mutant S67D, NADH as cofactor


enzyme_display_name: L-glycol dehydrogenase

organism: Klebsiella aerogenes

assay_conditions_summary: cofactor NADH

proof_lines:
with ethyl pyruvate
with 2,3-pentadione
with diacetyl

enzyme: L-glycol dehydrogenase


substrate_name: diacetyl

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

substrate: diacetyl


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


substrate_name: ethyl pyruvate

substrate: ethyl pyruvate


substrate_name: ethyl 4-chloro-3-oxobutanoate

smiles: CCOC(=O)CC(=O)CCl

substrate: ethyl 4-chloro-3-oxobutanoate


substrate_name: p-toluquinone

substrate: p-toluquinone


assay_conditions_summary: pH 6; 323.15 K; cofactor NADPH


enzyme_display_name: GDP-4-dehydro-D-rhamnose reductase

organism: Pseudomonas sp.

proof_lines:
with NADPH as reductant
with NADH as reductant

enzyme: GDP-4-dehydro-D-rhamnose reductase


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH


substrate_name: ethyl 2-oxo-4-phenylbutyrate

substrate: ethyl 2-oxo-4-phenylbutyrate


substrate_name: ethyl 2-methylacetoacetate

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

substrate: ethyl 2-methylacetoacetate


substrate_name: 7alpha-Hydroxycholesterol; NAD+

assay_conditions_summary: cofactor NAD+

substrate: 7alpha-Hydroxycholesterol; NAD+


substrate_name: glyceraldehyde

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

proof_lines: enzyme form of pI 7.2, at pH 7.0 and 25°C

substrate: glyceraldehyde


substrate_name: Glyoxal

smiles: C(=O)C=O

proof_lines: enzyme form of pI 6.2, at pH 7.0 and 25°C

substrate: Glyoxal


proof_lines:
pI 7.2 form
pI 6.2 form


substrate_name: acetoin

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

proof_lines:
pI 6.2 form
pI 4.8 form
pI 7.2 form

substrate: acetoin


substrate_name: NADH

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH

proof_lines:
pH 6.5, 30°C, recombinant mutant S1M1
pH 6.5, 30°C, recombinant mutant S1M4

substrate: NADH


proof_lines: pH 6.5, 30°C, recombinant wild-type enzyme


proof_lines:
pH 6.5, 30°C, recombinant mutant S1M4
pH 6.5, 30°C, recombinant mutant S1M1


proof_lines:
with 2,3-pentanedione
with glyoxal
with methylglyoxal


proof_lines:
pI 7.2 form
pI 6.2 form
pI 4.8 form


substrate_name: nerol

proof_lines:
pH 9.5, 25°C, recombinant enzyme
at pH 9.5 and 25°C

substrate: nerol


substrate_name: NADP+

assay_conditions_summary: pH 9.5; 298.15 K; cofactor NADP+

substrate: NADP+


substrate_name: menadione

proof_lines: after treatment with S-nitrosoglutathione, pH 7.4, 25°C

proof_lines: enzyme modified by S-nitrosoglutathione, pH 7.4, 37°C

substrate: menadione


organism: Citrus sp.

substrate_name: geraniol

assay_conditions_summary: pH 9

substrate: geraniol


assay_conditions_summary: pH 9; cofactor NADP+


substrate_name: NADPH

proof_lines: pH 7.4, 37°C, recombinant isozyme CBR V244

proof_lines: pH 7.4, 37°C, recombinant isozyme CBR M244

substrate: NADPH


organism: Kluyveromyces marxianus

substrate_name: methyl glyoxal

substrate: methyl glyoxal


assay_conditions_summary: pH 6; 298.15 K; cofactor NADPH


substrate_name: diacetyl

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADPH

substrate: diacetyl


organism: Pichia kudriavzevii

substrate_name: ethyl 2-oxo-4-phenylbutanoate

substrate: ethyl 2-oxo-4-phenylbutanoate


organism: [Candida] boidinii

smiles: CC(C)(C)OC(=O)C(C(=O)CCCC#N)O


organism: Candida parapsilosis

sequence_variant_note: Resolved canonical sequence from genbank_accession:DQ675534 and applied mutation signature S172T to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 5; buffer 100 mM acetate; cofactor NADH

column_label: Valid PDF Table 2 row S172T in the NADPH block, columns Km=0.68 +/- 0.02 mM, kcat=1.36 +/- 0.04 s^-1, kcat/Km=2.00 x 10^3 s^-1 M^-1.

normalized_value_unit_evidence: kcat 1.36 s^-1; Km 0.68 mM; kcat/Km 2.00 s^-1 mM^-1, matching exported kcat/Km 2.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row S172T, NADPH cells: Km 0.68 +/- 0.02 mM; kcat 1.36 +/- 0.04 s^-1; kcat/Km 2.00 x 10^3 s^-1 M^-1; relative kcat/Km 80; Kd nd; h nd.

row_label: S172T, NADPH section

table_label: Table 2. Kinetic parameters for 2-hydroxyacetophenone reduction by wild-type and mutant enzymes.


sequence_variant_note: Resolved canonical sequence from genbank_accession:DQ675534 and applied mutation signature V270D to reconstruct the assayed variant sequence.

column_label: Valid PDF Table 2 row V270D in the NADPH block, columns Km=0.71 +/- 0.03 mM, kcat=1.34 +/- 0.05 s^-1, kcat/Km=1.89 x 10^3 s^-1 M^-1.

raw_value_unit_evidence: Table 2 row V270D, NADPH cells: Km 0.71 +/- 0.03 mM; kcat 1.34 +/- 0.05 s^-1; kcat/Km 1.89 x 10^3 s^-1 M^-1; relative kcat/Km 75; Kd nd; h nd.

row_label: V270D, NADPH section


sequence_variant_note: Resolved canonical sequence from genbank_accession:DQ675534 and applied mutation signature Δ31 to reconstruct the assayed variant sequence.

column_label: Valid PDF Table 2 row D31 in the NADPH block, columns Km=0.63 +/- 0.02 mM, kcat=1.39 +/- 0.03 s^-1, kcat/Km=2.21 x 10^3 s^-1 M^-1.

raw_value_unit_evidence: Table 2 row D31, NADPH cells: Km 0.63 +/- 0.02 mM; kcat 1.39 +/- 0.03 s^-1; kcat/Km 2.21 x 10^3 s^-1 M^-1; relative kcat/Km 88; Kd nd; h nd.

row_label: D31, NADPH section


enzyme_display_name: Dehydrogenase/reductase SDR family member 4

organism: Oryctolagus cuniculus

substrate_name: 16-Ketoestrone (at pH6)

assay_conditions_summary: pH 6

proof_lines: kcat is 2 min(-1) with 5beta-Pregnane-3,20-dione as substrate (at pH7.4).

substrate: 16-Ketoestrone (at pH6)


substrate_name: all-trans-Retinal (at pH7.4)

enzyme: Dehydrogenase/reductase SDR family member 4

substrate: all-trans-Retinal (at pH7.4)


substrate_name: Isatin (at pH6)

substrate: Isatin (at pH6)


substrate_name: Propiophenone (at pH6)

substrate: Propiophenone (at pH6)


substrate_name: Heptanophenone (at pH6)

substrate: Heptanophenone (at pH6)


substrate_name: Nonanophenone (at pH6)

substrate: Nonanophenone (at pH6)


substrate_name: 4-Hexanoylpyridine (at pH6)

substrate: 4-Hexanoylpyridine (at pH6)


substrate_name: Hexanophenone (at pH6)

substrate: Hexanophenone (at pH6)


substrate_name: Valerophenone (at pH6)

substrate: Valerophenone (at pH6)


substrate_name: n-Butyrophenone (at pH6)

substrate: n-Butyrophenone (at pH6)


substrate_name: 3-Benzoylpyridine (at pH6)

substrate: 3-Benzoylpyridine (at pH6)


substrate_name: 4-Benzoylpyridine (at pH6)

substrate: 4-Benzoylpyridine (at pH6)


substrate_name: 2,3-Hexanedione (at pH6)

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

substrate: 2,3-Hexanedione (at pH6)


substrate_name: 1-phenyl-1,2-propanedione (at pH6)

substrate: 1-phenyl-1,2-propanedione (at pH6)


substrate_name: Benzil (at pH6)

substrate: Benzil (at pH6)


substrate_name: Diacetyl (at pH6)

substrate: Diacetyl (at pH6)


substrate_name: Pyridine-4-aldehyde (at pH6)

substrate: Pyridine-4-aldehyde (at pH6)


substrate_name: 1-Phenylisatin (at pH6)

substrate: 1-Phenylisatin (at pH6)


substrate_name: 9,10-Phenanthrenequinone (at pH6)

substrate: 9,10-Phenanthrenequinone (at pH6)


substrate_name: Menadione (at pH6)

substrate: Menadione (at pH6)


substrate_name: S-(-)-1-Phenyl-1-butanol (at pH7.4)

substrate: S-(-)-1-Phenyl-1-butanol (at pH7.4)


substrate_name: all-trans-Retinol (at pH7.4)

substrate: all-trans-Retinol (at pH7.4)


organism: Bacillus cereus

substrate_name: ethyl 4-chloroacetoacetate

substrate: ethyl 4-chloroacetoacetate


organism: Carpoglyphus lactis

substrate_name: geraniol

substrate: geraniol


substrate_name: NAD+

assay_conditions_summary: pH 9; cofactor NAD+

substrate: NAD+


enzyme_display_name: UniProt Q8WNV7

organism: Sus scrofa

proof_lines: kcat is 45 min(-1) with all-trans-Retinal as substrate (at pH7.4) (PubMed:12604222). kcat is 990 min(-1) with isatin as substrate (at pH6) (PubMed:12604222). kcat is 1180 min(-1) with 1-phenyl-1,2-propanedione as substrate (at pH6) (PubMed:

enzyme: UniProt Q8WNV7


substrate_name: 16-Ketoestrone (at pH6)

substrate: 16-Ketoestrone (at pH6)


substrate_name: all-trans-Retinal (at pH7.4)

substrate: all-trans-Retinal (at pH7.4)


substrate_name: isatin (at pH6)

substrate: isatin (at pH6)


substrate_name: Propiophenone (at pH6)

substrate: Propiophenone (at pH6)


substrate_name: Heptanophenone (at pH6)

substrate: Heptanophenone (at pH6)


substrate_name: Nonanophenone (at pH6)

substrate: Nonanophenone (at pH6)


substrate_name: 4-Hexanoylpyridine (at pH6)

substrate: 4-Hexanoylpyridine (at pH6)


substrate_name: Hexanophenone (at pH6)

substrate: Hexanophenone (at pH6)


substrate_name: Valerophenone (at pH6)

substrate: Valerophenone (at pH6)


substrate_name: n-Butyrophenone (at pH6)

substrate: n-Butyrophenone (at pH6)


substrate_name: 3-Benzoylpyridine (at pH6)

substrate: 3-Benzoylpyridine (at pH6)


substrate_name: 4-Benzoylpyridine (at pH6)

substrate: 4-Benzoylpyridine (at pH6)


substrate_name: 2,3-Hexanedione (at pH6)

substrate: 2,3-Hexanedione (at pH6)


substrate_name: 1-phenyl-1,2-propanedione (at pH6)

substrate: 1-phenyl-1,2-propanedione (at pH6)


substrate_name: Benzil (at pH6)

substrate: Benzil (at pH6)


substrate_name: Diacetyl (at pH6)

substrate: Diacetyl (at pH6)


substrate_name: Pyridine-4-aldehyde (at pH6)

substrate: Pyridine-4-aldehyde (at pH6)


substrate_name: 1-Phenylisatin (at pH6)

substrate: 1-Phenylisatin (at pH6)


substrate_name: Menadione (at pH6)

substrate: Menadione (at pH6)


substrate_name: S-(-)-1-Phenyl-1-butanol (at pH7.4)

substrate: S-(-)-1-Phenyl-1-butanol (at pH7.4)


substrate_name: all-trans-Retinol (at pH7.4)

substrate: all-trans-Retinol (at pH7.4)


organism: Homo sapiens

substrate_name: Isatin (at pH6)

proof_lines: kcat is 3.4 min(-1) with 5beta-Pregnane-3,20-dione as substrate (at pH7.4) (PubMed:23128527). kcat is 11.8 min(-1) with 5beta-Androstan-17beta-ol-3-one as substrate (at pH7.4) (PubMed:23128527). kcat is 475 min(-1) with Isatin as substrate

proof_lines: kcat is 3.8 min(-1) with 5beta-Pregnane-3,20-dione as substrate (at pH7.4) (PubMed:18571493). kcat is 5 min(-1) with 5beta-Androstan-17beta-ol-3-one as substrate (at pH7.4) (PubMed:18571493). kcat is 4.6 min(-1) with 5beta-Androstane-3,17-d

substrate: Isatin (at pH6)


substrate_name: 5beta-Androstane-3,17-dione (at pH7.4)

substrate: 5beta-Androstane-3,17-dione (at pH7.4)


substrate_name: 5alpha-Dihydrotestosterone (at pH7.4)

substrate: 5alpha-Dihydrotestosterone (at pH7.4)


substrate_name: Dehydrolithocholic acid (at pH7.4)

substrate: Dehydrolithocholic acid (at pH7.4)


substrate_name: all-trans-Retinal (at pH7.4)

substrate: all-trans-Retinal (at pH7.4)


substrate_name: 4-Hexanoylpyridine (at pH6)

substrate: 4-Hexanoylpyridine (at pH6)


substrate_name: Hexanophenone (at pH6)

substrate: Hexanophenone (at pH6)


substrate_name: Valerophenone (at pH6)

substrate: Valerophenone (at pH6)


substrate_name: n-Butyrophenone (at pH6)

substrate: n-Butyrophenone (at pH6)


substrate_name: 4-Benzoylpyridine (at pH6)

substrate: 4-Benzoylpyridine (at pH6)


substrate_name: 3,4-hexanedione (at pH6)

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

substrate: 3,4-hexanedione (at pH6)


substrate_name: 2,3-heptanedione (at pH6)

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

substrate: 2,3-heptanedione (at pH6)


substrate_name: 4,4'-Dimethylbenzil (at pH6)

substrate: 4,4'-Dimethylbenzil (at pH6)


substrate_name: 2,3-Pentanedione (at pH6)

substrate: 2,3-Pentanedione (at pH6)


substrate_name: Diacetyl (at pH6)

substrate: Diacetyl (at pH6)


substrate_name: 4-Nitrobenzaldehyde (at pH6)

substrate: 4-Nitrobenzaldehyde (at pH6)


substrate_name: Pyridine-4-aldehyde (at pH6)

substrate: Pyridine-4-aldehyde (at pH6)


substrate_name: 1,4-Naphthoquinone (at pH6)

substrate: 1,4-Naphthoquinone (at pH6)


substrate_name: 5b-Pregnan-3b-ol-20-one (at pH7.4)

substrate: 5b-Pregnan-3b-ol-20-one (at pH7.4)


substrate_name: 5b-Androstane-3b,17b-diol (at pH7.4)

substrate: 5b-Androstane-3b,17b-diol (at pH7.4)


substrate_name: 5b-Androstan-3b-ol-17-one (at pH7.4)

substrate: 5b-Androstan-3b-ol-17-one (at pH7.4)


substrate_name: menadione

proof_lines: kcats are 2 min(-1), 285 min(-1), 460 min(-1), 58 min(-1) for prostaglandin E2, menadione, 9,1 O-phenanthrene-quinone and 4-nitrobenzaldehyde as substrates, respectively.

substrate: menadione


enzyme_display_name: Carbonyl reductase [NADPH] 1

substrate_name: prostaglandin E2

enzyme: Carbonyl reductase [NADPH] 1

substrate: prostaglandin E2


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


enzyme_display_name: Aldo/keto reductase slr0942

organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)

substrate_name: hexanal

smiles: CCCCCC=O

assay_conditions_summary: pH 7.4; buffer pH 7; cofactor NADPH

column_label: Table 1. Kinetic parameters for the reduction of different classes of carbonyl containing compounds; row Hexanal; column Km (mM).

raw_value_unit_evidence: Table 1. Kinetic parameters for the reduction of different classes of carbonyl containing compounds; category Aldehydes; row Hexanal; column Km (mM): Km=0.094 +/- 0.035 mM.

row_label: Hexanal

enzyme: Aldo/keto reductase slr0942

substrate: hexanal


column_label: Table 1. Kinetic parameters for the reduction of different classes of carbonyl containing compounds; row 4-Pyridinecarboxaldehyde; column Km (mM).

raw_value_unit_evidence: Table 1. Kinetic parameters for the reduction of different classes of carbonyl containing compounds; category Aldehydes; row 4-Pyridinecarboxaldehyde; column Km (mM): Km=0.077 +/- 0.009 mM.


column_label: Table 1. Kinetic parameters for the reduction of different classes of carbonyl containing compounds; row 4-Nitrobenzaldehyde; column Km (mM).

raw_value_unit_evidence: Table 1. Kinetic parameters for the reduction of different classes of carbonyl containing compounds; category Aldehydes; row 4-Nitrobenzaldehyde; column Km (mM): Km=0.046 +/- 0.01 mM.


column_label: Table 1. Kinetic parameters for the reduction of different classes of carbonyl containing compounds; row 9,10-Phenanthrenequinone; column Km (mM).

raw_value_unit_evidence: Table 1. Kinetic parameters for the reduction of different classes of carbonyl containing compounds; category Quinones; row 9,10-Phenanthrenequinone; column Km (mM): Km=0.005 +/- 0.001 mM.


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

column_label: Table 1. Kinetic parameters for the reduction of different classes of carbonyl containing compounds; row 4-ONE (4-oxo-2-nonenal); column Km (mM).

raw_value_unit_evidence: Table 1. Kinetic parameters for the reduction of different classes of carbonyl containing compounds; category Unsaturated carbonyls; row 4-ONE (4-oxo-2-nonenal); column Km (mM): Km=0.0047 +/- 0.001 mM.

row_label: 4-ONE (4-oxo-2-nonenal)


smiles: CCCCCC(C=CC=O)O

column_label: Table 1. Kinetic parameters for the reduction of different classes of carbonyl containing compounds; row 4-Hydroxynonenal (4-hydroxy-2-nonenal); column Km (mM).

raw_value_unit_evidence: Table 1. Kinetic parameters for the reduction of different classes of carbonyl containing compounds; category Unsaturated carbonyls; row 4-Hydroxynonenal (4-hydroxy-2-nonenal); column Km (mM): Km=0.0595 +/- 0.011 mM.

row_label: 4-Hydroxynonenal (4-hydroxy-2-nonenal)


substrate_name: furfural

column_label: Table 1. Kinetic parameters for the reduction of different classes of carbonyl containing compounds; row Furfural; column Km (mM).

raw_value_unit_evidence: Table 1. Kinetic parameters for the reduction of different classes of carbonyl containing compounds; category AGEs; row Furfural; column Km (mM): Km=0.89 +/- 0.1 mM.

row_label: Furfural

substrate: furfural


column_label: Table 1. Kinetic parameters for the reduction of different classes of carbonyl containing compounds; row NADPH; column Km (mM).

raw_value_unit_evidence: Table 1. Kinetic parameters for the reduction of different classes of carbonyl containing compounds; category Aromatic heterocyclic organic compounds; row NADPH; column Km (mM): Km=0.0085 +/- 0.00072 mM.

row_label: NADPH


enzyme_display_name: Carbonyl reductase [NADPH] 3

proof_lines: kcat is 0.55 min(-1) with menadione as substrate (PubMed:18493841). kcat is 0.70 min(-1) with 4-benzoylpyridine as substrate (PubMed:18493841). kcat is 0.59 min(-1) with 4-nitorobenzaldehyde as substrate (PubMed:18493841).

enzyme: Carbonyl reductase [NADPH] 3


substrate_name: isatin

substrate: isatin


substrate_name: oracin

substrate: oracin


substrate_name: methylglyoxal

proof_lines: kcat is 351 min(-1) with methylglyoxal as substrate. kcat is 1049 min(-1) with glyoxal as substrate. kcat is 226 min(-1) with 3-deoxyglucosone as substrate. kcat is 1078 min(-1) with acrolein as substrate. kcat is 1.75 sec(-1) with hexanal

substrate: methylglyoxal


substrate_name: glyoxal

substrate: glyoxal


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


substrate_name: acrolein

smiles: C=CC=O

substrate: acrolein


substrate_name: 5beta-Pregnane-3,20-dione(at pH7.4)

assay_conditions_summary: pH 7.4; cofactor NADPH

column_label: Table 2 NRDRB1 columns report 5beta-Pregnane-3,20-dione* Km = 5.1 microM, not the sheet value 2.9 microM.

raw_value_unit_evidence: Km raw_value=5.1 raw_unit=microM

row_label: NRDRB1 / 5beta-Pregnane-3,20-dione*

table_label: Table 2. Kinetic constants of NRDRB1 and NRDR towards dicarbonyl compounds and steroids

substrate: 5beta-Pregnane-3,20-dione(at pH7.4)


substrate_name: Benzil (at pH6)

assay_conditions_summary: pH 6; cofactor NADPH

column_label: Table 2 NRDRB1 columns report Benzil Km = 1.8 microM.

raw_value_unit_evidence: Km raw_value=1.8 raw_unit=microM

row_label: NRDRB1 / Benzil

substrate: Benzil (at pH6)


substrate_name: 1-Phenylisatin (at pH6)

column_label: Table 2 NRDRB1 columns report 1-Phenyisatin Km = 18.8 microM, not the sheet value 5.2 microM.

raw_value_unit_evidence: Km raw_value=18.8 raw_unit=microM

row_label: NRDRB1 / 1-Phenyisatin

substrate: 1-Phenylisatin (at pH6)


substrate_name: 9,10-Phenanthrenequinone (at pH7.4)

column_label: Table 2 NRDRB1 columns report 9,10-Phenanthrenequinone* Km = 2.2 microM.

raw_value_unit_evidence: Km raw_value=2.2 raw_unit=microM

row_label: NRDRB1 / 9,10-Phenanthrenequinone*

substrate: 9,10-Phenanthrenequinone (at pH7.4)


substrate_name: Menadione (at pH6)

column_label: Table 2 NRDRB1 columns report Menadione Km = 7.5 microM.

raw_value_unit_evidence: Km raw_value=7.5 raw_unit=microM

row_label: NRDRB1 / Menadione

substrate: Menadione (at pH6)


assay_conditions_summary: pH 7; cofactor NADPH


substrate_name: doxorubicin

assay_conditions_summary: pH 7

substrate: doxorubicin


substrate_name: 5alpha-Pregnane-3,20-dione (at pH7.4)

substrate: 5alpha-Pregnane-3,20-dione (at pH7.4)


substrate_name: Dehydrolithocholic acid (at pH7.4)

substrate: Dehydrolithocholic acid (at pH7.4)


substrate_name: 2,3-Pentanedione (at pH6)

substrate: 2,3-Pentanedione (at pH6)


substrate_name: Methyl benzoylformate (at pH6)

substrate: Methyl benzoylformate (at pH6)


substrate_name: 4-Nitrobenzaldehyde (at pH6)

substrate: 4-Nitrobenzaldehyde (at pH6)


substrate_name: menadione

substrate: menadione


substrate_name: NADPH

substrate: NADPH


substrate_name: 5beta-Pregnane-3,20-dione (at pH7.4)

substrate: 5beta-Pregnane-3,20-dione (at pH7.4)


substrate_name: 4-Acetylpyridine (at pH6)

substrate: 4-Acetylpyridine (at pH6)


substrate_name: Pyridine-3-aldehyde (at pH6)

substrate: Pyridine-3-aldehyde (at pH6)


substrate_name: 4-Nitroacetophenone (at pH6)

substrate: 4-Nitroacetophenone (at pH6)


organism: Rattus norvegicus

proof_lines: kcat is 14 min(-1) with 4-benzoylpyridine as substrate (PubMed:18983987). kcat is 0.030 min(-1) with menadione as substrate (PubMed:18983987).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T38D to reconstruct the assayed variant sequence.


substrate_name: NAD+

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NADH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

substrate: NADH


substrate_name: NADP+

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

substrate: NADP+


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C122A to reconstruct the assayed variant sequence.

column_label: Table 1. Apparent kinetic constants (Km, kcat) of wild-type and mutant recombinant human carbonyl reductases.; row C122A / 4-Benzoylpyridine; 4-Benzoylpyridine row C122A: Km raw_value=330 raw_unit=uM; kcat raw_value=4.7 raw_unit=s^-1; NADPH Km raw_value=3 raw_unit=uM

normalized_value_unit_evidence: kcat normalized_value=4.7 normalized_unit=s^-1; Km normalized_value=0.33 normalized_unit=mM from 330 uM / 1000; kcat/Km normalized_value=14.2424242424242 normalized_unit=s^-1*mM^-1 from same-row kcat and Km

row_label: C122A / 4-Benzoylpyridine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C150A to reconstruct the assayed variant sequence.

column_label: Table 1. Apparent kinetic constants (Km, kcat) of wild-type and mutant recombinant human carbonyl reductases.; row C150A / 4-Benzoylpyridine; 4-Benzoylpyridine row C150A: Km raw_value=270 raw_unit=uM; kcat raw_value=5.4 raw_unit=s^-1; NADPH Km raw_value=3 raw_unit=uM

normalized_value_unit_evidence: kcat normalized_value=5.4 normalized_unit=s^-1; Km normalized_value=0.27 normalized_unit=mM from 270 uM / 1000; kcat/Km normalized_value=20 normalized_unit=s^-1*mM^-1 from same-row kcat and Km

row_label: C150A / 4-Benzoylpyridine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C26A to reconstruct the assayed variant sequence.


substrate_name: Daunorubicin

column_label: Table 1. Apparent kinetic constants (Km, kcat) of wild-type and mutant recombinant human carbonyl reductases.; row C122A / Daunorubicin; Daunorubicin row C122A: Km raw_value=160 raw_unit=uM; kcat raw_value=1.7 raw_unit=s^-1; NADPH Km raw_value=3 raw_unit=uM

normalized_value_unit_evidence: kcat normalized_value=1.7 normalized_unit=s^-1; Km normalized_value=0.16 normalized_unit=mM from 160 uM / 1000; kcat/Km normalized_value=10.625 normalized_unit=s^-1*mM^-1 from same-row kcat and Km

row_label: C122A / Daunorubicin

substrate: Daunorubicin


column_label: Table 1. Apparent kinetic constants (Km, kcat) of wild-type and mutant recombinant human carbonyl reductases.; row C150A / Daunorubicin; Daunorubicin row C150A: Km raw_value=180 raw_unit=uM; kcat raw_value=1.4 raw_unit=s^-1; NADPH Km raw_value=3 raw_unit=uM

normalized_value_unit_evidence: kcat normalized_value=1.4 normalized_unit=s^-1; Km normalized_value=0.18 normalized_unit=mM from 180 uM / 1000; kcat/Km normalized_value=7.77777777777778 normalized_unit=s^-1*mM^-1 from same-row kcat and Km

row_label: C150A / Daunorubicin


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C226A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C227A to reconstruct the assayed variant sequence.

column_label: Table 1. Apparent kinetic constants (Km, kcat) of wild-type and mutant recombinant human carbonyl reductases.; row C227A / Daunorubicin; Daunorubicin row C227A: Km raw_value=440 raw_unit=uM; kcat raw_value=0.12 raw_unit=s^-1; NADPH Km raw_value=13 raw_unit=uM

normalized_value_unit_evidence: kcat normalized_value=0.12 normalized_unit=s^-1; Km normalized_value=0.44 normalized_unit=mM from 440 uM / 1000; kcat/Km normalized_value=0.272727272727273 normalized_unit=s^-1*mM^-1 from same-row kcat and Km

row_label: C227A / Daunorubicin


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C227S to reconstruct the assayed variant sequence.

column_label: Table 1. Apparent kinetic constants (Km, kcat) of wild-type and mutant recombinant human carbonyl reductases.; row C227S / Daunorubicin; Daunorubicin row C227S: Km raw_value=470 raw_unit=uM; kcat raw_value=0.55 raw_unit=s^-1; NADPH Km raw_value=12 raw_unit=uM

normalized_value_unit_evidence: kcat normalized_value=0.55 normalized_unit=s^-1; Km normalized_value=0.47 normalized_unit=mM from 470 uM / 1000; kcat/Km normalized_value=1.17021276595745 normalized_unit=s^-1*mM^-1 from same-row kcat and Km

row_label: C227S / Daunorubicin


column_label: Table 1. Apparent kinetic constants (Km, kcat) of wild-type and mutant recombinant human carbonyl reductases.; row C26A / Daunorubicin; Daunorubicin row C26A: Km raw_value=140 raw_unit=uM; kcat raw_value=1.2 raw_unit=s^-1; NADPH Km raw_value=3 raw_unit=uM

normalized_value_unit_evidence: kcat normalized_value=1.2 normalized_unit=s^-1; Km normalized_value=0.14 normalized_unit=mM from 140 uM / 1000; kcat/Km normalized_value=8.57142857142857 normalized_unit=s^-1*mM^-1 from same-row kcat and Km

row_label: C26A / Daunorubicin


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


organism: Ocimum basilicum

substrate_name: geraniol

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

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

column_label: ScienceDirect Table 3 reports GEDH1 geraniol Km = 30 +/- 5 uM.

raw_value_unit_evidence: KM raw_value=30 +/- 5 raw_unit=uM

row_label: GEDH1 / Geraniol

table_label: ScienceDirect PMID 16150417 Table 3

substrate: geraniol


enzyme_display_name: geraniol dehydrogenase (NADP(+))

substrate_name: Geraniol

smiles: CC(C)=CCC/C(C)=C/CO

column_label: ScienceDirect Table 3, GEDH1 block, Geraniol row: Km column 30 +/- 5 uM; kcat column 1.0 +/- 0.1 s^-1; kcat/Km column 0.033.

normalized_value_unit_evidence: Paper central Km 30 uM converts to 0.030 mM; paper central kcat is 1.0 s^-1; printed kcat/Km 0.033 s^-1 uM^-1 converts to 33 s^-1 mM^-1. Export kcat/Km is 33.333333333333336 s^-1 mM^-1 and does not exactly equal the printed value.

raw_value_unit_evidence: Table 3 GEDH1 Geraniol row reports Km = 30 +/- 5 uM, kcat = 1.0 +/- 0.1 s^-1, and kcat/Km = 0.033 s^-1 uM^-1.

table_label: ScienceDirect PMID 16150417 Table 3: Kinetic parameters of CAD1 and GEDH1

enzyme: geraniol dehydrogenase (NADP(+))

substrate: Geraniol


substrate_name: Nerol

smiles: CC(C)=CCC/C(C)=C\CO

column_label: ScienceDirect Table 3, GEDH1 block, Nerol row: Km column 37 +/- 8 uM; kcat column 1.5 +/- 0.2 s^-1; kcat/Km column 0.040.

normalized_value_unit_evidence: Paper central Km 37 uM converts to 0.037 mM; paper central kcat is 1.5 s^-1; printed kcat/Km 0.040 s^-1 uM^-1 converts to 40 s^-1 mM^-1. Export kcat/Km is 40.54054054054054 s^-1 mM^-1 and does not exactly equal the printed value.

raw_value_unit_evidence: Table 3 GEDH1 Nerol row reports Km = 37 +/- 8 uM, kcat = 1.5 +/- 0.2 s^-1, and kcat/Km = 0.040 s^-1 uM^-1.

row_label: GEDH1 / Nerol

substrate: Nerol


substrate_name: cinnamyl alcohol

column_label: ScienceDirect Table 3, GEDH1 block, Cinnamyl alcohol row: Km column 655 +/- 45 uM; kcat column 1.8 +/- 0.1 s^-1; kcat/Km column 0.0027.

normalized_value_unit_evidence: Paper central Km 655 uM converts to 0.655 mM; paper central kcat is 1.8 s^-1; printed kcat/Km 0.0027 s^-1 uM^-1 converts to 2.7 s^-1 mM^-1. Export kcat/Km is 2.7480916030534353 s^-1 mM^-1 and does not exactly equal the printed value.

raw_value_unit_evidence: Table 3 GEDH1 Cinnamyl alcohol row reports Km = 655 +/- 45 uM, kcat = 1.8 +/- 0.1 s^-1, and kcat/Km = 0.0027 s^-1 uM^-1.

row_label: GEDH1 / Cinnamyl alcohol

substrate: cinnamyl alcohol


enzyme_display_name: Geraniol dehydrogenase 1

column_label: ScienceDirect Table 3 reports GEDH1 cinnamyl alcohol Km = 655 +/- 45 uM.

raw_value_unit_evidence: KM raw_value=655 +/- 45 raw_unit=uM

enzyme: Geraniol dehydrogenase 1


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


assay_conditions_summary: pH 8.4; 298.15 K; cofactor NADPH


substrate_name: daunorubicin

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

substrate: daunorubicin


enzyme_display_name: carbonyl reductase (NADPH)

substrate_name: Prostaglandin E2

enzyme: carbonyl reductase (NADPH)

substrate: Prostaglandin E2


substrate_name: prostaglandin E2

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

column_label: Official PMC Table 3, PGE2 row, CBR1 V88 Km (microM) column = 309 +/- 94; the adjacent I88 Km is 320 +/- 63 microM and is not substituted.

normalized_value_unit_evidence: 309 +/- 94 microM = 0.309 mM; the exported Km is 0.309 mM.

raw_value_unit_evidence: Table 3 PGE2 row, CBR1 V88 Km column: 309 +/- 94 microM.

row_label: PGE2 row / CBR1 V88

table_label: Table 3 / CBR1 V88 and CBR1 I88 kinetic constants for prototypical substrates

substrate: prostaglandin E2


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C226A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C227A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C227S with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


substrate_name: menadiol

substrate: menadiol


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -1, so it is treated as a source-provided variant sequence.


column_label: Table 1; row Wild-type; column 'Menadione Km' cell 22 (the Km column header renders as '(mm)' in the PDF text layer because the micro sign is dropped by the extractor; the printed paper unit is microM); column 'Menadione kcat (s^-1)' cell 6.7; column 'NADPH Km' cell 3. Table 1 prints no kcat/Km column, so absolute kcat/Km is derived by dividing this row's Menadione kcat cell by its Menadione Km cell.

raw_value_unit_evidence: Table 1 (Eur. J. Biochem. 260, page 11), row Wild-type, Menadione block: Km cell 22, kcat cell 6.7; NADPH Km cell 3. The same micro-sign artifact appears in the footnote '[NADPH] = 50 mm', which the paper prints as 50 microM. No kcat/Km column is printed anywhere in Table 1.

row_label: Wild-type

table_label: Table 1. Apparent kinetic constants (Km, kcat) of wild-type and mutant recombinant human carbonyl reductases


substrate_name: Adriamycin

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P131S with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

substrate: Adriamycin


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V88I to reconstruct the assayed variant sequence.


substrate_name: isatin

substrate: isatin


substrate_name: menadione

substrate: menadione


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

column_label: Table 3 row WT-CBR1 / 2,3-hexanedione; columns Km (uM), kcat (min^-1), and kcat/Km ((uM min)^-1); explicit central cells 159 +/- 20, 308 +/- 24, and 1.9.

normalized_value_unit_evidence: kcat 5.133333333333333333333333333 s^-1 from explicit paper cell; kcat_over_km 31.66666666666666666666666667 s^-1 mM^-1 from explicit paper cell; km 0.159 mM from explicit paper cell

raw_value_unit_evidence: Table 3 row WT-CBR1 / 2,3-hexanedione: Km 159 +/- 20 uM; kcat 308 +/- 24 min^-1; kcat/Km 1.9 (uM min)^-1.

row_label: WT-CBR1 / 2,3-hexanedione

table_label: Table 3, kinetics constants for WT-CBR1 and CBR1 modified


assay_conditions_summary: pH 7.4; 310.15 K; buffer a 10 mM sodium phosphate; cofactor NADP+

column_label: Table 3 (Kinetics constants for WT-CBR1 and CBR1 "modified"), enzyme-form row WT-CBR1 with substrate NNK; column 'Km (uM)' = 7840 ± 690; column 'kcat (min^-1)' = 121 ± 2; column 'kcat/Km (uM^-1 min^-1)' = 0.015.

raw_value_unit_evidence: Table 3, enzyme-form row WT-CBR1 with substrate NNK: Km = 7840 ± 690 uM; kcat = 121 ± 2 min^-1; printed kcat/Km = 0.015 uM^-1 min^-1.

row_label: Table 3, WT-CBR1 row, substrate NNK

table_label: Table 3: Kinetics constants for WT-CBR1 and CBR1 "modified" (Chemico-Biological Interactions 202 (2013) 136-145)


column_label: Table 3 columns Enzyme form/substrate, Km (uM), kcat (min^-1), and kcat/Km ((uM min)^-1); footnote defines CBR1 modified as CBR1 treated with 2 mM GSNO and notes kcat/Km errors were less than 20%.

raw_value_unit_evidence: Table 3 row CBR1 modified / 1,2-naphthoquinone: Km 117 +/- 12 uM; kcat 402 +/- 6 min^-1; kcat/Km 3.4 (uM min)^-1.

row_label: CBR1 modified / 1,2-naphthoquinone


substrate_name: oracin

column_label: Table 3 (Kinetics constants for WT-CBR1 and CBR1 "modified"), enzyme-form row WT-CBR1 with substrate oracin; column 'Km (uM)' = 96 ± 9; column 'kcat (min^-1)' = 70 ± 1; column 'kcat/Km (uM^-1 min^-1)' = 0.73.

raw_value_unit_evidence: Table 3, enzyme-form row WT-CBR1 with substrate oracin: Km = 96 ± 9 uM; kcat = 70 ± 1 min^-1; printed kcat/Km = 0.73 uM^-1 min^-1.

row_label: Table 3, WT-CBR1 row, substrate oracin

substrate: oracin


substrate_name: prostaglandin E1

substrate: prostaglandin E1


substrate_name: phenylglyoxal

substrate: phenylglyoxal


proof_lines: kcat is 0.55 min(-1) with menadione as substrate (PubMed:18493841).


substrate_name: NADPH

substrate: NADPH


substrate_name: S-nitrosoglutathione

proof_lines:
hCBR1 GSNO reducing enzyme
Raw SKiD Env: Temp=-----, pH=7.4

substrate: S-nitrosoglutathione


substrate_name: S-Nitrosoglutathione

substrate: S-Nitrosoglutathione


assay_conditions_summary: pH 6.8; 298.15 K; cofactor NADPH


organism: Caenorhabditis elegans

substrate_name: Isatin

substrate: Isatin


substrate_name: isatin (at 25 degrees Celsius)

column_label: PDF p.80 states DHRS2 (Q93790) with isatin has Km-value 0.12 mM.

raw_value_unit_evidence: Results text states isatin is a good substrate for DHRS2 (Q93790) with Km value 0.12 mM and kcat/Km 7500 mM^-1 min^-1.

row_label: C. elegans DHRS2 (Q93790) / isatin substrate

table_label: CBI PDF p.80 Results / Fig. 5 kinetic text

substrate: isatin (at 25 degrees Celsius)


organism: Mesocricetus auratus


substrate_name: NAD+

substrate: NAD+


proof_lines: hCBR3 showed limited catalytic activity toward 4-benzoylpyridine.

proof_lines: The paper distinguishes hCBR3 from hCBR1 in human carbonyl reductase function.


substrate_name: p-Nitrobenzaldehyde

substrate: p-Nitrobenzaldehyde


enzyme_display_name: UniProt P15121

substrate_name: prostaglandin H2

proof_lines:
Raw SKiD Env: Temp=37°C, pH=5.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P15121

substrate: prostaglandin H2


enzyme_display_name: UniProt C5XC49

organism: Sorghum bicolor

substrate_name: coniferyl aldehyde

enzyme: UniProt C5XC49

substrate: coniferyl aldehyde


substrate_name: sinapyl aldehyde

substrate: sinapyl aldehyde


substrate_name: coniferyl alcohol

substrate: coniferyl alcohol


enzyme_display_name: cinnamyl-alcohol dehydrogenase

organism: Helicobacter pylori

substrate_name: benzaldehyde

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

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

proof_lines: pH 7.5, 37°C, recombinant enzyme, dismutase reaction with NADP+

enzyme: cinnamyl-alcohol dehydrogenase

substrate: benzaldehyde


substrate_name: butanol

smiles: CCCCO

substrate: butanol


substrate_name: ethanol

smiles: CCO

substrate: ethanol


substrate_name: cinnamyl aldehyde

substrate: cinnamyl aldehyde


substrate_name: benzyl alcohol

substrate: benzyl alcohol


substrate_name: Propanol

smiles: CCCO

substrate: Propanol


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: NADP+

proof_lines: pH 7.5, 37°C, recombinant enzyme, with benzyla alcohol

substrate: NADP+


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: NADPH

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

proof_lines: pH 7.5, 37°C, recombinant enzyme, with acetaldehyde

substrate: NADPH


enzyme_display_name: long-chain-alcohol dehydrogenase

organism: Pseudomonas putida

substrate_name: n-butanol

enzyme: long-chain-alcohol dehydrogenase

substrate: n-butanol


substrate_name: n-Propanol

substrate: n-Propanol


substrate_name: n-decanal

smiles: CCCCCCCCCC=O

substrate: n-decanal


substrate_name: n-Hexanol

smiles: CCCCCCO

substrate: n-Hexanol


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


substrate_name: n-Pentanol

smiles: CCCCCO

substrate: n-Pentanol


substrate_name: n-decanol

smiles: CCCCCCCCCCO

substrate: n-decanol


substrate_name: n-Heptanol

smiles: CCCCCCCO

substrate: n-Heptanol


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


substrate_name: n-Octanol

smiles: CCCCCCCCO

substrate: n-Octanol


substrate_name: n-nonanol

smiles: CCCCCCCCCO

substrate: n-nonanol


organism: Glycine max

substrate_name: coniferaldehyde

substrate: coniferaldehyde


substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


assay_conditions_summary: cofactor NADP+


substrate_name: sinapaldehyde

substrate: sinapaldehyde


assay_conditions_summary: cofactor NADPH


substrate_name: p-coumaraldehyde

substrate: p-coumaraldehyde


substrate_name: coniferyl alcohol

substrate: coniferyl alcohol


substrate_name: 3,4-dimethoxycinnamyl alcohol

substrate: 3,4-dimethoxycinnamyl alcohol


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: sinapyl alcohol

substrate: sinapyl alcohol


substrate_name: p-coumaryl alcohol

substrate: p-coumaryl alcohol


organism: Petroselinum crispum


substrate_name: benzaldehyde

substrate: benzaldehyde


organism: Amycolatopsis methanolica


substrate_name: 12-Hydroxydodecanoic acid

smiles: C(CCCCCC(=O)O)CCCCCO

substrate: 12-Hydroxydodecanoic acid


substrate_name: ethanol

substrate: ethanol


organism: Micrococcus luteus

substrate_name: 12-hydroxyoctadecanoic acid

smiles: CCCCCCC(CCCCCCCCCCC(=O)O)O

proof_lines: wild type enzyme, with NAD+ as cosubstrate, pH and temperature not specified in the publication

substrate: 12-hydroxyoctadecanoic acid


substrate_name: 10-hydroxyoctadecanoic acid

smiles: CCCCCCCCC(CCCCCCCCC(=O)O)O

substrate: 10-hydroxyoctadecanoic acid


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

proof_lines: mutant enzyme D37S/V39S, with NAD+ as cosubstrate, pH and temperature not specified in the publication


substrate_name: 10,12-dihydroxyoctadecanoic acid

proof_lines: mutant enzyme D37S/A38R/V39S/T15I, with NAD+ as cosubstrate, pH and temperature not specified in the publication

substrate: 10,12-dihydroxyoctadecanoic acid


organism: Phaseolus vulgaris

substrate_name: coniferyl aldehyde

proof_lines:
CAD2 isoform
CAD1 isoform

substrate: coniferyl aldehyde


substrate_name: sinapyl aldehyde

substrate: sinapyl aldehyde


substrate_name: benzyl alcohol

proof_lines: isoform CAD1, pH and temperature not specified in the publication

substrate: benzyl alcohol


organism: Geobacillus thermodenitrificans

substrate_name: NAD+

assay_conditions_summary: pH 8; 333.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NADP+

assay_conditions_summary: pH 8; 333.15 K; cofactor NADP+

substrate: NADP+


substrate_name: NADPH

assay_conditions_summary: pH 8; 333.15 K; cofactor NADPH

substrate: NADPH


enzyme_display_name: coniferyl-alcohol dehydrogenase

organism: Streptomyces sp.

substrate_name: coniferyl alcohol

enzyme: coniferyl-alcohol dehydrogenase

substrate: coniferyl alcohol


organism: Oryza sativa Japonica Group

substrate_name: 4-coumaryl aldehyde

substrate: 4-coumaryl aldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G301F to reconstruct the assayed variant sequence.

column_label: Table II p-Coumaraldehyde rows, G301F column: kcat (s^-1)=9.50; Km (uM)=267.98.

normalized_value_unit_evidence: kcat 9.50 s^-1; Km 0.26798 mM after converting uM to mM.

raw_value_unit_evidence: p-Coumaraldehyde kcat 9.50 s^-1; Km 267.98 uM.

row_label: G301F column, p-Coumaraldehyde rows

table_label: PMID 28606901 PMC5543964 Table II, kinetic parameters for SbCAD variants


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L119W/G301F to reconstruct the assayed variant sequence.

column_label: Table II p-Coumaraldehyde rows, L119W/G301F column: kcat (s^-1)=30.16; Km (uM)=80.88.

normalized_value_unit_evidence: kcat 30.16 s^-1; Km 0.08088 mM after converting uM to mM.

raw_value_unit_evidence: p-Coumaraldehyde kcat 30.16 s^-1; Km 80.88 uM.

row_label: L119W/G301F column, p-Coumaraldehyde rows


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W58L to reconstruct the assayed variant sequence.

column_label: Table II p-Coumaraldehyde rows, W58L column: kcat (s^-1)=3.27; Km (uM)=7,101.66.

normalized_value_unit_evidence: kcat 3.27 s^-1; Km 7.10166 mM after converting uM to mM.

raw_value_unit_evidence: p-Coumaraldehyde kcat 3.27 s^-1; Km 7,101.66 uM.

row_label: W58L column, p-Coumaraldehyde rows


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y288P to reconstruct the assayed variant sequence.

column_label: Table II p-Coumaraldehyde rows, Y288P column: kcat (s^-1)=1.19; Km (uM)=4,178.84.

normalized_value_unit_evidence: kcat 1.19 s^-1; Km 4.17884 mM after converting uM to mM.

raw_value_unit_evidence: p-Coumaraldehyde kcat 1.19 s^-1; Km 4,178.84 uM.

row_label: Y288P column, p-Coumaraldehyde rows


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y95V to reconstruct the assayed variant sequence.

column_label: Table II p-Coumaraldehyde rows, Y95V column: kcat (s^-1)=3.59; Km (uM)=6,882.54.

normalized_value_unit_evidence: kcat 3.59 s^-1; Km 6.88254 mM after converting uM to mM.

raw_value_unit_evidence: p-Coumaraldehyde kcat 3.59 s^-1; Km 6,882.54 uM.

row_label: Y95V column, p-Coumaraldehyde rows


organism: Plagiochasma appendiculatum


substrate_name: caffeylaldehyde

substrate: caffeylaldehyde


organism: Hibiscus cannabinus

substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


substrate_name: cinnamyl aldehyde

substrate: cinnamyl aldehyde


substrate_name: coniferaldehyde

substrate: coniferaldehyde


organism: Carthamus tinctorius


organism: Populus tomentosa


substrate_name: sinapaldehyde

substrate: sinapaldehyde


column_label: Table II Sinapaldehyde rows, G301F column: kcat (s^-1)=5.29; Km (uM)=16.83.

normalized_value_unit_evidence: kcat 5.29 s^-1; Km 0.01683 mM after converting uM to mM.

raw_value_unit_evidence: Sinapaldehyde kcat 5.29 s^-1; Km 16.83 uM.

row_label: G301F column, Sinapaldehyde rows


column_label: Table II Sinapaldehyde rows, L119W/G301F column: kcat (s^-1)=18.98; Km (uM)=105.19.

normalized_value_unit_evidence: kcat 18.98 s^-1; Km 0.10519 mM after converting uM to mM.

raw_value_unit_evidence: Sinapaldehyde kcat 18.98 s^-1; Km 105.19 uM.

row_label: L119W/G301F column, Sinapaldehyde rows


organism: Forsythia suspensa


substrate_name: 4-methoxycinnamyl alcohol

substrate: 4-methoxycinnamyl alcohol


substrate_name: 3,4-dimethoxy-cinnamyl alcohol

substrate: 3,4-dimethoxy-cinnamyl alcohol


substrate_name: p-coumaryl alcohol

substrate: p-coumaryl alcohol


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


organism: Pinus thunbergii


substrate_name: p-coumaraldehyde

substrate: p-coumaraldehyde


enzyme_display_name: indole-3-acetaldehyde reductase (NADPH)

organism: Brassica rapa subsp. pekinensis

enzyme: indole-3-acetaldehyde reductase (NADPH)


substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


substrate_name: acetaldehyde

substrate: acetaldehyde


assay_conditions_summary: pH 8


substrate_name: NAD+

assay_conditions_summary: pH 8; cofactor NAD+

substrate: NAD+


substrate_name: allyl alcohol

smiles: C=CCO

substrate: allyl alcohol


organism: Phycomyces blakesleeanus

substrate_name: NADPH

substrate: NADPH


substrate_name: dihydroxyacetone phosphate

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

substrate: dihydroxyacetone phosphate


organism: Geobacillus stearothermophilus

assay_conditions_summary: pH 8.8; 323.15 K; cofactor NAD+


substrate_name: NADH

assay_conditions_summary: pH 7.5; 323.15 K; cofactor NADH

substrate: NADH


enzyme_display_name: prostaglandin-F synthase

organism: Mus musculus

substrate_name: 9alpha,11beta-prostaglandin F2

enzyme: prostaglandin-F synthase

substrate: 9alpha,11beta-prostaglandin F2


assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH


substrate_name: Prostaglandin D2

substrate: Prostaglandin D2


organism: Populus x canadensis

assay_conditions_summary: cofactor CoA


organism: Rattus norvegicus


substrate_name: Unknown

substrate: Unknown


organism: Nostoc sp.

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


substrate_name: (2S)-5-hydroxy-2-aminovaleric acid

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

substrate: (2S)-5-hydroxy-2-aminovaleric acid


organism: Saccharum officinarum

substrate_name: sinapyl alcohol

substrate: sinapyl alcohol


substrate_name: coniferyl alcohol

substrate: coniferyl alcohol


organism: Glycine max

substrate_name: NADP+

substrate: NADP+


substrate_name: sinapyl aldehyde

proof_lines: pH 6.0, 30°C, recombinant His-tagged enzyme

proof_lines: pH 5.0, 30°C, recombinant His-tagged enzyme

substrate: sinapyl aldehyde


substrate_name: coniferyl aldehyde

substrate: coniferyl aldehyde


organism: Trypanosoma brucei

column_label: Table 2; 9,10-Phenanthrenequinone row; K_m (uM) column; raw K_m value 0.42 uM.

raw_value_unit_evidence: Table 2 reports 9,10-Phenanthrenequinone K_m = 0.42 uM.

row_label: 9,10-Phenanthrenequinone row; K_m column

table_label: PMID 11067881, Table 2: Substrate Specificity and Kinetic Parameters of TbPGFS


column_label: Table 2; p-Nitrobenzaldehyde row; K_m (uM) column; raw K_m value 0.80 uM.

raw_value_unit_evidence: Table 2 reports p-Nitrobenzaldehyde K_m = 0.80 uM.

row_label: p-Nitrobenzaldehyde row; K_m column


substrate_name: prostaglandin H2

column_label: Table 2; PGH2 row; K_m (uM) column; raw K_m value 1.30 uM.

raw_value_unit_evidence: Table 2 reports PGH2 K_m = 1.30 uM.

row_label: PGH2 row; K_m column

substrate: prostaglandin H2


substrate_name: testosterone

substrate: testosterone


proof_lines:
pH 6.5-7.5, 30°C, recombinant enzyme
pH 6.5-7.5, 26°C, recombinant enzyme


organism: Synechocystis sp.

substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


organism: Oryctolagus cuniculus


organism: Saccharomyces cerevisiae


enzyme_display_name: indole-3-acetaldehyde reductase (NADH)

organism: Cucumis sativus

proof_lines: marked function of the NaCl concentration

enzyme: indole-3-acetaldehyde reductase (NADH)


assay_conditions_summary: pH 7

proof_lines:
at pH 7.0, isoenzyme TH
at pH 7.0, isoenzyme TL
at pH 5.2, isoenzyme TH


substrate_name: hexadecanol

smiles: CCCCCCCCCCCCCCCCO

substrate: hexadecanol


organism: Artemisia annua

substrate_name: 4-coumaryl aldehyde

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

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

column_label: Figure 2D p-coumaryl aldehyde column reports Km 11.05 +/- 1.4 and Kcat 12.36.

raw_value_unit_evidence: Figure 2D p-coumaryl aldehyde column: Km 11.05 +/- 1.4 uM; Kcat 12.36 s^-1; Kcat/Km 1.12 uM^-1 s^-1

row_label: p-coumaryl aldehyde

table_label: Figure 2D

substrate: 4-coumaryl aldehyde


organism: Sus scrofa


enzyme_display_name: Long-chain-alcohol dehydrogenase 1

organism: Geobacillus thermodenitrificans (strain NG80-2)

substrate_name: ethanol

smiles: CCO

proof_lines: kcat is 638.69 sec(-1) for ethanol. kcat is 404.77 sec(-1) for acetaldehyde. kcat is 443.05 sec(-1) for NAD. kcat is 1645.74 sec(-1) for NADH. kcat is 43.90 sec(-1) for NADP.

enzyme: Long-chain-alcohol dehydrogenase 1

substrate: ethanol


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: NAD

substrate: NAD


substrate_name: NADH

substrate: NADH


substrate_name: NADP

substrate: NADP


enzyme_display_name: Long-chain-alcohol dehydrogenase 2

proof_lines: kcat is 136.24 sec(-1) for ethanol. kcat is 138.05 sec(-1) for acetaldehyde. kcat is 260.71 sec(-1) for 1-octanol. kcat is 518.42 sec(-1) for octanal. kcat is 283.08 sec(-1) for NAD. kcat is 4808.18 sec(-1) for NADH. kcat is 38.50 sec(-1) f

enzyme: Long-chain-alcohol dehydrogenase 2


substrate_name: octanal

smiles: CCCCCCCC=O

substrate: octanal


organism: Oryza sativa Japonica Group

assay_conditions_summary: pH 6.3; 303.15 K; cofactor NADPH

column_label: Table 2. Kinetic parameters of recombinant OsCAD2, 6 and 7 catalyzed reactions toward hydroxycinnamaldehydes. Enzyme block 'OsCAD7'; substrate row 'Sinapaldehyde'; column 'KM (uM)' = 6.42; column 'Vmax (umol min^-1 mg^-1)' = 0.17; column 'kcat (min^-1)' = 7.65; column 'kcat/KM (uM^-1 min^-1)' = 1.27.

raw_value_unit_evidence: Table 2, enzyme block 'OsCAD7', substrate row 'Sinapaldehyde': KM = 6.42 uM; kcat = 7.65 min^-1; printed kcat/KM = 1.27 uM^-1 min^-1.


substrate_name: cinnamyl aldehyde

column_label: Table 2. Kinetic parameters of recombinant OsCAD2, 6 and 7 catalyzed reactions toward hydroxycinnamaldehydes. Enzyme block 'OsCAD7'; substrate row 'Cinnamaldehyde'; column 'KM (uM)' = 14.11; column 'Vmax (umol min^-1 mg^-1)' = 0.25; column 'kcat (min^-1)' = 11.29; column 'kcat/KM (uM^-1 min^-1)' = 0.82.

raw_value_unit_evidence: Table 2, enzyme block 'OsCAD7', substrate row 'Cinnamaldehyde': KM = 14.11 uM; kcat = 11.29 min^-1; printed kcat/KM = 0.82 uM^-1 min^-1.

substrate: cinnamyl aldehyde


column_label: Table 2. Kinetic parameters of recombinant OsCAD2, 6 and 7 catalyzed reactions toward hydroxycinnamaldehydes. Enzyme block 'OsCAD7'; substrate row 'Coniferaldehyde'; column 'KM (uM)' = 11.44; column 'Vmax (umol min^-1 mg^-1)' = 0.38; column 'kcat (min^-1)' = 17.09; column 'kcat/KM (uM^-1 min^-1)' = 1.52.

raw_value_unit_evidence: Table 2, enzyme block 'OsCAD7', substrate row 'Coniferaldehyde': KM = 11.44 uM; kcat = 17.09 min^-1; printed kcat/KM = 1.52 uM^-1 min^-1.


column_label: Table 2. Kinetic parameters of recombinant OsCAD2, 6 and 7 catalyzed reactions toward hydroxycinnamaldehydes. Enzyme block 'OsCAD2'; substrate row 'Cinnamaldehyde'; column 'KM (uM)' = 5.30; column 'Vmax (umol min^-1 mg^-1)' = 11.62; column 'kcat (min^-1)' = 543.15; column 'kcat/KM (uM^-1 min^-1)' = 142.14.

raw_value_unit_evidence: Table 2, enzyme block 'OsCAD2', substrate row 'Cinnamaldehyde': KM = 5.30 uM; kcat = 543.15 min^-1; printed kcat/KM = 142.14 uM^-1 min^-1.


column_label: Table 2. Kinetic parameters of recombinant OsCAD2, 6 and 7 catalyzed reactions toward hydroxycinnamaldehydes. Enzyme block 'OsCAD2'; substrate row 'Coniferaldehyde'; column 'KM (uM)' = 4.37; column 'Vmax (umol min^-1 mg^-1)' = 38.67; column 'kcat (min^-1)' = 1808.07; column 'kcat/KM (uM^-1 min^-1)' = 429.29.

raw_value_unit_evidence: Table 2, enzyme block 'OsCAD2', substrate row 'Coniferaldehyde': KM = 4.37 uM; kcat = 1808.07 min^-1; printed kcat/KM = 429.29 uM^-1 min^-1.


column_label: Table 2. Kinetic parameters of recombinant OsCAD2, 6 and 7 catalyzed reactions toward hydroxycinnamaldehydes. Enzyme block 'OsCAD2'; substrate row 'Sinapaldehyde'; column 'KM (uM)' = 8.19; column 'Vmax (umol min^-1 mg^-1)' = 52.86; column 'kcat (min^-1)' = 2471.41; column 'kcat/KM (uM^-1 min^-1)' = 321.14.

raw_value_unit_evidence: Table 2, enzyme block 'OsCAD2', substrate row 'Sinapaldehyde': KM = 8.19 uM; kcat = 2471.41 min^-1; printed kcat/KM = 321.14 uM^-1 min^-1.


organism: Bos taurus

substrate_name: Hydrindantin

proof_lines:
37°C, liver-type isozyme
lung enzyme

substrate: Hydrindantin


substrate_name: Prostaglandin D3

substrate: Prostaglandin D3


substrate_name: prostaglandin D1

substrate: prostaglandin D1


substrate_name: Prostaglandin D2

proof_lines: expressed liver prostaglandin F synthase

substrate: Prostaglandin D2


substrate_name: p-nitroacetophenone

substrate: p-nitroacetophenone


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


substrate_name: cyclohexanone

substrate: cyclohexanone


substrate_name: DL-glyceraldehyde

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

substrate: DL-glyceraldehyde


organism: Medicago truncatula

substrate_name: sinapyl aldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F226A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

proof_lines: Mt-CAD2 mutant F226A, pH and temperature not specified in the publication

substrate: sinapyl aldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y136F/F226A with inferred residue-numbering offset -22 to reconstruct the assayed variant sequence.

proof_lines: Mt-CAD2 mutant Y136F/F226A, pH and temperature not specified in the publication


substrate_name: coniferyl aldehyde

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

proof_lines: Mt-CAD1, pH and temperature not specified in the publication

proof_lines: kcat is 15.6 sec(-1) with coumaraldehyde as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:25217505). kcat is 9.1 sec(-1) with coniferaldehyde as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:25217505). kcat is 10.2 sec(-1) w

substrate: coniferyl aldehyde


substrate_name: p-coumaryl aldehyde

substrate: p-coumaryl aldehyde


substrate_name: prostaglandin E2

proof_lines: kcats are 2 min(-1), 285 min(-1), 460 min(-1), 58 min(-1) for prostaglandin E2, menadione, 9,1 O-phenanthrene-quinone and 4-nitrobenzaldehyde as substrates, respectively.

substrate: prostaglandin E2


substrate_name: menadione

substrate: menadione


substrate_name: NADPH

substrate: NADPH


organism: Sorghum bicolor

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A278V to reconstruct the assayed variant sequence.

proof_lines: isoform CAD4 mutant A278V, at pH 6.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L119W with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

proof_lines: isoform CAD4 mutant L119W, at pH 6.5 and 30°C


proof_lines:
liver enzyme
lung enzyme
37°C, liver-type isozyme


proof_lines:
lung enzyme
37°C, liver-type isozyme
liver enzyme


enzyme_display_name: Aldo-keto reductase family 1 member C3

organism: Homo sapiens

proof_lines: kcat is 0.044 min(-1) for testosterone oxydation (PubMed:10998348). kcat is 13 min(-1) for 9-cis-retinal as substrate (PubMed:21851338). kcat is 4.18 min(-1) for 17beta-hydroxy-5alpha-androstan-3-one reduction (PubMed:10998348). kcat is 0.3

enzyme: Aldo-keto reductase family 1 member C3


substrate_name: testosterone (oxidation)

substrate: testosterone (oxidation)


proof_lines:
expressed lung enzyme
lung enzyme
native lung prostaglandin F synthase


substrate_name: prostaglandin H2

proof_lines: native and expressed liver prostaglandin F synthase

substrate: prostaglandin H2


organism: Sinopodophyllum hexandrum

substrate_name: sinapaldehyde

proof_lines:
isoform CAD3, at pH 7.5 and 30°C
isoform CAD4, at pH 7.5 and 30°C
isoform CAD2, at pH 7.5 and 30°C

substrate: sinapaldehyde


substrate_name: coniferaldehyde

proof_lines:
isoform CAD1, at pH 7.5 and 30°C
isoform CAD2, at pH 7.5 and 30°C
isoform CAD4, at pH 7.5 and 30°C

substrate: coniferaldehyde


substrate_name: Prostaglandin A2

substrate: Prostaglandin A2


column_label: Table 1 row 5beta-Androstan-3alpha-ol-17-one lists Km 1 microM.

raw_value_unit_evidence: Km raw_value=1 raw_unit=microM

table_label: Table 1. Substrate specificity of the purified recombinant human PGFS.


column_label: Table 1 row 5beta-Androstane-3,17-dione lists Km 3.1 microM.

raw_value_unit_evidence: Km raw_value=3.1 raw_unit=microM


substrate_name: progesterone

substrate: progesterone


substrate_name: androstanediol

substrate: androstanediol


proof_lines: recombinant wild-type liver-type isozyme, 37°C


enzyme_display_name: Riboflavin biosynthesis protein PYRR, chloroplastic

organism: Zea mays

column_label: Table 1 row Maize full length / Intermediate 2 gives Km 0.19 mM.

raw_value_unit_evidence: Km raw_value=0.19 mM raw_unit=mM

row_label: Maize full length / Intermediate 2

table_label: Official PMC full-text Table 1: Kinetic constants of bacterial and plant COG3236 enzymes


organism: Arabidopsis thaliana

assay_conditions_summary: pH 6.25; 303.15 K; buffer pH 6; cofactor NADPH

column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD3 / substrate 4 (5-hydroxyconiferyl aldehyde / 5-hydroxyconiferaldehyde), columns Km (uM), kcat (sec^-1), kenz (M^-1 sec^-1).


column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD2 / substrate 4 (5-hydroxyconiferyl aldehyde / 5-hydroxyconiferaldehyde), columns Km (uM), kcat (sec^-1), kenz (M^-1 sec^-1).


substrate_name: Caffeic aldehyde

column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD5 / substrate 2 (caffeyl aldehyde / caffeic aldehyde), columns Km (uM), kcat (sec^-1), kenz (M^-1 sec^-1).

substrate: Caffeic aldehyde


column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD4 / substrate 2 (caffeyl aldehyde / caffeic aldehyde), columns Km (uM), kcat (sec^-1), kenz (M^-1 sec^-1).


column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD7 / substrate 2 (caffeyl aldehyde / caffeic aldehyde), columns Km (uM), kcat (sec^-1), kenz (M^-1 sec^-1).


column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD8 / substrate 2 (caffeyl aldehyde / caffeic aldehyde), columns Km (uM), kcat (sec^-1), kenz (M^-1 sec^-1).


assay_conditions_summary: pH 6.25; 303.15 K; cofactor NADPH

column_label: Table 2: Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8; row AtCAD3 / substrate 2 (caffeyl aldehyde / caffeic aldehyde); Km 0.581 mM; Vmax 9.7e-06 mol s^-1 g^-1; kcat 0.8 s^-1; kcat/Km 1.4 s^-1 mM^-1.

raw_value_unit_evidence: Km 581 uM; Vmax 9.7 pKat/ug; kcat 0.8 sec^-1; kenz 1,400 M^-1 sec^-1


column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD2 / substrate 2 (caffeyl aldehyde / caffeic aldehyde), columns Km (uM), kcat (sec^-1), kenz (M^-1 sec^-1).


substrate_name: Coniferaldehyde

column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD5 / substrate 3 (coniferyl aldehyde / coniferaldehyde), columns Km (uM), kcat (sec^-1), kenz (M^-1 sec^-1).

substrate: Coniferaldehyde


column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD4 / substrate 3 (coniferyl aldehyde / coniferaldehyde), columns Km (uM), kcat (sec^-1), kenz (M^-1 sec^-1).


enzyme_display_name: Cinnamyl alcohol dehydrogenase 5

substrate_name: 4-coumaraldehyde (at pH 6.25-6.5 and 30 degrees Celsius)

assay_conditions_summary: pH 6.25; cofactor NADPH

column_label: Table 2; row AtCAD5 / p-Coumaryl aldehyde (1); Km column

normalized_value_unit_evidence: Km=0.013 mM converted from 13 uM

raw_value_unit_evidence: Table 2 AtCAD5 / p-Coumaryl aldehyde (1) Km 13 uM

row_label: AtCAD5 / p-Coumaryl aldehyde (1)

table_label: Table 2

enzyme: Cinnamyl alcohol dehydrogenase 5


substrate_name: caffeyl aldehyde (at pH 6.0-6.25 and 30-35 degrees Celsius)

column_label: Table 2; row AtCAD5 / Caffeyl aldehyde (2); Km column

normalized_value_unit_evidence: Km=0.068 mM converted from 68 uM

raw_value_unit_evidence: Table 2 AtCAD5 / Caffeyl aldehyde (2) Km 68 uM

row_label: AtCAD5 / Caffeyl aldehyde (2)


substrate_name: coniferaldehyde (at pH 6.0-6.25 and 30-35 degrees Celsius)

column_label: Table 2; row AtCAD5 / Coniferyl aldehyde (3); Km column

normalized_value_unit_evidence: Km=0.035 mM converted from 35 uM

raw_value_unit_evidence: Table 2 AtCAD5 / Coniferyl aldehyde (3) Km 35 uM

row_label: AtCAD5 / Coniferyl aldehyde (3)


substrate_name: 5-hydroxyconiferaldehyde (at pH 6.25-6.5 and 30 degrees Celsius)

column_label: Table 2; row AtCAD5 / 5-Hydroxyconiferyl aldehyde (4); Km column

normalized_value_unit_evidence: Km=0.022 mM converted from 22 uM

raw_value_unit_evidence: Table 2 AtCAD5 / 5-Hydroxyconiferyl aldehyde (4) Km 22 uM


substrate_name: sinapaldehyde (at pH 6.0-6.25 and 30-35 degrees Celsius)

column_label: Table 2; row AtCAD5 / Sinapyl aldehyde (5); Km column

normalized_value_unit_evidence: Km=0.02 mM converted from 20 uM

raw_value_unit_evidence: Table 2 AtCAD5 / Sinapyl aldehyde (5) Km 20 uM

row_label: AtCAD5 / Sinapyl aldehyde (5)


enzyme_display_name: Cinnamyl alcohol dehydrogenase 3

substrate_name: 4-coumaraldehyde (at pH 6.25 and 40 degrees Celsius)

enzyme: Cinnamyl alcohol dehydrogenase 3


substrate_name: caffeyl aldehyde (at pH 6.25 and 40 degrees Celsius)


substrate_name: coniferaldehyde (at pH 6.25 and 40 degrees Celsius)


substrate_name: 5-hydroxyconiferaldehyde (at pH 6.25 and 37 degrees Celsius)


substrate_name: sinapaldehyde (at pH 6.25 and 40 degrees Celsius)


enzyme_display_name: Cinnamyl alcohol dehydrogenase 2

substrate_name: 4-coumaraldehyde (at pH 6.5 and 40 degrees Celsius)

enzyme: Cinnamyl alcohol dehydrogenase 2


substrate_name: caffeyl aldehyde (at pH 6.25-6.5 and 40 degrees Celsius)


substrate_name: coniferaldehyde (at pH 6.5 and 40 degrees Celsius)


substrate_name: 5-hydroxyconiferaldehyde (at pH 6.5 and 37 degrees Celsius)


substrate_name: sinapaldehyde (at pH 6.5 and 40 degrees Celsius)


enzyme_display_name: Cinnamyl alcohol dehydrogenase 4

substrate_name: 4-coumaraldehyde (at pH 6.25-6.5 and 35 degrees Celsius)

enzyme: Cinnamyl alcohol dehydrogenase 4


substrate_name: caffeyl aldehyde (at pH 6.25 and 30 degrees Celsius)

column_label: Table 2; row AtCAD4 / Caffeyl aldehyde (2); Km column

normalized_value_unit_evidence: Km=0.087 mM converted from 87 uM

raw_value_unit_evidence: Table 2 AtCAD4 / Caffeyl aldehyde (2) Km 87 uM

row_label: AtCAD4 / Caffeyl aldehyde (2)


substrate_name: coniferaldehyde (at pH 6.25-6.5 and 35 degrees Celsius)


column_label: Table 2; row AtCAD4 / 5-Hydroxyconiferyl aldehyde (4); Km column

normalized_value_unit_evidence: Km=0.085 mM converted from 85 uM

raw_value_unit_evidence: Table 2 AtCAD4 / 5-Hydroxyconiferyl aldehyde (4) Km 85 uM

substrate: 5-hydroxyconiferaldehyde (at pH 6.25-6.5 and 30 degrees Celsius)


substrate_name: sinapaldehyde (at pH 6.25-6.5 and 30 degrees Celsius)

column_label: Table 2; row AtCAD4 / Sinapyl aldehyde (5); Km column

normalized_value_unit_evidence: Km=0.274 mM converted from 274 uM

raw_value_unit_evidence: Table 2 AtCAD4 / Sinapyl aldehyde (5) Km 274 uM

row_label: AtCAD4 / Sinapyl aldehyde (5)