enzyme_display_name: Retinol dehydrogenase 12

proof_lines: kcat is 36 min(-1) for all-trans-retinal as substrate. kcat is 45 min(-1) for 11-cis-retinal as substrate. kcat is 14 min(-1) for 9-cis-retinal as substrate. kcat is 27 min(-1) for all-trans-retinol as substrate. kcat is 7 min(-1) for 11-ci

enzyme: Retinol dehydrogenase 12


organism: Homo sapiens

substrate_name: NADH

source_db: uniprot

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: cofactor NADH

data_origin: experimental

substrate: NADH

status: unverified

source: uniprot


substrate_name: all-trans-retinal

substrate: all-trans-retinal


substrate_name: nonanal

smiles: CCCCCCCCC=O

substrate: nonanal


smiles: CCCCCCC=CC=O


smiles: CCC=CCCCCC=O


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)

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

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)


enzyme_display_name: NADP-dependent 3-hydroxy acid dehydrogenase YdfG

organism: Escherichia coli (strain K12)

substrate_name: NADP(+) (at pH 9 and at 30 degrees Celsius)

assay_conditions_summary: pH 9

proof_lines: The highest catalytic efficiency was observed with L-allo-threonine.


substrate_name: L-serine (at pH 9 and at 30 degrees Celsius)

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

enzyme: NADP-dependent 3-hydroxy acid dehydrogenase YdfG


substrate_name: D-threonine (at pH 9 and at 30 degrees Celsius)

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


substrate_name: L-glycerate (at pH 9 and at 30 degrees Celsius)

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


substrate_name: D-glycerate (at pH 9 and at 30 degrees Celsius)


enzyme_display_name: Aldo-keto reductase family 1 member B15

substrate_name: androsterone (tested with isoform 1 in the reductive reaction)

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 1.7 min(-1) using isoform 1 for the reduction of androsterone. kcat is 1.1 min(-1) using isoform 1 for the reduction of delta-4-androstenedione. kcat is 1.0 min(-1) using isoform 1 for the reduction of estrone. kcat is 0.5 min(-1) u

enzyme: Aldo-keto reductase family 1 member B15


substrate_name: delta-4-androstenedione (tested with isoform 1 in the reductive reaction)


substrate_name: estrone (tested with isoform 1 in the reductive reaction)


substrate_name: acetoacetyl-CoA (tested with isoform 1 in the reductive reaction)


substrate_name: testosterone (tested with isoform 1 in the oxidative reaction)


substrate_name: 17-beta-estradiol (tested with isoform 1 in the oxidative reaction)


organism: Sus scrofa

substrate_name: 16-Ketoestrone (at pH6)

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:

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: 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)


enzyme_display_name: Retinol dehydrogenase 14

substrate_name: NADPH

verification_status: verified

assay_conditions_summary: cofactor NADPH

column_label: Abstract/prose sentence lists NADPH apparent Km = 0.32 uM, matching the UniProt exported row after conversion to 0.00032 mM.

raw_value_unit_evidence: Abstract/prose reports apparent Km for NADPH is 0.32 uM.

row_label: NADPH

table_label: Abstract/prose apparent Km sentence

enzyme: Retinol dehydrogenase 14

substrate: NADPH

status: verified


substrate_name: NADP

assay_conditions_summary: cofactor NADP+

column_label: Abstract/prose sentence lists NADP+ apparent Km = 0.65 uM, matching the UniProt exported NADP/NADP+ row after conversion to 0.00065 mM.

raw_value_unit_evidence: Abstract/prose reports apparent Km for NADP+ is 0.65 uM.

row_label: NADP+ cofactor (export substrate label NADP)

substrate: NADP


substrate_name: all-trans-retinal

proof_lines: Vmax is measured per mg microsomal protein.

substrate: all-trans-retinal


substrate_name: all-trans-retinol

substrate: all-trans-retinol


substrate_name: NADH

column_label: Abstract/prose sentence lists NADH apparent Km = 1060 uM, matching the UniProt exported row after conversion to 1.06 mM.

normalized_value_unit_evidence: 1060 uM = 1.06 mM; exported Km is 1.06 mM.

raw_value_unit_evidence: Abstract/prose reports apparent Km for NADH is 1060 uM.

row_label: NADH

substrate: NADH


enzyme_display_name: D-arabitol-phosphate dehydrogenase

organism: Enterococcus avium

source_db: brenda

assay_conditions_summary: pH 7.2; cofactor NADH

proof_lines: 20°C, pH 7.2, cosubstrate: D-xylulose 5-phosphate

enzyme: D-arabitol-phosphate dehydrogenase

source: brenda


assay_conditions_summary: pH 7.2; cofactor NADPH


substrate_name: NAD+

assay_conditions_summary: pH 8.5; cofactor NAD+

proof_lines: 20°C, pH 8.5: cosubstrate: D-arabitol 5-phosphate

proof_lines: 20°C, pH 8.5, cosubstrate: D-arabitol 1-phosphate

substrate: NAD+


substrate_name: NADP+

assay_conditions_summary: pH 8.5; cofactor NADP+

substrate: NADP+


substrate_name: D-arabitol 1-phosphate

proof_lines:
20°C, pH 8.5, cofactor: NAD+
20°C, pH 8.5, cofactor: NADP+

substrate: D-arabitol 1-phosphate


enzyme_display_name: diacetyl reductase [(S)-acetoin forming]

organism: Columba livia

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

assay_conditions_summary: pH 5.9; 298.15 K; cofactor NADH


substrate_name: diacetyl

assay_conditions_summary: pH 6.7; 298.15 K; cofactor NADH

enzyme: diacetyl reductase [(S)-acetoin forming]

substrate: diacetyl


enzyme_display_name: malate dehydrogenase [NAD(P)+]

organism: Flavobacterium frigidimaris

assay_conditions_summary: 283.15 K; cofactor NAD+

enzyme: malate dehydrogenase [NAD(P)+]


substrate_name: L-malate

substrate: L-malate


enzyme_display_name: Aldo-keto reductase family 1 member B1

substrate_name: acrolein

smiles: C=CC=O

proof_lines: kcat is 15 min(-1) for all-trans-retinal as substrate. kcat is 30 min(-1) for 9-cis-retinal as substrate. kcat is 94 min(-1) for 13-cis-retinal as substrate (PubMed:12732097). kcat is 11 min(-1) for acrolein as substrate. kcat is 31 min(-1)

enzyme: Aldo-keto reductase family 1 member B1

substrate: acrolein


smiles: CC(=CC=O)C


smiles: CCCC=CC=O


smiles: CC=CC=CC=O


smiles: CCCCCC(C=CC=O)O


organism: Geobacillus stearothermophilus


enzyme_display_name: D-xylose reductase [NAD(P)H]

organism: Yamadazyma tenuis

km_display: Not reported

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K274M to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7; cofactor NADPH

enzyme: D-xylose reductase [NAD(P)H]


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K274R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; cofactor NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K274G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K274R/N276D with inferred residue-numbering offset -23 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N276D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R280H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S275A with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.


organism: Thermochaetoides thermophila

substrate_name: D-glucose

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH

proof_lines: recombinant enzyme, pH 6.5, 30°C, with NADPH

substrate: D-glucose


assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADH

proof_lines: recombinant enzyme, pH 6.5, 30°C, with D-xylose


substrate_name: L-arabinose

proof_lines: recombinant enzyme, pH 6.5, 55°C, with NADPH

substrate: L-arabinose


organism: Neurospora crassa

substrate_name: D-xylose

assay_conditions_summary: pH 6.3; 298.15 K; cofactor NADPH

proof_lines:
pH 6.3, 25°C, cosubstrate: NADH
pH 6.3, 25°C
pH 6.3, 25°C, cosubstrate: NADPH

substrate: D-xylose


assay_conditions_summary: pH 6.3; 298.15 K; cofactor NADH


organism: Scheffersomyces stipitis

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K21A with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; cofactor NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K21A/N272D to reconstruct the assayed variant sequence.


proof_lines: pH 6.0, wild-type enzyme, wild-type enzyme


proof_lines: mutant K21A/N272D, cosubstrate NADH, pH 6.5, 35°C


proof_lines: mutant K21A, cosubstrate NADH, pH 6.5, 35°C


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)

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

assay_conditions_summary: pH 6

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)


enzyme_display_name: Aldo-keto reductase family 1 member B10

proof_lines: kcat is 640 min(-1) for glyceraldehyde as substrate (PubMed:12732097). kcat is 185 min(-1) for pyridine-3-aldehyde as substrate (PubMed:12732097). kcat is 116 min(-1) for acrolein as substrate. kcat is 103 min(-1) for 3-methyl-2-butenal as

enzyme: Aldo-keto reductase family 1 member B10


enzyme_display_name: UniProt D3U1D9

organism: Klebsiella oxytoca

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt D3U1D9

source: skid


substrate_name: isethionate

substrate: isethionate


enzyme_display_name: UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)

organism: Ralstonia solanacearum

substrate_name: UDP-glucuronic acid

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

substrate: UDP-glucuronic acid


assay_conditions_summary: pH 7.6; cofactor NAD+

enzyme: UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)


organism: Mus musculus

substrate_name: D,L-glyceraldehyde

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

proof_lines: kcat is 1.3 sec(-1) for D,L-glyceraldehyde as substrate. kcat is 0.95 sec(-1) for D-xylose as substrate. kcat is 0.9 sec(-1) for D-glucose as substrate. kcat is 1.1 sec(-1) for D-galactose as substrate. kcat is 0.9 sec(-1) for D-glucuronate

substrate: D,L-glyceraldehyde


substrate_name: D-glucuronate

substrate: D-glucuronate


enzyme_display_name: (S)-sulfolactate dehydrogenase

organism: Chromohalobacter israelensis

substrate_name: NADH

assay_conditions_summary: pH 9; 298.15 K; buffer 25 mM Tris; cofactor NADH

proof_lines: apparent value, in 25 mM Tris buffer, pH 9.0 and 25°C

enzyme: (S)-sulfolactate dehydrogenase

substrate: NADH


assay_conditions_summary: pH 9; 298.15 K; buffer 25 mM Tris


substrate_name: NAD+

sequence_source: multiple

assay_conditions_summary: pH 9; 298.15 K; buffer 25 mM Tris; cofactor NAD+

source_databases_merged: brenda uniprot

substrate: NAD+


enzyme_display_name: Retinol dehydrogenase 11

substrate_name: all-trans-retinal

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 167 min(-1) for NADPH as substrate.

enzyme: Retinol dehydrogenase 11

substrate: all-trans-retinal


smiles: CCCCCCCCCO


substrate_name: NADPH

substrate: NADPH


enzyme_display_name: Malate dehydrogenase

organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)

substrate_name: (2S,3S)-tartrate (in the presence of NAD)

proof_lines: kcat is 2.6 sec(-1) for NAD-dependent malate oxidation. kcat is 1.4 sec(-1) for NADP-dependent malate oxidation.

enzyme: Malate dehydrogenase


substrate_name: NAD (in the presence of malate)

substrate: NAD (in the presence of malate)


substrate_name: NADP (in the presence of malate)

substrate: NADP (in the presence of malate)


organism: Homo sapiens


substrate_name: glucose

substrate: glucose


enzyme_display_name: 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase

organism: Sphingomonas paucimobilis

assay_conditions_summary: cofactor NAD+

proof_lines:
in the presence of NAD+
in the presence of NADP+


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

enzyme: 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase

substrate: NADP+


organism: Chlorobaculum tepidum

substrate_name: diacetyl

substrate: diacetyl


enzyme_display_name: 5-exo-hydroxycamphor dehydrogenase

organism: Pseudomonas putida

enzyme: 5-exo-hydroxycamphor dehydrogenase


enzyme_display_name: isoeugenol synthase

organism: Daucus carota subsp. sativus

substrate_name: coniferyl acetate

enzyme: isoeugenol synthase

substrate: coniferyl acetate


assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH


enzyme_display_name: eugenol synthase

organism: Ocimum kilimandscharicum

enzyme: eugenol synthase


substrate_name: 4-coumaryl acetate

substrate: 4-coumaryl acetate


organism: Phytopseudomonas straminea

assay_conditions_summary: 298.15 K; cofactor NADP+


substrate_name: Unknown

ki_unit: mM

proof_lines: coenzyme NADP+, similar value with coenzyme NAD+

substrate: Unknown


organism: Larrea tridentata


enzyme_display_name: UniProt Q7NQL0

organism: Chromobacterium violaceum

substrate_name: UDP-alpha-D-glucuronate

enzyme: UniProt Q7NQL0

substrate: UDP-alpha-D-glucuronate


organism: Ocimum tenuiflorum


enzyme_display_name: benzil reductase [(S)-benzoin forming]

organism: Ogataea glucozyma

substrate_name: benzil

protein_accession_database: NCBI Protein

sequence_source: GenBank: AKP95857.1

assay_conditions_summary: pH 8; cofactor NADPH

enzyme: benzil reductase [(S)-benzoin forming]

substrate: benzil


enzyme_display_name: chanoclavine-I dehydrogenase

organism: Penicillium roqueforti

assay_conditions_summary: 303.15 K; cofactor NAD+

proof_lines: pH not specified in the publication, 30°C

enzyme: chanoclavine-I dehydrogenase


substrate_name: chanoclavine-I

substrate: chanoclavine-I


organism: Trichophyton benhamiae


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+


organism: Bordetella pertussis


proof_lines: presence of transaminase WlbC, 25°C, pH 8.5


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NAD+


enzyme_display_name: (+)-thujan-3-ol dehydrogenase

organism: Tanacetum vulgare

enzyme: (+)-thujan-3-ol dehydrogenase


enzyme_display_name: (-)-endo-fenchol dehydrogenase

organism: Anethum foeniculum

substrate_name: (-)-endo-fenchol

enzyme: (-)-endo-fenchol dehydrogenase

substrate: (-)-endo-fenchol


organism: Ocimum gratissimum


organism: Weissella confusa

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

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


substrate_name: phenylglyoxylate

substrate: phenylglyoxylate


substrate_name: pyruvate

substrate: pyruvate


substrate_name: phenylpyruvate

substrate: phenylpyruvate


substrate_name: oxo-tert-leucine

substrate: oxo-tert-leucine


sequence_source: GenBank: AAQ61788.1

column_label: pmc3050068_jats.xml table-wrap T3: row Km for the UDP-sugar / column C. violaceum WlbA with UDP-GlcA = 0.20 +/- 0.02; row kcat = 0.00015 +/- 0.00001; row kcat/Km UDP-linked sugar = 0.75

raw_value_unit_evidence: Table 3 column C. violaceum WlbA with UDP-GlcA: Km 0.20 +/- 0.02 mM; kcat 0.00015 +/- 0.00001 s^-1; kcat/Km 0.75 M^-1 s^-1

row_label: C. violaceum WlbA with UDP-GlcA; rows Km for the UDP-sugar, kcat, kcat/Km UDP-linked sugar

table_label: Table 3 Kinetic Parameters


substrate_name: NAD+

assay_conditions_summary: pH 8.5; cofactor NAD+

column_label: pmc3050068_jats.xml table-wrap T3: row Km NAD+ / column C. violaceum WlbA with UDP-GlcNAcA = 0.47 +/- 0.07

normalized_value_unit_evidence: Km 0.47 mM

raw_value_unit_evidence: Table 3 column C. violaceum WlbA with UDP-GlcNAcA: Km NAD+ 0.47 +/- 0.07 mM

row_label: C. violaceum WlbA with UDP-GlcNAcA; row Km NAD+

substrate: NAD+


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


organism: Pimpinella anisum

sequence_source: UniProt: B8RCD2


enzyme_display_name: D-2-hydroxyacid dehydrogenase (NAD+)

organism: Lacticaseibacillus paracasei

substrate_name: NADH

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

proof_lines:
pH 7.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7

source_databases_merged: brenda skid uniprot

enzyme: D-2-hydroxyacid dehydrogenase (NAD+)

substrate: NADH


proof_lines: pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88


proof_lines: pH 7.0, 30°C, mutant enzyme del I81/delK82


proof_lines:
pH 7.0, 30°C, mutant enzyme del I81
pH 7.0, 30°C, mutant enzyme delK82
pH 7.0, 30°C, mutant enzyme delP88


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

organism: Thermotoga maritima

assay_conditions_summary: pH 7.5; 343.15 K; cofactor NAD+

proof_lines: wild type enzyme, in 100 mM HEPES (pH 7.5), at 70°C


proof_lines: mutant enzyme N32D/R33L/T34S, in 100 mM HEPES (pH 7.5), at 70°C

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


proof_lines: mutant enzyme N32D, in 100 mM HEPES (pH 7.5), at 70°C


proof_lines: mutant enzyme N32D/R33I/T34I, in 100 mM HEPES (pH 7.5), at 70°C


proof_lines: mutant enzyme N32E/R33I7T34I, in 100 mM HEPES (pH 7.5), at 70°C


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


substrate_name: L-lactate

substrate: L-lactate


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


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


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


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


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


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


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


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


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

organism: Gossypium hirsutum

substrate_name: NADPH

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

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

substrate: NADPH


substrate_name: Nonanal

smiles: CCCCCCCCC=O

substrate: Nonanal


enzyme_display_name: L-galactose 1-dehydrogenase

organism: Lathyrus oleraceus

substrate_name: L-galactose

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

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: L-galactose 1-dehydrogenase

substrate: L-galactose


organism: Methanobrevibacter millerae

assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADH


substrate_name: sulfopyruvate

substrate: sulfopyruvate


organism: Gluconacetobacter diazotrophicus

proof_lines: pH 7.5, temperature not specified in the publication, membrane-purified enzyme

proof_lines: pH 7.5, temperature not specified in the publication, cytoplasm-purified enzyme


substrate_name: NADP+

assay_conditions_summary: pH 7.5; cofactor NADP+

substrate: NADP+


assay_conditions_summary: pH 7.5; cofactor NAD+


organism: Methanothermus fervidus

assay_conditions_summary: pH 8; 343.15 K; cofactor NADH

proof_lines:
cosubstrate NADH, pH 8.0, 70°C
cosubstrate NADPH, pH 8.0, 70°C


substrate_name: oxaloacetate

substrate: oxaloacetate


enzyme_display_name: 8-hydroxygeraniol dehydrogenase

organism: Rauvolfia serpentina

substrate_name: Nerol; NADP+

source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org)

assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+

enzyme: 8-hydroxygeraniol dehydrogenase

substrate: Nerol; NADP+


assay_conditions_summary: pH 7


organism: Petunia x hybrida

substrate_name: coniferyl acetate

substrate: coniferyl acetate


organism: Musca domestica

substrate_name: sepiapterin

proof_lines:
pH 6.4, 37°C
pH 6.4, 37°C, recombinant enzyme

substrate: sepiapterin


enzyme_display_name: Benzil reductase ((S)-benzoin forming)

organism: Bacillus cereus

substrate_name: benzil (with NADPH at 37 degrees Celsius and pH 6.5)

assay_conditions_summary: pH 6.5; cofactor NADPH

proof_lines: kcat is 64.4 min(-1) with benzil as substrate. kcat is 165 min(-1) with 1-phenyl-1,2-propanedione as substrate. kcat is 7.4 min(-1) with 1,4-naphthoquinone as substrate. kcat is 1.2 min(-1) with p-nitrobenzaldehyde as substrate. kcat is 31.

enzyme: Benzil reductase ((S)-benzoin forming)


substrate_name: 1-phenyl-1,2-propanedione (with NADPH at 37 degrees Celsius and pH 6.5)


substrate_name: 1,4-naphthoquinone (with NADPH at 37 degrees Celsius and pH 6.5)


substrate_name: p-nitrobenzaldehyde (with NADPH and at 37 degrees Celsius and pH 6.5)


substrate_name: methyl benzoylformate (with NADPH and at 37 degrees Celsius and pH 6.5)


enzyme_display_name: CDP-paratose synthase

organism: Salmonella enterica subsp. enterica serovar Typhi

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

enzyme: CDP-paratose synthase


enzyme_display_name: Retinol dehydrogenase 11

organism: Homo sapiens

assay_conditions_summary: cofactor NADPH

proof_lines: Vmax is measured per mg microsomal protein.

enzyme: Retinol dehydrogenase 11


substrate_name: NADP

substrate: NADP


substrate_name: all-trans-retinal

substrate: all-trans-retinal


substrate_name: all-trans-retinol

substrate: all-trans-retinol


enzyme_display_name: D-xylose reductase [NAD(P)H]

organism: Scheffersomyces stipitis

substrate_name: D-xylose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K270S/N272P/S271G/R276F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; cofactor NADPH

proof_lines: pH 6.0, cofactor: NADPH, mutant enzyme K270S/N272P/S271G/R276F

proof_lines: pH 6.0, cofactor: NADH, mutant enzyme K270S/N272P/S271G/R276F

enzyme: D-xylose reductase [NAD(P)H]

substrate: D-xylose


substrate_name: NADPH

proof_lines: pH 6.0, mutant enzyme K270S/N272P/S271G/R276F


substrate_name: NADH

assay_conditions_summary: pH 6; cofactor NADH


proof_lines: pH 6.0, cofactor: NADH, wild-type enzyme

proof_lines: pH 6.0, cofactor: NADPH, wild-type enzyme

proof_lines: wild-type, cosubstrate NADPH, pH 6.5, 35°C


proof_lines: pH 6.0, wild-type enzyme, wild-type enzyme


organism: Methanocaldococcus jannaschii

assay_conditions_summary: pH 8; cofactor NADPH

proof_lines:
pH 8.0, 70°C
cosubstrate NADH, pH 8.0, 70°C
cosubstrate NADPH, pH 8.0, 70°C


substrate_name: 2-oxopentanedioic acid

assay_conditions_summary: pH 8; cofactor NADH

proof_lines:
pH 8.0, 70°C
cosubstrate NADH, pH 8.0, 70°C

substrate: 2-oxopentanedioic acid


enzyme_display_name: methylecgonone reductase

organism: Erythroxylum coca

substrate_name: NADP+

assay_conditions_summary: pH 6.8; cofactor NADP+

proof_lines: pH 6.8, temperature not specified in the publication

enzyme: methylecgonone reductase


enzyme_display_name: Dehydrogenase/reductase SDR family member 4

organism: Oryctolagus cuniculus

substrate_name: 4-Acetylpyridine (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: 4-Acetylpyridine (at pH6)


substrate_name: Pyridine-3-aldehyde (at pH6)

enzyme: Dehydrogenase/reductase SDR family member 4

substrate: Pyridine-3-aldehyde (at pH6)


substrate_name: 4-Nitroacetophenone (at pH6)

substrate: 4-Nitroacetophenone (at pH6)


enzyme_display_name: NADP-retinol dehydrogenase

organism: Danio rerio

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M147G with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

enzyme: NADP-retinol dehydrogenase


substrate_name: estrone

substrate: estrone


enzyme_display_name: zerumbone synthase

organism: Zingiber zerumbet

substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y155A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

enzyme: zerumbone synthase

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S142A to reconstruct the assayed variant sequence.


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

assay_conditions_summary: pH 8; cofactor NAD+

column_label: Table label: Table 1. Kinetic parameters for recombinant wild-type ZSD1 and four mutants. ND, enzymatic activity was not detected.. Row: Wild-type. Substrate column group: 8-HAH. Columns read: Km (lM) cell 58.5, kcat (s)1) cell 1.3, kcat ⁄ Km (lM)1Æs)1) cell 2.2 · 10)2. metric: kcat; raw value: 1.3; raw unit: s^-1; normalized value: 1.3 s^(-1); metric: Km; raw value: 58.5; raw unit: uM; normalized value: 0.0585 mM; metric: kcat/Km; raw value: 1.3 / 58.5; raw unit: s^-1 over uM; normalized value: 22.22222222222222 s^-1 mM^-1; assay condition: Recombinant wild-type ZSD1 (Zingiber zerumbet short-chain dehydrogenase, expressed in Escherichia coli and purified); kinetics assay done in a volume of 1 mL with 20 mM KH2PO4 (pH 8.0), 1 mM NAD and 10 mM EDTA; the reaction was monitored at 37 C by absorbance at 340 nm. Export row conditions: pH 8.

normalized_value_unit_evidence: 8-HAH column group of Table 1 wild-type row: kcat 1.3 s^-1 = 1.3 s^(-1); Km 58.5 uM = 0.0585 mM (1 uM = 0.001 mM); kcat/Km = 1.3 s^-1 / 58.5 uM = 22.22222222222222 s^-1 mM^-1. The printed kcat ⁄ Km cell 2.2 · 10)2 lM)1Æs)1 is the paper's 2.2 x 10^-2 uM^-1 s^-1 = 22.0 s^-1 mM^-1; the exported quotient rounds to that printed cell at the printed cell's own precision, so the two agree. In the PDF text layer the micro sign renders as `l` (so `lM` is the paper's uM), the superscript minus one renders as `)1` (so `s)1` is s^-1 and `10)1` is 10^-1), the multiplication sign renders as `·`, the fraction slash in kcat ⁄ Km renders as `⁄`, and the middle dot in compound units renders as `Æ`.

raw_value_unit_evidence: Table 1. Kinetic parameters for recombinant wild-type ZSD1 and four mutants. ND, enzymatic activity was not detected. | substrate column-group header row of Table 1: NAD+                                          8-HAH                                         Borneol | metric header row (superscripts flattened by the PDF text layer): Km (lM)   kcat (s )   kcat ⁄ Km (lM Æs )      Km (lM)   kcat (s )   kcat ⁄ Km (lM Æs )      Km (lM)   kcat (s)1)   kcat ⁄ Km (lM)1Æs)1) | wild-type data row: Wild-type    27.3     3.8         1.39 · 10)1              58.5     1.3         2.2 · 10)2               22.8     4.1          1.79 · 10)1 | 8-HAH column group of the wild-type row reads: Km = 58.5 lM (58.5 uM); kcat = 1.3 s^-1; printed kcat ⁄ Km cell = 2.2 · 10)2 lM)1Æs)1 (2.2 x 10^-2 uM^-1 s^-1).

row_label: Wild-type | 8-HAH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S144A to reconstruct the assayed variant sequence.


column_label: Table label: Table 1. Kinetic parameters for recombinant wild-type ZSD1 and four mutants. ND, enzymatic activity was not detected.. Row: Wild-type. Substrate column group: NAD+. Columns read: Km (lM) cell 27.3, kcat (s)1) cell 3.8, kcat ⁄ Km (lM)1Æs)1) cell 1.39 · 10)1. metric: kcat; raw value: 3.8; raw unit: s^-1; normalized value: 3.8 s^(-1); metric: Km; raw value: 27.3; raw unit: uM; normalized value: 0.0273 mM; metric: kcat/Km; raw value: 3.8 / 27.3; raw unit: s^-1 over uM; normalized value: 139.19413919413918 s^-1 mM^-1; assay condition: Recombinant wild-type ZSD1 (Zingiber zerumbet short-chain dehydrogenase, expressed in Escherichia coli and purified); kinetics assay done in a volume of 1 mL with 20 mM KH2PO4 (pH 8.0), 1 mM NAD and 10 mM EDTA; the reaction was monitored at 37 C by absorbance at 340 nm. Export row conditions: pH 8; cofactor NAD+.

normalized_value_unit_evidence: NAD+ column group of Table 1 wild-type row: kcat 3.8 s^-1 = 3.8 s^(-1); Km 27.3 uM = 0.0273 mM (1 uM = 0.001 mM); kcat/Km = 3.8 s^-1 / 27.3 uM = 139.19413919413918 s^-1 mM^-1. The printed kcat ⁄ Km cell 1.39 · 10)1 lM)1Æs)1 is the paper's 1.39 x 10^-1 uM^-1 s^-1 = 139.0 s^-1 mM^-1; the exported quotient rounds to that printed cell at the printed cell's own precision, so the two agree. In the PDF text layer the micro sign renders as `l` (so `lM` is the paper's uM), the superscript minus one renders as `)1` (so `s)1` is s^-1 and `10)1` is 10^-1), the multiplication sign renders as `·`, the fraction slash in kcat ⁄ Km renders as `⁄`, and the middle dot in compound units renders as `Æ`.

raw_value_unit_evidence: Table 1. Kinetic parameters for recombinant wild-type ZSD1 and four mutants. ND, enzymatic activity was not detected. | substrate column-group header row of Table 1: NAD+                                          8-HAH                                         Borneol | metric header row (superscripts flattened by the PDF text layer): Km (lM)   kcat (s )   kcat ⁄ Km (lM Æs )      Km (lM)   kcat (s )   kcat ⁄ Km (lM Æs )      Km (lM)   kcat (s)1)   kcat ⁄ Km (lM)1Æs)1) | wild-type data row: Wild-type    27.3     3.8         1.39 · 10)1              58.5     1.3         2.2 · 10)2               22.8     4.1          1.79 · 10)1 | NAD+ column group of the wild-type row reads: Km = 27.3 lM (27.3 uM); kcat = 3.8 s^-1; printed kcat ⁄ Km cell = 1.39 · 10)1 lM)1Æs)1 (1.39 x 10^-1 uM^-1 s^-1).

row_label: Wild-type | NAD+


enzyme_display_name: Zerumbone synthase

substrate_name: NAD

assay_conditions_summary: pH 8; cofactor NADP+

column_label: Table 1 wild-type row, NAD+ Km column reports 27.3 uM and kcat 3.8 s^-1; 27.3 uM normalizes to 0.0273 mM.

raw_value_unit_evidence: Km raw_value=27.3 raw_unit=uM; kcat raw_value=3.8 raw_unit=s^-1

row_label: Wild-type

table_label: Table 1. Kinetic parameters for recombinant wild-type ZSD1 and four mutants

enzyme: Zerumbone synthase

substrate: NAD


column_label: Table 1 wild-type row, 8-HAH Km column reports 58.5 uM and kcat 1.3 s^-1; 58.5 uM normalizes to 0.0585 mM.

raw_value_unit_evidence: Km raw_value=58.5 raw_unit=uM; kcat raw_value=1.3 raw_unit=s^-1


substrate_name: borneol

column_label: Table 1 wild-type row, Borneol Km column reports 22.8 uM and kcat 4.1 s^-1; 22.8 uM normalizes to 0.0228 mM.

raw_value_unit_evidence: Km raw_value=22.8 raw_unit=uM; kcat raw_value=4.1 raw_unit=s^-1

substrate: borneol


organism: Rasamsonia emersonii

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K271R/N273D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADPH

substrate: NADPH


enzyme_display_name: phosphonoacetaldehyde reductase (NADH)

organism: Streptomyces viridochromogenes

substrate_name: phosphonoacetaldehyde

proof_lines: in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication

enzyme: phosphonoacetaldehyde reductase (NADH)

substrate: phosphonoacetaldehyde


assay_conditions_summary: pH 7.5; cofactor NADH


assay_conditions_summary: pH 6.8; cofactor NADPH

proof_lines: substrate inhibition, pH 6.8, temperature not specified in the publication

proof_lines: kcat is 0.24 sec(-1) for ecgonone methyl ester. kcat is 0.121 sec(-1) for NADPH. kcat is 5.538 sec(-1) for ecgonine methyl ester. kcat is 5.238 sec(-1) for NADP(+).


substrate: NADP+


substrate_name: methyl ecgonone

substrate: methyl ecgonone


substrate_name: methyl ecgonine

substrate: methyl ecgonine


enzyme_display_name: Methylecgonone reductase

substrate_name: NADP(+)

enzyme: Methylecgonone reductase

substrate: NADP(+)


organism: Spathaspora arborariae


enzyme_display_name: Aldo-keto reductase family 1 member B10

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

column_label: The abstract reports AKR1B10 reduces 4-oxonon-2-enal with Km = 0.3 mM and kcat = 40 min^-1.

raw_value_unit_evidence: Km raw_value=0.3 mM raw_unit=mM

row_label: Prose segment: 4-oxonon-2-enal Km

table_label: PubMed PMID 19013440 abstract

enzyme: Aldo-keto reductase family 1 member B10


smiles: CC(C)CCC=O

column_label: The abstract reports AKR1B10 reduces 4-methylpentanal with Km = 0.05 mM and kcat = 25 min^-1.

raw_value_unit_evidence: Km raw_value=0.05 mM raw_unit=mM

row_label: Prose segment: 4-methylpentanal Km


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7.5; cofactor NAD+

proof_lines: pH 7.5, temperature not specified in the publication


substrate_name: L-galactose

substrate: L-galactose


assay_conditions_summary: pH 7.5; cofactor NADP+


substrate_name: L-fucose

substrate: L-fucose


enzyme_display_name: Eugenol synthase 1

organism: Clarkia breweri

substrate_name: coniferyl acetate

raw_value_unit_evidence: Km raw_value=93.3 raw_unit=uM

table_label: Table 3 - Kinetic parameters of C. breweri and P. hybrida EGS and IGS enzymes for coniferyl acetate

enzyme: Eugenol synthase 1

substrate: coniferyl acetate


enzyme_display_name: Eugenol synthase 2

raw_value_unit_evidence: Km raw_value=310.5 raw_unit=uM

enzyme: Eugenol synthase 2


enzyme_display_name: Benzil reductase ((S)-benzoin forming) IRC24

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: benzil (with NADPH as cosubstrate)

proof_lines: kcat is 9.2 min(-1) with benzil as substrate. kcat is 86.2 min(-1) with 1-phenyl-1,2-propanedione as substrate.

substrate: benzil (with NADPH as cosubstrate)


enzyme: Benzil reductase ((S)-benzoin forming) IRC24


enzyme_display_name: UniProt P23457

organism: Rattus norvegicus

substrate_name: dihydrotestosterone

enzyme: UniProt P23457

substrate: dihydrotestosterone


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

organism: Gluconobacter oxydans

assay_conditions_summary: pH 7; 298.15 K; buffer 40 mM potassium phosphate

proof_lines: in 40 mM potassium phosphate buffer, at pH 7.0 and 25°C

proof_lines: kcat is 23 sec(-1). Can use NAD or NADP, but has a clear preference for NAD in vivo.


assay_conditions_summary: pH 7; 298.15 K; buffer 40 mM potassium phosphate; cofactor NAD+

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


enzyme_display_name: Isoeugenol synthase 1

organism: Petunia hybrida

substrate_name: coniferyl acetate (at pH 6.5 and 28 degrees Celsius)

proof_lines: kcat is 1.3 sec(-1) with coniferyl acetate as substrate.

enzyme: Isoeugenol synthase 1


substrate_name: NADPH (at pH 6.5 and 28 degrees Celsius)

assay_conditions_summary: pH 6.5; cofactor NADPH


enzyme_display_name: Aldo-keto reductase family 1 member B1

substrate_name: prostaglandin H2

proof_lines: kcat is 15 min(-1) for all-trans-retinal as substrate. kcat is 30 min(-1) for 9-cis-retinal as substrate. kcat is 94 min(-1) for 13-cis-retinal as substrate (PubMed:12732097). kcat is 11 min(-1) for acrolein as substrate. kcat is 31 min(-1)

enzyme: Aldo-keto reductase family 1 member B1

substrate: prostaglandin H2


enzyme_display_name: 3alpha-hydroxysteroid 3-dehydrogenase

source_db: oed

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

enzyme: 3alpha-hydroxysteroid 3-dehydrogenase

source: oed


substrate_name: D,L-glyceraldehyde

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

proof_lines: kcat is 640 min(-1) for glyceraldehyde as substrate (PubMed:12732097). kcat is 185 min(-1) for pyridine-3-aldehyde as substrate (PubMed:12732097). kcat is 116 min(-1) for acrolein as substrate. kcat is 103 min(-1) for 3-methyl-2-butenal as

substrate: D,L-glyceraldehyde


substrate_name: all-trans-retinal

substrate: all-trans-retinal


substrate_name: NADPH

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH


substrate_name: NADP+

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+


substrate_name: NADH

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH


substrate_name: NAD+

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

substrate: NAD+


organism: Comamonas testosteroni

substrate_name: Cyclohexanol

proof_lines: reombinant His-tagged enzyme, pH 10.5, 25°C

substrate: Cyclohexanol


substrate_name: androsterone

proof_lines: pH 8.9, temperature not specified in the publication, NAD(P)+

substrate: androsterone


substrate_name: Fusidic acid

proof_lines: pH 8.9, temperature not specified in the publication

substrate: Fusidic acid


assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication, NAD(P)H


substrate_name: cholic acid

substrate: cholic acid


substrate_name: androstandiol

substrate: androstandiol


substrate_name: Metyrapone

substrate: Metyrapone


substrate_name: metyrapol

substrate: metyrapol


substrate_name: Dehydrolithocholic acid

substrate: Dehydrolithocholic acid


substrate: NADPH


organism: Pseudomonas sp.


substrate_name: androstenol

assay_conditions_summary: pH 10.5; 298.15 K; cofactor NAD+

substrate: androstenol


proof_lines: reombinant His-tagged enzyme, pH 10.5, 25°C, with androstenol

proof_lines: reombinant His-tagged enzyme, pH 10.5, 25°C, with androsterone


enzyme_display_name: 5'-hydroxyaverantin dehydrogenase

organism: Levilactobacillus brevis

assay_conditions_summary: pH 7.5; 310.15 K; buffer 30 mM potassium phosphate

proof_lines: in 30 mM potassium phosphate buffer (pH 7.5), at 37°C

enzyme: 5'-hydroxyaverantin dehydrogenase


enzyme_display_name: Aldo-keto reductase family 1 member C2

organism: Homo sapiens

substrate_name: (s)-tetralol (oxidation)

proof_lines: kcat is 19.88 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:10998348). kcat is 1.98 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:19218247). kcat is 1.39 min(-1) for the reduction of

enzyme: Aldo-keto reductase family 1 member C2

substrate: (s)-tetralol (oxidation)


substrate_name: benzene dihydrodiol (oxidation)

substrate: benzene dihydrodiol (oxidation)


substrate_name: prostaglandin D2 (reduction)

substrate: prostaglandin D2 (reduction)


enzyme_display_name: Aldo-keto reductase family 1 member C1

substrate_name: (s)-tetralol

proof_lines: kcat is 0.29 min(-1) for the reduction of progesterone (PubMed:10998348). kcat is 1.1 min(-1) for the reduction of 3beta-hydroxy-5beta-pregnane-20-one (PubMed:10998348). kcat is 1.2 min(-1) for the oxidation of (20S)-hydroxypregn-4-en-3-one

enzyme: Aldo-keto reductase family 1 member C1

substrate: (s)-tetralol


substrate_name: dihydrotestosterone

substrate: dihydrotestosterone


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH


substrate_name: NADP(+)

substrate: NADP(+)


substrate_name: allopregnanolone (oxidation)

substrate: allopregnanolone (oxidation)


enzyme_display_name: Aldo-keto reductase family 1 member C4

organism: Macaca fuscata fuscata

proof_lines: kcat is 4.9 min(-1) for 5-beta-pregnan-20-alpha-ol-3-one as substrate. kcat is 4.9 min(-1) for 3alpha-hydroxy-5alpha-androstan-17-one as substrate. kcat is 23 min(-1) for 5alpha-pregnane-3alpha,21-diol-20-one.

enzyme: Aldo-keto reductase family 1 member C4


enzyme_display_name: Aldo-keto reductase family 1 member C3

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


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

organism: Thermoplasma acidophilum

substrate_name: beta-D-glucose

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

substrate: beta-D-glucose


organism: Saccharolobus solfataricus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T41V to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V

proof_lines: pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V


substrate_name: D-xylose

substrate: D-xylose


sequence_variant_note: Mutation signature T41A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A

proof_lines: pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A


substrate_name: D-galactose

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

proof_lines: pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme

proof_lines: pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme

substrate: D-galactose


substrate_name: androsterone

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature R1C with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

substrate: androsterone


assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 3 Kinetic parameters for 17-ketosteroid reduction and 17alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Androsterone reduction / AKR1C3; Km column raw 8.96 uM normalized 0.008960000000000001 mM

raw_value_unit_evidence: Km 8.96 uM

row_label: Androsterone reduction / AKR1C3


column_label: Table 2 Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-Androstane-3,17-dione reduction / AKR1C3; Km column raw 5.00 uM normalized 0.005 mM

raw_value_unit_evidence: Km 5.00 uM


substrate_name: testosterone (oxidation)

assay_conditions_summary: pH 7; cofactor NADP+

column_label: Table 3 Kinetic parameters for 17-ketosteroid reduction and 17alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Testosterone oxidation / AKR1C3 (R); Km column raw 24.3 uM normalized 0.024300000000000002 mM

raw_value_unit_evidence: Km 24.3 uM

row_label: Testosterone oxidation / AKR1C3 (R)

substrate: testosterone (oxidation)


column_label: Table 2 Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C2; Km column raw 22.0 uM normalized 0.022 mM

raw_value_unit_evidence: Km 22.0 uM


substrate_name: progesterone (reduction)

verification_status: corrected

column_label: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation row Progesterone reduction / AKR1C1; columns Km (uM), Vmax (nmol/min per mg), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation row Progesterone reduction / AKR1C1: Km 2.65 uM; Vmax 7.85 +/- 0.35; kcat 0.29 min^-1; kcat/Km 109 min^-1 mM^-1.

row_label: Progesterone reduction / AKR1C1

substrate: progesterone (reduction)

status: corrected


column_label: Table 4 Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3beta-Hydroxy-5beta-pregnan-20-one reduction / AKR1C1; Km column raw 16.2 uM normalized 0.0162 mM

raw_value_unit_evidence: Km 16.2 uM


column_label: Table 4 Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 20alpha-Hydroxyprogesterone oxidation / AKR1C1; Km column raw 14.7 uM normalized 0.0147 mM

raw_value_unit_evidence: Km 14.7 uM


column_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-DHT reduction / AKR1C1 (R); columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-DHT reduction / AKR1C1 (R): Km 80.6 uM; kcat 0.66 min^-1; kcat/Km 8 min^-1 mM^-1.

row_label: 5alpha-DHT reduction / AKR1C1 (R)


column_label: Table 3 Kinetic parameters for 17-ketosteroid reduction and 17alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Testosterone oxidation / AKR1C1 (R); Km column raw 39.8 uM normalized 0.039799999999999995 mM

raw_value_unit_evidence: Km 39.8 uM

row_label: Testosterone oxidation / AKR1C1 (R)


column_label: Table 4 Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 20alpha-Hydroxy-5beta-pregnan-3-one oxidation / AKR1C1; Km column raw 19.4 uM normalized 0.0194 mM

raw_value_unit_evidence: Km 19.4 uM


column_label: Table 2 Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C4; Km column raw 10.5 uM normalized 0.0105 mM

raw_value_unit_evidence: Km 10.5 uM


proof_lines: kcat is 1.99 min(-1) for 17beta-hydroxy-5alpha-androstan-3-one reduction. kcat is 1.79 min(-1) for 5alpha-androstan-3,17-dione reduction. kcat is 2.1 min(-1) for 5alpha-androstane-3alpha,17beta-diol oxydation. kcat is 1.39.1 min(-1) for 3al


column_label: Table 2 Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-Androstane-3,17-dione reduction / AKR1C4; Km column raw 1.44 uM normalized 0.0014399999999999999 mM

raw_value_unit_evidence: Km 1.44 uM


assay_conditions_summary: pH 6.5; 343.15 K; cofactor NADP+

proof_lines:
pH 6.5, 70°C, cosubstrate: NADP+
pH 7.5, 70°C, cofactor: NADP+
pH 6.5, 70°C, cosubstrate: NAD+

source_databases_merged: brenda skid


substrate_name: L-arabinose

proof_lines: pH 8.0, 70°C, native enzyme from xylose-grown cell extract

substrate: L-arabinose


substrate_name: (s)-indan-1-ol (oxidation)

substrate: (s)-indan-1-ol (oxidation)


enzyme_display_name: D-xylose reductase [NAD(P)H]

organism: Yamadazyma tenuis

proof_lines:
pH 7, 25°C
pH 6.0, 25°C, cosubstrate: NADH
pH 7, 25°C, cosubstrate: NADH

enzyme: D-xylose reductase [NAD(P)H]


organism: Pseudomonas sp. B-0831

substrate_name: cholic acid

proof_lines: recombinant His-tagged mutant S114A/Y153F, pH 8.0, 37°C

substrate: cholic acid


proof_lines: recombinant His-tagged mutant K157A, pH 8.0, 37°C


proof_lines: recombinant His-tagged mutant Y153F, pH 8.0, 37°C


proof_lines: recombinant His-tagged mutant S114A, pH 8.0, 37°C


substrate_name: Dehydrocholic acid

substrate: Dehydrocholic acid


proof_lines: recombinant His-tagged wild-type enzyme, pH 8.0, 37°C


proof_lines: kcat is 19.88 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:10998348). kcat is 1.98 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:19218247). kcat is 1.39 min(-1) for the reduction of


enzyme_display_name: isoeugenol synthase

substrate_name: coniferyl acetate

proof_lines: kcat is 0.99 sec(-1) with coniferyl acetate as substrate.

enzyme: isoeugenol synthase

substrate: coniferyl acetate


proof_lines: kcat is 0.60 sec(-1) with coniferyl acetate as substrate.


organism: Campylobacter jejuni

substrate_name: UDP-ManNAc

substrate: UDP-ManNAc


enzyme_display_name: 8-hydroxygeraniol dehydrogenase

organism: Nepeta racemosa

substrate_name: NADP+

assay_conditions_summary: pH 9.5; cofactor NADP+

column_label: Page 109 prose near Table II, NADP+ apparent Km: 18 uM.

raw_value_unit_evidence: Text reports apparent Km for NADP+ was 18 uM with 2.0 mM 10-hydroxynerol as substrate.

row_label: NADP+ with 10-hydroxynerol substrate

table_label: Page 109 prose near Table II

enzyme: 8-hydroxygeraniol dehydrogenase

substrate: NADP+


enzyme_display_name: perakine reductase

organism: Rauvolfia serpentina

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

enzyme: perakine reductase


organism: Streptomyces avermitilis

substrate_name: NAD+

assay_conditions_summary: pH 8; cofactor NAD+

substrate: NAD+


enzyme_display_name: 6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating

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

proof_lines: The catalytic efficiency with NAD(+) is about 2000-fold higher than with NADP(+), indicating that NAD(+) is the physiological electron acceptor.


organism: Gluconobacter oxydans (strain 621H)

proof_lines: kcat is 23 sec(-1). Can use NAD or NADP, but has a clear preference for NAD in vivo.

enzyme: 6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating


assay_conditions_summary: pH 9; 343.15 K; cofactor NADP+

proof_lines: pH 9.0, 70°C, cosubstrate: beta-D-glucose


assay_conditions_summary: pH 8; 343.15 K; cofactor NAD+


enzyme_display_name: versiconal hemiacetal acetate reductase

organism: Aspergillus parasiticus

substrate_name: versiconal hemiacetal acetate

assay_conditions_summary: pH 7.5; buffer 60 mM potassium phosphate

proof_lines: isoform VHA reductase II, in 60 mM potassium phosphate buffer (pH 7.5), at 37°C

proof_lines: isoform VHA reductase I, in 60 mM potassium phosphate buffer (pH 7.5), at 37°C

enzyme: versiconal hemiacetal acetate reductase

substrate: versiconal hemiacetal acetate


substrate_name: 5alpha-androstan-3,17-dione (reduction)

substrate: 5alpha-androstan-3,17-dione (reduction)


enzyme_display_name: NADPH-dependent D-xylose reductase

organism: Candida boidinii

substrate_name: NADPH

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

proof_lines: Mutations at positions 272 to 274 modify the cofactor specificity and increase specificity for NADH over NADPH.

enzyme: NADPH-dependent D-xylose reductase

substrate: NADPH


enzyme_display_name: GDP-L-colitose synthase

organism: Yersinia pseudotuberculosis

assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: Prose reports that with NADPH the Km for 9 is 75 +/- 15 uM and Vmax is 0.037 +/- 0.003 uM min^-1.

raw_value_unit_evidence: Km raw_value=75 +/- 15 raw_unit=uM

row_label: ColC reaction with GDP-4-keto-3,6-dideoxy-D-mannose (9) and NADPH

table_label: Kinetic Properties of ColD and ColC / Figure 3B/prose

enzyme: GDP-L-colitose synthase


column_label: Table 1, substrate row '5α-DHDOC (Red)', AKR1C4 column group: Km cell = 1.7, kcat cell = 2.1, kcat/Km cell = 1.2. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 2.1 min^-1 normalizes to 0.035 s^-1 (divide by 60); Km raw 1.7 uM normalizes to 0.0017 mM (divide by 1000); kcat/Km = 0.035 s^-1 / 0.0017 mM = 20.58823529411765 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 1.2 min^-1 uM^-1 normalizes to 20.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5α-DHDOC (Red)'; AKR1C4 column group; Km cell = 1.7 uM; kcat cell = 2.1 min^-1; printed kcat/Km cell = 1.2 min^-1 uM^-1.

row_label: 5α-DHDOC (Red) | AKR1C4 column group

table_label: Table 1. Comparison of kinetic constants for substrate pairs in the reduction and oxidation catalyzed by human AKR1C isoenzymes


column_label: Table 1, substrate row '5α-DHDOC (Red)', AKR1C2 column group: Km cell = 0.8, kcat cell = 0.49, kcat/Km cell = 0.61. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.49 min^-1 normalizes to 0.008166666666666666 s^-1 (divide by 60); Km raw 0.8 uM normalizes to 0.0008 mM (divide by 1000); kcat/Km = 0.008166666666666666 s^-1 / 0.0008 mM = 10.208333333333334 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.61 min^-1 uM^-1 normalizes to 10.166666666666666 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5α-DHDOC (Red)'; AKR1C2 column group; Km cell = 0.8 uM; kcat cell = 0.49 min^-1; printed kcat/Km cell = 0.61 min^-1 uM^-1.

row_label: 5α-DHDOC (Red) | AKR1C2 column group


column_label: Table 1, substrate row '5α-DHDOC (Red)', AKR1C1 column group: Km cell = 1.2, kcat cell = 0.56, kcat/Km cell = 0.42. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.56 min^-1 normalizes to 0.009333333333333334 s^-1 (divide by 60); Km raw 1.2 uM normalizes to 0.0012 mM (divide by 1000); kcat/Km = 0.009333333333333334 s^-1 / 0.0012 mM = 7.777777777777778 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.42 min^-1 uM^-1 normalizes to 7.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5α-DHDOC (Red)'; AKR1C1 column group; Km cell = 1.2 uM; kcat cell = 0.56 min^-1; printed kcat/Km cell = 0.42 min^-1 uM^-1.

row_label: 5α-DHDOC (Red) | AKR1C1 column group


substrate_name: Pregnanediol

column_label: Table 1, substrate row '5β-Pregnane-3α,20α-diol (Oxi)', AKR1C4 column group: Km cell = 0.2, kcat cell = 1.2, kcat/Km cell = 6.0. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 1.2 min^-1 normalizes to 0.02 s^-1 (divide by 60); Km raw 0.2 uM normalizes to 0.0002 mM (divide by 1000); kcat/Km = 0.02 s^-1 / 0.0002 mM = 100.0 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 6.0 min^-1 uM^-1 normalizes to 100.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnane-3α,20α-diol (Oxi)'; AKR1C4 column group; Km cell = 0.2 uM; kcat cell = 1.2 min^-1; printed kcat/Km cell = 6.0 min^-1 uM^-1.

row_label: 5β-Pregnane-3α,20α-diol (Oxi) | AKR1C4 column group

substrate: Pregnanediol


column_label: Table 1, substrate row '5β-Pregnane-3α,20α-diol (Oxi)', AKR1C3 column group: Km cell = 27, kcat cell = 1.7, kcat/Km cell = 0.06. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 1.7 min^-1 normalizes to 0.028333333333333332 s^-1 (divide by 60); Km raw 27 uM normalizes to 0.027 mM (divide by 1000); kcat/Km = 0.028333333333333332 s^-1 / 0.027 mM = 1.0493827160493827 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.06 min^-1 uM^-1 normalizes to 1.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnane-3α,20α-diol (Oxi)'; AKR1C3 column group; Km cell = 27 uM; kcat cell = 1.7 min^-1; printed kcat/Km cell = 0.06 min^-1 uM^-1.

row_label: 5β-Pregnane-3α,20α-diol (Oxi) | AKR1C3 column group


column_label: Table 1, substrate row '5β-Pregnane-3α,20α-diol (Oxi)', AKR1C2 column group: Km cell = 1.0, kcat cell = 0.22, kcat/Km cell = 0.22. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.22 min^-1 normalizes to 0.0036666666666666666 s^-1 (divide by 60); Km raw 1.0 uM normalizes to 0.001 mM (divide by 1000); kcat/Km = 0.0036666666666666666 s^-1 / 0.001 mM = 3.6666666666666665 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.22 min^-1 uM^-1 normalizes to 3.6666666666666665 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnane-3α,20α-diol (Oxi)'; AKR1C2 column group; Km cell = 1.0 uM; kcat cell = 0.22 min^-1; printed kcat/Km cell = 0.22 min^-1 uM^-1.

row_label: 5β-Pregnane-3α,20α-diol (Oxi) | AKR1C2 column group


column_label: Table 1, substrate row '5β-Pregnane-3α,20α-diol (Oxi)', AKR1C1 column group: Km cell = 1.5, kcat cell = 9.6, kcat/Km cell = 6.4. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 9.6 min^-1 normalizes to 0.16 s^-1 (divide by 60); Km raw 1.5 uM normalizes to 0.0015 mM (divide by 1000); kcat/Km = 0.16 s^-1 / 0.0015 mM = 106.66666666666667 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 6.4 min^-1 uM^-1 normalizes to 106.66666666666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnane-3α,20α-diol (Oxi)'; AKR1C1 column group; Km cell = 1.5 uM; kcat cell = 9.6 min^-1; printed kcat/Km cell = 6.4 min^-1 uM^-1.

row_label: 5β-Pregnane-3α,20α-diol (Oxi) | AKR1C1 column group


column_label: Table 1, substrate row '5α-Pregnan-20α-ol-3-one (Red)', AKR1C4 column group: Km cell = 1.1, kcat cell = 1.3, kcat/Km cell = 1.2. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 1.3 min^-1 normalizes to 0.021666666666666667 s^-1 (divide by 60); Km raw 1.1 uM normalizes to 0.0011 mM (divide by 1000); kcat/Km = 0.021666666666666667 s^-1 / 0.0011 mM = 19.696969696969695 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 1.2 min^-1 uM^-1 normalizes to 20.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5α-Pregnan-20α-ol-3-one (Red)'; AKR1C4 column group; Km cell = 1.1 uM; kcat cell = 1.3 min^-1; printed kcat/Km cell = 1.2 min^-1 uM^-1.

row_label: 5α-Pregnan-20α-ol-3-one (Red) | AKR1C4 column group


column_label: Table 1, substrate row '5α-Pregnan-20α-ol-3-one (Red)', AKR1C3 column group: Km cell = 2.1, kcat cell = 0.52, kcat/Km cell = 0.25. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.52 min^-1 normalizes to 0.008666666666666666 s^-1 (divide by 60); Km raw 2.1 uM normalizes to 0.0021 mM (divide by 1000); kcat/Km = 0.008666666666666666 s^-1 / 0.0021 mM = 4.126984126984127 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.25 min^-1 uM^-1 normalizes to 4.166666666666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5α-Pregnan-20α-ol-3-one (Red)'; AKR1C3 column group; Km cell = 2.1 uM; kcat cell = 0.52 min^-1; printed kcat/Km cell = 0.25 min^-1 uM^-1.

row_label: 5α-Pregnan-20α-ol-3-one (Red) | AKR1C3 column group


column_label: Table 1, substrate row '5α-Pregnan-20α-ol-3-one (Red)', AKR1C2 column group: Km cell = 0.5, kcat cell = 0.48, kcat/Km cell = 0.96. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.48 min^-1 normalizes to 0.008 s^-1 (divide by 60); Km raw 0.5 uM normalizes to 0.0005 mM (divide by 1000); kcat/Km = 0.008 s^-1 / 0.0005 mM = 16.0 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.96 min^-1 uM^-1 normalizes to 16.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5α-Pregnan-20α-ol-3-one (Red)'; AKR1C2 column group; Km cell = 0.5 uM; kcat cell = 0.48 min^-1; printed kcat/Km cell = 0.96 min^-1 uM^-1.

row_label: 5α-Pregnan-20α-ol-3-one (Red) | AKR1C2 column group


column_label: Table 1, substrate row '5α-Pregnan-20α-ol-3-one (Red)', AKR1C1 column group: Km cell = 0.7, kcat cell = 0.6, kcat/Km cell = 0.86. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.6 min^-1 normalizes to 0.01 s^-1 (divide by 60); Km raw 0.7 uM normalizes to 0.0007 mM (divide by 1000); kcat/Km = 0.01 s^-1 / 0.0007 mM = 14.285714285714286 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.86 min^-1 uM^-1 normalizes to 14.333333333333334 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '5α-Pregnan-20α-ol-3-one (Red)'; AKR1C1 column group; Km cell = 0.7 uM; kcat cell = 0.6 min^-1; printed kcat/Km cell = 0.86 min^-1 uM^-1.

row_label: 5α-Pregnan-20α-ol-3-one (Red) | AKR1C1 column group


column_label: Table 1, substrate row '5β-Pregnan-20α-ol-3-one (Red)', AKR1C4 column group: Km cell = 1.5, kcat cell = 1.4, kcat/Km cell = 0.93. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 1.4 min^-1 normalizes to 0.02333333333333333 s^-1 (divide by 60); Km raw 1.5 uM normalizes to 0.0015 mM (divide by 1000); kcat/Km = 0.02333333333333333 s^-1 / 0.0015 mM = 15.555555555555554 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.93 min^-1 uM^-1 normalizes to 15.5 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnan-20α-ol-3-one (Red)'; AKR1C4 column group; Km cell = 1.5 uM; kcat cell = 1.4 min^-1; printed kcat/Km cell = 0.93 min^-1 uM^-1.

row_label: 5β-Pregnan-20α-ol-3-one (Red) | AKR1C4 column group


column_label: Table 1, substrate row '5β-Pregnan-20α-ol-3-one (Red)', AKR1C3 column group: Km cell = 0.9, kcat cell = 1.1, kcat/Km cell = 1.2. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 1.1 min^-1 normalizes to 0.018333333333333333 s^-1 (divide by 60); Km raw 0.9 uM normalizes to 0.0009 mM (divide by 1000); kcat/Km = 0.018333333333333333 s^-1 / 0.0009 mM = 20.37037037037037 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 1.2 min^-1 uM^-1 normalizes to 20.0 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnan-20α-ol-3-one (Red)'; AKR1C3 column group; Km cell = 0.9 uM; kcat cell = 1.1 min^-1; printed kcat/Km cell = 1.2 min^-1 uM^-1.

row_label: 5β-Pregnan-20α-ol-3-one (Red) | AKR1C3 column group


column_label: Table 1, substrate row '5β-Pregnan-20α-ol-3-one (Red)', AKR1C2 column group: Km cell = 0.3, kcat cell = 0.65, kcat/Km cell = 2.2. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.65 min^-1 normalizes to 0.010833333333333334 s^-1 (divide by 60); Km raw 0.3 uM normalizes to 0.0003 mM (divide by 1000); kcat/Km = 0.010833333333333334 s^-1 / 0.0003 mM = 36.111111111111114 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 2.2 min^-1 uM^-1 normalizes to 36.666666666666664 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnan-20α-ol-3-one (Red)'; AKR1C2 column group; Km cell = 0.3 uM; kcat cell = 0.65 min^-1; printed kcat/Km cell = 2.2 min^-1 uM^-1.

row_label: 5β-Pregnan-20α-ol-3-one (Red) | AKR1C2 column group


column_label: Table 1, substrate row '5β-Pregnan-20α-ol-3-one (Red)', AKR1C1 column group: Km cell = 1.3, kcat cell = 2.2, kcat/Km cell = 1.7. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 2.2 min^-1 normalizes to 0.03666666666666667 s^-1 (divide by 60); Km raw 1.3 uM normalizes to 0.0013 mM (divide by 1000); kcat/Km = 0.03666666666666667 s^-1 / 0.0013 mM = 28.205128205128208 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 1.7 min^-1 uM^-1 normalizes to 28.333333333333332 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnan-20α-ol-3-one (Red)'; AKR1C1 column group; Km cell = 1.3 uM; kcat cell = 2.2 min^-1; printed kcat/Km cell = 1.7 min^-1 uM^-1.

row_label: 5β-Pregnan-20α-ol-3-one (Red) | AKR1C1 column group


column_label: Table 1, substrate row '3α,5α-THP (Oxi)', AKR1C4 column group: Km cell = 0.2, kcat cell = 4.0, kcat/Km cell = 20. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 4.0 min^-1 normalizes to 0.06666666666666667 s^-1 (divide by 60); Km raw 0.2 uM normalizes to 0.0002 mM (divide by 1000); kcat/Km = 0.06666666666666667 s^-1 / 0.0002 mM = 333.3333333333333 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 20 min^-1 uM^-1 normalizes to 333.3333333333333 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '3α,5α-THP (Oxi)'; AKR1C4 column group; Km cell = 0.2 uM; kcat cell = 4.0 min^-1; printed kcat/Km cell = 20 min^-1 uM^-1.

row_label: 3α,5α-THP (Oxi) | AKR1C4 column group


column_label: Table 1, substrate row '3α,5α-THP (Oxi)', AKR1C2 column group: Km cell = 28, kcat cell = 0.28, kcat/Km cell = 0.01. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.28 min^-1 normalizes to 0.004666666666666667 s^-1 (divide by 60); Km raw 28 uM normalizes to 0.028 mM (divide by 1000); kcat/Km = 0.004666666666666667 s^-1 / 0.028 mM = 0.16666666666666669 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.01 min^-1 uM^-1 normalizes to 0.16666666666666666 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '3α,5α-THP (Oxi)'; AKR1C2 column group; Km cell = 28 uM; kcat cell = 0.28 min^-1; printed kcat/Km cell = 0.01 min^-1 uM^-1.

row_label: 3α,5α-THP (Oxi) | AKR1C2 column group


organism: Sungouiella intermedia

substrate_name: D-xylose

proof_lines:
cosubstrate NADPH, pH 7, 25°C
pH 7, 25°C
cosubstrate NADH, pH 7, 25°C

substrate: D-xylose


substrate_name: prostaglandin H2

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

substrate: prostaglandin H2


enzyme_display_name: Dehydrogenase/reductase SDR family member 4

organism: Oryctolagus cuniculus

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

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

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


organism: Homo sapiens


enzyme_display_name: diacetyl reductase [(S)-acetoin forming]

organism: Staphylococcus aureus

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


enzyme_display_name: 3alpha-hydroxysteroid 3-dehydrogenase

column_label: Table 1, substrate row '3α,5α-THP (Oxi)', AKR1C1 column group: Km cell = 3.3, kcat cell = 0.08, kcat/Km cell = 0.02. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.08 min^-1 normalizes to 0.0013333333333333333 s^-1 (divide by 60); Km raw 3.3 uM normalizes to 0.0033 mM (divide by 1000); kcat/Km = 0.0013333333333333333 s^-1 / 0.0033 mM = 0.40404040404040403 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.02 min^-1 uM^-1 normalizes to 0.3333333333333333 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '3α,5α-THP (Oxi)'; AKR1C1 column group; Km cell = 3.3 uM; kcat cell = 0.08 min^-1; printed kcat/Km cell = 0.02 min^-1 uM^-1.

row_label: 3α,5α-THP (Oxi) | AKR1C1 column group


assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

column_label: Table 1, substrate row '3α,5β-THP (Oxi)', AKR1C4 column group: Km cell = 0.4, kcat cell = 1.6, kcat/Km cell = 4.0. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 1.6 min^-1 normalizes to 0.02666666666666667 s^-1 (divide by 60); Km raw 0.4 uM normalizes to 0.0004 mM (divide by 1000); kcat/Km = 0.02666666666666667 s^-1 / 0.0004 mM = 66.66666666666667 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 4.0 min^-1 uM^-1 normalizes to 66.66666666666667 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '3α,5β-THP (Oxi)'; AKR1C4 column group; Km cell = 0.4 uM; kcat cell = 1.6 min^-1; printed kcat/Km cell = 4.0 min^-1 uM^-1.

row_label: 3α,5β-THP (Oxi) | AKR1C4 column group


column_label: Table 1, substrate row '3α,5β-THP (Oxi)', AKR1C2 column group: Km cell = 2.8, kcat cell = 0.27, kcat/Km cell = 0.10. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.27 min^-1 normalizes to 0.0045000000000000005 s^-1 (divide by 60); Km raw 2.8 uM normalizes to 0.0028 mM (divide by 1000); kcat/Km = 0.0045000000000000005 s^-1 / 0.0028 mM = 1.6071428571428574 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.10 min^-1 uM^-1 normalizes to 1.6666666666666667 s^-1 mM^-1 (multiply by 1000/60).

raw_value_unit_evidence: Table 1; substrate row '3α,5β-THP (Oxi)'; AKR1C2 column group; Km cell = 2.8 uM; kcat cell = 0.27 min^-1; printed kcat/Km cell = 0.10 min^-1 uM^-1.

row_label: 3α,5β-THP (Oxi) | AKR1C2 column group


column_label: Exact Table 1 row 3α,5β-THP (Oxi), AKR1C1 column group: same-row cells 4.5, 0.36, 0.08; captured segment is preserved verbatim.

normalized_value_unit_evidence: Primary cells normalize exactly to Km 0.0045 mM and kcat 0.006 s^-1; current stored precision is 0.005 mM and 0.006 s^-1, whose quotient is 1.2; printed efficiency normalizes to 1.3333333333333333.

raw_value_unit_evidence: Table 1 row 3α,5β-THP (Oxi), AKR1C1: Km 4.5 µM, kcat 0.36 min^-1, printed kcat/Km 0.08 min^-1 µM^-1.

row_label: 3α,5β-THP (Oxi) | AKR1C1 column group


column_label: Exact Table 1 row 5α-Pregnane-3α,20α-diol (Oxi), AKR1C4 column group: same-row cells 0.2, 4.0, 20; captured segment is preserved verbatim.

normalized_value_unit_evidence: Primary cells normalize exactly to Km 0.0002 mM and kcat 0.06666666666666667 s^-1; current stored precision is 0.0002 mM and 0.067 s^-1, whose quotient is 335.0; printed efficiency normalizes to 333.3333333333333.

raw_value_unit_evidence: Table 1 row 5α-Pregnane-3α,20α-diol (Oxi), AKR1C4: Km 0.2 µM, kcat 4.0 min^-1, printed kcat/Km 20 min^-1 µM^-1.

row_label: 5α-Pregnane-3α,20α-diol (Oxi) | AKR1C4 column group


column_label: Exact Table 1 row 5α-Pregnane-3α,20α-diol (Oxi), AKR1C2 column group: same-row cells 1.8, 0.19, 0.11; captured segment is preserved verbatim.

normalized_value_unit_evidence: Primary cells normalize exactly to Km 0.0018 mM and kcat 0.0031666666666666666 s^-1; current stored precision is 0.002 mM and 0.003 s^-1, whose quotient is 1.5; printed efficiency normalizes to 1.8333333333333333.

raw_value_unit_evidence: Table 1 row 5α-Pregnane-3α,20α-diol (Oxi), AKR1C2: Km 1.8 µM, kcat 0.19 min^-1, printed kcat/Km 0.11 min^-1 µM^-1.

row_label: 5α-Pregnane-3α,20α-diol (Oxi) | AKR1C2 column group


column_label: Exact Table 1 row 5α-Pregnane-3α,20α-diol (Oxi), AKR1C1 column group: same-row cells 0.9, 2.2, 2.4; captured segment is preserved verbatim.

normalized_value_unit_evidence: Primary cells normalize exactly to Km 0.0009 mM and kcat 0.03666666666666667 s^-1; current stored precision is 0.0009 mM and 0.037 s^-1, whose quotient is 41.11111111111111; printed efficiency normalizes to 40.0.

raw_value_unit_evidence: Table 1 row 5α-Pregnane-3α,20α-diol (Oxi), AKR1C1: Km 0.9 µM, kcat 2.2 min^-1, printed kcat/Km 2.4 min^-1 µM^-1.

row_label: 5α-Pregnane-3α,20α-diol (Oxi) | AKR1C1 column group


column_label: Exact Table 1 row 3α,5α-THDOC (Oxi), AKR1C4 column group: same-row cells 0.3, 4.2, 14; captured segment is preserved verbatim.

normalized_value_unit_evidence: Primary cells normalize exactly to Km 0.0003 mM and kcat 0.07 s^-1; current stored values are identical and their quotient is 233.33333333333337; printed efficiency normalizes to 233.33333333333334.

raw_value_unit_evidence: Table 1 row 3α,5α-THDOC (Oxi), AKR1C4: Km 0.3 µM, kcat 4.2 min^-1, printed kcat/Km 14 min^-1 µM^-1.

row_label: 3α,5α-THDOC (Oxi) | AKR1C4 column group


column_label: Exact Table 1 row 3α,5α-THDOC (Oxi), AKR1C2 column group: same-row cells 6.8, 0.13, 0.02; captured segment is preserved verbatim.

normalized_value_unit_evidence: Primary cells normalize exactly to Km 0.0068 mM and kcat 0.0021666666666666666 s^-1; current stored precision is 0.007 mM and 0.002 s^-1, whose quotient is 0.2857142857142857; printed efficiency normalizes to 0.3333333333333333.

raw_value_unit_evidence: Table 1 row 3α,5α-THDOC (Oxi), AKR1C2: Km 6.8 µM, kcat 0.13 min^-1, printed kcat/Km 0.02 min^-1 µM^-1.

row_label: 3α,5α-THDOC (Oxi) | AKR1C2 column group


column_label: Exact Table 1 row 3α,5α-THDOC (Oxi), AKR1C1 column group: same-row cells 2.6, 0.22, 0.08; captured segment is preserved verbatim.

normalized_value_unit_evidence: Primary cells normalize exactly to Km 0.0026 mM and kcat 0.003666666666666667 s^-1; current stored precision is 0.003 mM and 0.004 s^-1, whose quotient is 1.3333333333333333 s^-1 mM^-1; printed efficiency normalizes to 1.3333333333333333.

raw_value_unit_evidence: Table 1 row 3α,5α-THDOC (Oxi), AKR1C1: Km 2.6 µM, kcat 0.22 min^-1, printed kcat/Km 0.08 min^-1 µM^-1.

row_label: 3α,5α-THDOC (Oxi) | AKR1C1 column group


enzyme_display_name: zerumbone synthase

organism: Zingiber zerumbet

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S142A to reconstruct the assayed variant sequence.

enzyme: zerumbone synthase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S144A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y155A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+


proof_lines:
Table 1
wild-type ZSD1
NAD+


proof_lines:
Table 1
Y155A
NAD+


organism: [Candida] intermedia

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

column_label: Table label: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR. Row: 5,6-Difluoro (4). Enzyme column group: Candida intermedia II. Columns read: kcat (s−1) cell 12, K ROm (mM) cell 4.5, kcat/K ROm (M−1:s−1) cell 2667. captured primary segment: 5,6-Difluoro (4) 18p1.9 1.4p0.6 12 857 (1.1) 15.9 (0.1) 12p1 4.5p1.4 2667 (1.7) 17.1 (1.3). metric: kcat; raw value: 12; raw unit: s^-1; normalized value: 12.0 s^(-1); metric: Km; raw value: 4.5; raw unit: mM; normalized value: 4.5 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 2.6666666666666665 s^-1 mM^-1; assay condition: Table 4 assay: the concentration of NADH was 220 uM and saturating. Reaction conditions: 50 mM potassium phosphate buffer, pH 7.0, 25 C. Enzyme: the NADH-linked aldose reductase of Candida intermedia, printed in the table as Candida intermedia II. Export row conditions: pH 7; 298.15 K.

normalized_value_unit_evidence: Candida intermedia II columns of Table 4 row 5,6-Difluoro (4): kcat 12 s^-1 = 12.0 s^(-1) (no conversion, the paper already prints s^-1); Km 4.5 mM = 4.5 mM (no conversion, the paper already prints mM); kcat/Km 2.6666666666666665 s^-1 mM^-1, the same-row quotient 12 s^-1 / 4.5 mM (1 M^-1 s^-1 = 0.001 s^-1 mM^-1, so the table's printed cell 2667 M^-1:s^-1 is 2667 / 1000 = 2.667 s^-1 mM^-1, the same quotient carried to the printed cell's own four-figure precision). Rendering quirks of the pdftotext extract: the printed plus-minus sign is flattened to `p`, the printed minus sign of a negative number to `k`, superscript -1 to the character '−1', the micro sign to 'µ', the degree sign of '25 °C' to 'm', the centred dot of M^-1.s^-1 to ':', and the small capital D of the sugar names is dropped, so the cell text `5,6-Difluoro (4) 18p1.9 1.4p0.6 12 857 (` is the paper's own printed row.

raw_value_unit_evidence: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR | column group header row: Candida tenuis Candida intermedia II | metric header row: Substrate kcat (s−1) K ROm (mM) kcat/K ROm k ∆∆G (kJ/mol) kcat (s−1) K ROm (mM) kcat/K ROm (M−1:s−1) k∆∆G (kJ/mol) | data row: 5,6-Difluoro (4) 18p1.9 1.4p0.6 12 857 (1.1) 15.9 (0.1) 12p1 4.5p1.4 2667 (1.7) 17.1 (1.3) | Candida intermedia II cells read: kcat = 12 s^-1 (printed with its standard deviation as p in the pdftotext extract); K ROm = 4.5 mM; kcat/K ROm = 2667 M^-1:s^-1.

row_label: Candida intermedia II | 5,6-Difluoro (4)


column_label: Table label: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR. Row: 6-Deoxy-5-fluoro (6). Enzyme column group: Candida intermedia II. Columns read: kcat (s−1) cell 13, K ROm (mM) cell 8.9, kcat/K ROm (M−1:s−1) cell 1461. captured primary segment: 6-Deoxy-5-fluoro (6) 18p0.5 1.2p0.2 15 000 (1.2) 16.3 (0.5) 13p1 8.9p2.2 1461 (0.9) 15.6 (k0.2). metric: kcat; raw value: 13; raw unit: s^-1; normalized value: 13.0 s^(-1); metric: Km; raw value: 8.9; raw unit: mM; normalized value: 8.9 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 1.4606741573033708 s^-1 mM^-1; assay condition: Table 4 assay: the concentration of NADH was 220 uM and saturating. Reaction conditions: 50 mM potassium phosphate buffer, pH 7.0, 25 C. Enzyme: the NADH-linked aldose reductase of Candida intermedia, printed in the table as Candida intermedia II. Export row conditions: pH 7; 298.15 K.

normalized_value_unit_evidence: Candida intermedia II columns of Table 4 row 6-Deoxy-5-fluoro (6): kcat 13 s^-1 = 13.0 s^(-1) (no conversion, the paper already prints s^-1); Km 8.9 mM = 8.9 mM (no conversion, the paper already prints mM); kcat/Km 1.4606741573033708 s^-1 mM^-1, the same-row quotient 13 s^-1 / 8.9 mM (1 M^-1 s^-1 = 0.001 s^-1 mM^-1, so the table's printed cell 1461 M^-1:s^-1 is 1461 / 1000 = 1.461 s^-1 mM^-1, the same quotient carried to the printed cell's own four-figure precision). Rendering quirks of the pdftotext extract: the printed plus-minus sign is flattened to `p`, the printed minus sign of a negative number to `k`, superscript -1 to the character '−1', the micro sign to 'µ', the degree sign of '25 °C' to 'm', the centred dot of M^-1.s^-1 to ':', and the small capital D of the sugar names is dropped, so the cell text `6-Deoxy-5-fluoro (6) 18p0.5 1.2p0.2 15 0` is the paper's own printed row.

raw_value_unit_evidence: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR | column group header row: Candida tenuis Candida intermedia II | metric header row: Substrate kcat (s−1) K ROm (mM) kcat/K ROm k ∆∆G (kJ/mol) kcat (s−1) K ROm (mM) kcat/K ROm (M−1:s−1) k∆∆G (kJ/mol) | data row: 6-Deoxy-5-fluoro (6) 18p0.5 1.2p0.2 15 000 (1.2) 16.3 (0.5) 13p1 8.9p2.2 1461 (0.9) 15.6 (k0.2) | Candida intermedia II cells read: kcat = 13 s^-1 (printed with its standard deviation as p in the pdftotext extract); K ROm = 8.9 mM; kcat/K ROm = 1461 M^-1:s^-1.

row_label: Candida intermedia II | 6-Deoxy-5-fluoro (6)


column_label: Table label: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR. Row: 5-Deoxy-6-fluoro (7). Enzyme column group: Candida intermedia II. Columns read: kcat (s−1) cell 21, K ROm (mM) cell 14.7, kcat/K ROm (M−1:s−1) cell 1428. captured primary segment: 5-Deoxy-6-fluoro (7) 18p2.8 2.6p1.3 6 923 (0.6) 14.4 (k1.4) 21p5 14.7p7.0 1428 (0.9) 15.5 (k0.2). metric: kcat; raw value: 21; raw unit: s^-1; normalized value: 21.0 s^(-1); metric: Km; raw value: 14.7; raw unit: mM; normalized value: 14.7 mM; metric: kcat/Km; raw value: 1428; raw unit: M^-1:s^-1; normalized value: 1.428 s^-1 mM^-1; primary_cell: true; independently_reported: true; assay condition: Table 4 assay: the concentration of NADH was 220 uM and saturating. Reaction conditions: 50 mM potassium phosphate buffer, pH 7.0, 25 C. Enzyme: the NADH-linked aldose reductase of Candida intermedia, printed in the table as Candida intermedia II. Export row conditions: pH 7; 298.15 K.

normalized_value_unit_evidence: Candida intermedia II columns of Table 4 row 5-Deoxy-6-fluoro (7): kcat 21 s^-1 = 21.0 s^(-1) (no conversion, the paper already prints s^-1); Km 14.7 mM = 14.7 mM (no conversion, the paper already prints mM); kcat/Km primary printed kcat/Km cell 1428 M^-1:s^-1; direct unit conversion by division by 1000 gives 1.428 s^-1 mM^-1. Rendering quirks of the pdftotext extract: the printed plus-minus sign is flattened to `p`, the printed minus sign of a negative number to `k`, superscript -1 to the character '−1', the micro sign to 'µ', the degree sign of '25 °C' to 'm', the centred dot of M^-1.s^-1 to ':', and the small capital D of the sugar names is dropped, so the cell text `5-Deoxy-6-fluoro (7) 18p2.8 2.6p1.3 6 92` is the paper's own printed row.

raw_value_unit_evidence: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR | column group header row: Candida tenuis Candida intermedia II | metric header row: Substrate kcat (s−1) K ROm (mM) kcat/K ROm k ∆∆G (kJ/mol) kcat (s−1) K ROm (mM) kcat/K ROm (M−1:s−1) k∆∆G (kJ/mol) | data row: 5-Deoxy-6-fluoro (7) 18p2.8 2.6p1.3 6 923 (0.6) 14.4 (k1.4) 21p5 14.7p7.0 1428 (0.9) 15.5 (k0.2) | Candida intermedia II cells read: kcat = 21 s^-1 (printed with its standard deviation as p in the pdftotext extract); K ROm = 14.7 mM; kcat/K ROm = 1428 M^-1:s^-1.

row_label: Candida intermedia II | 5-Deoxy-6-fluoro (7)


column_label: Table label: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR. Row: 5,6-Dideoxy (8). Enzyme column group: Candida intermedia II. Columns read: kcat (s−1) cell 14, K ROm (mM) cell 1.7, kcat/K ROm (M−1:s−1) cell 8235. captured primary segment: 5,6-Dideoxy (8) 18p1.3 0.5p0.3 36 000 (3.0) 18.5 (2.7) 14p1 1.7p0.5 8235 (5.3) 19.9 (4.1). metric: kcat; raw value: 14; raw unit: s^-1; normalized value: 14.0 s^(-1); metric: Km; raw value: 1.7; raw unit: mM; normalized value: 1.7 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 8.23529411764706 s^-1 mM^-1; assay condition: Table 4 assay: the concentration of NADH was 220 uM and saturating. Reaction conditions: 50 mM potassium phosphate buffer, pH 7.0, 25 C. Enzyme: the NADH-linked aldose reductase of Candida intermedia, printed in the table as Candida intermedia II. Export row conditions: pH 7; 298.15 K.

normalized_value_unit_evidence: Candida intermedia II columns of Table 4 row 5,6-Dideoxy (8): kcat 14 s^-1 = 14.0 s^(-1) (no conversion, the paper already prints s^-1); Km 1.7 mM = 1.7 mM (no conversion, the paper already prints mM); kcat/Km 8.23529411764706 s^-1 mM^-1, the same-row quotient 14 s^-1 / 1.7 mM (1 M^-1 s^-1 = 0.001 s^-1 mM^-1, so the table's printed cell 8235 M^-1:s^-1 is 8235 / 1000 = 8.235 s^-1 mM^-1, the same quotient carried to the printed cell's own four-figure precision). Rendering quirks of the pdftotext extract: the printed plus-minus sign is flattened to `p`, the printed minus sign of a negative number to `k`, superscript -1 to the character '−1', the micro sign to 'µ', the degree sign of '25 °C' to 'm', the centred dot of M^-1.s^-1 to ':', and the small capital D of the sugar names is dropped, so the cell text `5,6-Dideoxy (8) 18p1.3 0.5p0.3 36 000 (3` is the paper's own printed row.

raw_value_unit_evidence: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR | column group header row: Candida tenuis Candida intermedia II | metric header row: Substrate kcat (s−1) K ROm (mM) kcat/K ROm k ∆∆G (kJ/mol) kcat (s−1) K ROm (mM) kcat/K ROm (M−1:s−1) k∆∆G (kJ/mol) | data row: 5,6-Dideoxy (8) 18p1.3 0.5p0.3 36 000 (3.0) 18.5 (2.7) 14p1 1.7p0.5 8235 (5.3) 19.9 (4.1) | Candida intermedia II cells read: kcat = 14 s^-1 (printed with its standard deviation as p in the pdftotext extract); K ROm = 1.7 mM; kcat/K ROm = 8235 M^-1:s^-1.

row_label: Candida intermedia II | 5,6-Dideoxy (8)


column_label: Table label: Table 2     Kinetic parameters for NADH-dependent reduction of xylose derivatives by yALR. Row: 5-Deoxy (1). Enzyme column group: Candida intermedia II. Columns read: kcat (s−1) cell 13.5, K ROm (mM) cell 1.3, kcat/K ROm (M−1:s−1) cell 10 384. captured primary segment: 5-Deoxy (1) 18p1 0.9p0.3 (1.0) 20 000 (1.2) 11.2 (0.5) 13.5p0.6 1.3p0.3 (2.0) 10 384 (0.7) 9.7 (k1.0). metric: kcat; raw value: 13.5; raw unit: s^-1; normalized value: 13.5 s^(-1); metric: Km; raw value: 1.3; raw unit: mM; normalized value: 1.3 mM; metric: kcat/Km; raw value: 10 384; raw unit: M^-1:s^-1; normalized value: 10.384 s^-1 mM^-1; primary_cell: true; independently_reported: true; assay condition: Table 2 assay: the concentration of NADH was 220 uM and saturating. Reaction conditions: 50 mM potassium phosphate buffer, pH 7.0, 25 C. Enzyme: the NADH-linked aldose reductase of Candida intermedia, printed in the table as Candida intermedia II. Export row conditions: pH 7; 298.15 K.

normalized_value_unit_evidence: Candida intermedia II columns of Table 2 row 5-Deoxy (1): kcat 13.5 s^-1 = 13.5 s^(-1) (no conversion, the paper already prints s^-1); Km 1.3 mM = 1.3 mM (no conversion, the paper already prints mM); kcat/Km primary printed kcat/Km cell 10 384 M^-1:s^-1; direct unit conversion by division by 1000 gives 10.384 s^-1 mM^-1. Rendering quirks of the pdftotext extract: the printed plus-minus sign is flattened to `p`, the printed minus sign of a negative number to `k`, superscript -1 to the character '−1', the micro sign to 'µ', the degree sign of '25 °C' to 'm', the centred dot of M^-1.s^-1 to ':', and the small capital D of the sugar names is dropped, so the cell text `5-Deoxy (1) 18p1 0.9p0.3 (1.0) 20 000 (1` is the paper's own printed row.

raw_value_unit_evidence: Table 2     Kinetic parameters for NADH-dependent reduction of xylose derivatives by yALR | column group header row: Candida tenuis Candida intermedia II | metric header row: kcat (s ) K ROm (mM) kcat/K ROm (M−1:s−1) k ∆∆G (kJ/mol) kcat (s−1) K ROm (mM) kcat/K ROm (M−1:s−1) k∆∆G (kJ/mol) | data row: 5-Deoxy (1) 18p1 0.9p0.3 (1.0) 20 000 (1.2) 11.2 (0.5) 13.5p0.6 1.3p0.3 (2.0) 10 384 (0.7) 9.7 (k1.0) | Candida intermedia II cells read: kcat = 13.5 s^-1 (printed with its standard deviation as p in the pdftotext extract); K ROm = 1.3 mM; kcat/K ROm = 10 384 M^-1:s^-1.

row_label: Candida intermedia II | 5-Deoxy (1)


column_label: Table label: Table 2     Kinetic parameters for NADH-dependent reduction of xylose derivatives by yALR. Row: 5-Fluoro (2). Enzyme column group: Candida intermedia II. Columns read: kcat (s−1) cell 15.5, K ROm (mM) cell 2.4, kcat/K ROm (M−1:s−1) cell 6 458. captured primary segment: 5-Fluoro (2) 19p1 0.6p0.4 (0.7) 31 667 (1.9) 12.3 (1.6) 15.5p1.9 2.4p0.8 (3.6) 6 458 (0.4) 8.5 (k2.2). metric: kcat; raw value: 15.5; raw unit: s^-1; normalized value: 15.5 s^(-1); metric: Km; raw value: 2.4; raw unit: mM; normalized value: 2.4 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 6.458333333333334 s^-1 mM^-1; assay condition: Table 2 assay: the concentration of NADH was 220 uM and saturating. Reaction conditions: 50 mM potassium phosphate buffer, pH 7.0, 25 C. Enzyme: the NADH-linked aldose reductase of Candida intermedia, printed in the table as Candida intermedia II. Export row conditions: pH 7; 298.15 K.

normalized_value_unit_evidence: Candida intermedia II columns of Table 2 row 5-Fluoro (2): kcat 15.5 s^-1 = 15.5 s^(-1) (no conversion, the paper already prints s^-1); Km 2.4 mM = 2.4 mM (no conversion, the paper already prints mM); kcat/Km 6.458333333333334 s^-1 mM^-1, the same-row quotient 15.5 s^-1 / 2.4 mM (1 M^-1 s^-1 = 0.001 s^-1 mM^-1, so the table's printed cell 6 458 M^-1:s^-1 is 6458 / 1000 = 6.458 s^-1 mM^-1, the same quotient carried to the printed cell's own four-figure precision). Rendering quirks of the pdftotext extract: the printed plus-minus sign is flattened to `p`, the printed minus sign of a negative number to `k`, superscript -1 to the character '−1', the micro sign to 'µ', the degree sign of '25 °C' to 'm', the centred dot of M^-1.s^-1 to ':', and the small capital D of the sugar names is dropped, so the cell text `5-Fluoro (2) 19p1 0.6p0.4 (0.7) 31 667 (` is the paper's own printed row.

raw_value_unit_evidence: Table 2     Kinetic parameters for NADH-dependent reduction of xylose derivatives by yALR | column group header row: Candida tenuis Candida intermedia II | metric header row: kcat (s ) K ROm (mM) kcat/K ROm (M−1:s−1) k ∆∆G (kJ/mol) kcat (s−1) K ROm (mM) kcat/K ROm (M−1:s−1) k∆∆G (kJ/mol) | data row: 5-Fluoro (2) 19p1 0.6p0.4 (0.7) 31 667 (1.9) 12.3 (1.6) 15.5p1.9 2.4p0.8 (3.6) 6 458 (0.4) 8.5 (k2.2) | Candida intermedia II cells read: kcat = 15.5 s^-1 (printed with its standard deviation as p in the pdftotext extract); K ROm = 2.4 mM; kcat/K ROm = 6 458 M^-1:s^-1.

row_label: Candida intermedia II | 5-Fluoro (2)


proof_lines: D-xylose L-arabinose L-idose


substrate_name: D-galactose

column_label: Official PMC PDF page 5 (journal page 105), Table 4, Galactose row under Candida intermedia II, columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat=5.9 s^-1; Km=74 mM; printed kcat/Km=0.080 s^-1 mM^-1. The exported 0.07972972972972973 is the same-row 5.9/74 quotient before table rounding.

raw_value_unit_evidence: Table 4, Candida intermedia II, Galactose: kcat=5.9 +/- 0.1 s^-1; Km=74 +/- 4 mM; kcat/Km=80 M^-1 s^-1.

row_label: Galactose; Candida intermedia II

table_label: Table 4. Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR

substrate: D-galactose


substrate_name: oenanthaldehyde

column_label: Table label: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR. Row: Oenanthaldehyde. Enzyme column group: Candida intermedia II. Columns read: kcat (s−1) cell 4.6, K ROm (mM) cell 4.7, kcat/K ROm (M−1:s−1) cell 979. captured primary segment: Oenanthaldehyde 21p3 5.4p0.6 3 888 – 4.6p0.2 4.7p1.1 979 –. metric: kcat; raw value: 4.6; raw unit: s^-1; normalized value: 4.6 s^(-1); metric: Km; raw value: 4.7; raw unit: mM; normalized value: 4.7 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 0.978723404255319 s^-1 mM^-1; assay condition: Table 4 assay: the concentration of NADH was 220 uM and saturating. Reaction conditions: 50 mM potassium phosphate buffer, pH 7.0, 25 C. Enzyme: the NADH-linked aldose reductase of Candida intermedia, printed in the table as Candida intermedia II. Export row conditions: pH 7; 298.15 K.

normalized_value_unit_evidence: Candida intermedia II columns of Table 4 row Oenanthaldehyde: kcat 4.6 s^-1 = 4.6 s^(-1) (no conversion, the paper already prints s^-1); Km 4.7 mM = 4.7 mM (no conversion, the paper already prints mM); kcat/Km 0.978723404255319 s^-1 mM^-1, the same-row quotient 4.6 s^-1 / 4.7 mM (1 M^-1 s^-1 = 0.001 s^-1 mM^-1, so the table's printed cell 979 M^-1:s^-1 is 979 / 1000 = 0.979 s^-1 mM^-1, the same quotient carried to the printed cell's own four-figure precision). Rendering quirks of the pdftotext extract: the printed plus-minus sign is flattened to `p`, the printed minus sign of a negative number to `k`, superscript -1 to the character '−1', the micro sign to 'µ', the degree sign of '25 °C' to 'm', the centred dot of M^-1.s^-1 to ':', and the small capital D of the sugar names is dropped, so the cell text `Oenanthaldehyde 21p3 5.4p0.6 3 888 – 4.6` is the paper's own printed row.

raw_value_unit_evidence: Table 4     Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR | column group header row: Candida tenuis Candida intermedia II | metric header row: Substrate kcat (s−1) K ROm (mM) kcat/K ROm k ∆∆G (kJ/mol) kcat (s−1) K ROm (mM) kcat/K ROm (M−1:s−1) k∆∆G (kJ/mol) | data row: Oenanthaldehyde 21p3 5.4p0.6 3 888 – 4.6p0.2 4.7p1.1 979 – | Candida intermedia II cells read: kcat = 4.6 s^-1 (printed with its standard deviation as p in the pdftotext extract); K ROm = 4.7 mM; kcat/K ROm = 979 M^-1:s^-1.

row_label: Candida intermedia II | Oenanthaldehyde

substrate: oenanthaldehyde


substrate_name: D-Xylose

column_label: Official PMC PDF page 3 (journal page 103), Table 2, Xylose row under Candida intermedia II, columns kcat, Km, and kcat/Km.

raw_value_unit_evidence: Table 2, Candida intermedia II, Xylose: kcat=10.5 +/- 0.6 s^-1; Km=50 +/- 5 mM; kcat/Km=210 M^-1 s^-1.

row_label: Xylose; Candida intermedia II

table_label: Table 2. Kinetic parameters for NADH-dependent reduction of xylose derivatives by yALR

substrate: D-Xylose


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

organism: Moorella thermoacetica

sequence_variant_note: Resolved canonical sequence from ncbi_genpept_accession:ABC19597.1 and applied mutation signature A30C/R31I/T32K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 323.15 K; cofactor NAD+

column_label: PMID 27587230 DOI 10.1038/srep32644 Table 2; row A30C/R31I/T32K; NAD+ columns under Km (uM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

table_label: Table 2. Kinetics parameters of 6PGDH and mutants


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A30D/R31I/T32I to reconstruct the assayed variant sequence.

column_label: Table 2, row 'A30D/R31I/T32I', NAD+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

table_label: Table 2

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A30E/R31I/T32D to reconstruct the assayed variant sequence.

column_label: Table 2, row 'A30E/R31I/T32D', NAD+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 2, row 'R31I', NAD+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

row_label: R31I / NAD+