enzyme_display_name: pyridoxal 4-dehydrogenase

organism: Microbacterium luteolum

substrate_name: NAD+; Pyridoxal

enzyme: pyridoxal 4-dehydrogenase

substrate: NAD+; Pyridoxal


enzyme_display_name: carnitine 3-dehydrogenase

organism: Rhizobium sp. (Cicer)

substrate_name: NAD+; L-Carnitine

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

km_unit: mM

sequence_source: multiple

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

assay_conditions_summary: cofactor NAD+

enzyme: carnitine 3-dehydrogenase

substrate: NAD+; L-Carnitine

status: unverified


organism: Xanthomonas translucens

substrate_name: L-Carnitine; NAD+

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

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

substrate: L-Carnitine; NAD+


enzyme_display_name: L-carnitine dehydrogenase

organism: Pseudomonas sp

substrate_name: L-carnithine

source_db: uniprot

source_license: CC BY 4.0

proof_lines: Part of the values are for the recombinant protein expressed in E.coli (PubMed:20530902). Other values are for the wild-type protein (Ref.2).

enzyme: L-carnitine dehydrogenase

substrate: L-carnithine

source: uniprot


enzyme_display_name: Aromatic 2-oxoacid reductase

organism: Clostridium sporogenes (strain ATCC 15579)

substrate_name: phenyllactate

enzyme: Aromatic 2-oxoacid reductase

substrate: phenyllactate


enzyme_display_name: indanol dehydrogenase

organism: Homo sapiens

substrate_name: Indan-1-ol; NADP+

assay_conditions_summary: cofactor NADP+

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: indanol dehydrogenase

substrate: Indan-1-ol; NADP+


substrate_name: NADP+; Indan-1-ol

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

substrate: NADP+; Indan-1-ol


enzyme_display_name: D-arabinose 1-dehydrogenase

organism: Saccharomyces cerevisiae

substrate_name: NAD+; D-Arabinose

enzyme: D-arabinose 1-dehydrogenase

substrate: NAD+; D-Arabinose


enzyme_display_name: glucose 1-dehydrogenase (NADP+)

organism: Halobacterium volcanii

substrate_name: D-Glucose; NADP+

enzyme: glucose 1-dehydrogenase (NADP+)

substrate: D-Glucose; NADP+


enzyme_display_name: Glucose 1-dehydrogenase

organism: Gluconobacter oxydans (strain 621H)

substrate_name: Unknown

km_display: Not reported

proof_lines: kcat is 84.8 sec(-1) with glucose as substrate. kcat is 106 sec(-1) with mannose as substrate.

enzyme: Glucose 1-dehydrogenase

substrate: Unknown


organism: Saccharolobus solfataricus

substrate_name: D-glucose (in the presence of NAD(+), at 70 degrees Celsius and pH 8)

assay_conditions_summary: pH 8


enzyme_display_name: L-arabinose 1-dehydrogenase (NAD(P)(+))

organism: Azospirillum brasilense

substrate_name: L-arabinose (in the presence of NAD(+), at 30 degrees Celsius and pH 9.0)

assay_conditions_summary: pH 9

enzyme: L-arabinose 1-dehydrogenase (NAD(P)(+))


enzyme_display_name: UniProt Q5SLC4

organism: Thermus thermophilus HB8

source_db: skid

verification_status: verified

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q5SLC4

status: verified

source: skid


enzyme_display_name: L-fucose dehydrogenase

substrate_name: L-fuctose

proof_lines: kcat is 14.00 sec(-1) with L-fucose as substrate. kcat is 16.89 sec(-1) with NAD(+) as substrate (PubMed:38944119). kcat is 0.0003 sec(-1) with beta-estradiol as substrate. kcat is 0.00028sec(-1) with androst-5-en-3beta,17beta-diol as subst

enzyme: L-fucose dehydrogenase

substrate: L-fuctose


enzyme_display_name: D-threo-aldose 1-dehydrogenase

enzyme: D-threo-aldose 1-dehydrogenase


organism: Rattus norvegicus

proof_lines: kcat is 0.13 sec(-1) with L-fucose as substrate. kcat is 0.15 sec(-1) with NAD(+) as substrate.


organism: Oryctolagus cuniculus

proof_lines: kcat is 7.00 sec(-1) with L-fucose as substrate. kcat is 7.00 sec(-1) with NAD(+) as substrate (PubMed:38944119). kcat/KM=4878 min(-1) mM(-1) for L-fuctose (PubMed:38944119).


enzyme_display_name: GDP-mannose 6-dehydrogenase

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

enzyme: GDP-mannose 6-dehydrogenase


enzyme_display_name: dTDP-4-dehydrorhamnose reductase

organism: Salmonella typhimurium

enzyme: dTDP-4-dehydrorhamnose reductase


organism: Aneurinibacillus thermoaerophilus

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


organism: Pseudomonas aeruginosa

substrate_name: UDP-GlcNAc (refolded enzyme, in the presence of NAD(+))

proof_lines: kcat is 110 min(-1) with UDP-GlcNAc as substrate. kcat is 0.69 min(-1) with UDP-GalNAc as substrate. kcat is 110 min(-1) with NAD(+) as substrate. kcat is 0.71 min(-1) with NADP(+) as substrate (PubMed:18065759). kcat is 5.5 min(-1) with UD


substrate_name: UDP-D-GlcNAc

substrate: UDP-D-GlcNAc


enzyme_display_name: mannitol 2-dehydrogenase (NADP+)

organism: Alternaria alternata

substrate_name: H+; D-Fructose; NADPH

enzyme: mannitol 2-dehydrogenase (NADP+)

substrate: H+; D-Fructose; NADPH


enzyme_display_name: UniProt P28845

data_origin: experimental

enzyme: UniProt P28845


substrate_name: dehydroepiandrosterone

source_db: brenda

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

proof_lines: wild-type, presence of 2-mercatoethanol pH 7.4

substrate: dehydroepiandrosterone

source: brenda


substrate_name: NAD+

assay_conditions_summary: pH 7.4; 300.15 K; cofactor NAD+

substrate: NAD+


organism: Solanum lycopersicum

substrate_name: pregnenolone

substrate: pregnenolone


substrate_name: dehydrotomatidine

substrate: dehydrotomatidine


organism: Digitalis lanata

substrate_name: NADH

assay_conditions_summary: pH 7.8; 303.15 K; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 7.8; 303.15 K; cofactor NAD+


organism: Rhinella arenarum


organism: Bufo gargarizans


proof_lines:
NAD+ as cofactor
pH 7.8, 30°C


enzyme_display_name: 16alpha-hydroxysteroid dehydrogenase

organism: Rattus sp.

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

enzyme: 16alpha-hydroxysteroid dehydrogenase

substrate: NADPH


assay_conditions_summary: cofactor NADH


organism: Cricetinae

proof_lines:
type I
type II


enzyme_display_name: perillyl-alcohol dehydrogenase

organism: Acinetobacter calcoaceticus

substrate_name: perillyl alcohol

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

enzyme: perillyl-alcohol dehydrogenase

substrate: perillyl alcohol


organism: Pseudomonas sp.

assay_conditions_summary: pH 8.6; cofactor NAD+


organism: Homo sapiens

proof_lines:
wild-type 3beta-HSD1, pH 7.4, 27°C
wild-type 3beta-HSD2, pH 7.4, 27°C
pH 7.4, 27°C, wild-tpye 3beta-HSD1


enzyme_display_name: 11beta-hydroxysteroid dehydrogenase

substrate_name: cortisol

proof_lines: pH 7.5, 22°C, recombinant wild-type isozyme 11beta-HSD1 oxidized with K3Fe(CN)6

enzyme: 11beta-hydroxysteroid dehydrogenase

substrate: cortisol


organism: Comamonas testosteroni


organism: Clarias gariepinus


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C72S with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.4; cofactor NAD+

proof_lines: mutant C72S, presence of 2-mercatoethanol pH 7.4


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C83A with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant C83A, presence of 2-mercatoethanol pH 7.4


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C72F with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

proof_lines: mutant C72F, presence of 2-mercatoethanol pH 7.4


enzyme_display_name: Geraniol dehydrogenase

organism: Castellaniella defragrans (strain DSM 12143 / CCUG 39792 / 65Phen)

substrate_name: geraniol

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

proof_lines: The values given here are for the native GeDH, the values for the recombinant protein can be found in another article (PubMed:22286981).

enzyme: Geraniol dehydrogenase

substrate: geraniol


substrate_name: (S)-perillyl alcohol

substrate: (S)-perillyl alcohol


substrate_name: citronellol

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

substrate: citronellol


substrate_name: cumic alcohol

substrate: cumic alcohol


substrate_name: benzyl alcohol

substrate: benzyl alcohol


kcat_over_km_origin: calculated


proof_lines: pH 7.4, 27°C, chimeric R195P-1 mutant of the enzyme (3beta-HSD1)


assay_conditions_summary: pH 7.4; cofactor NADH


substrate_name: prostaglandin E1

proof_lines: kcat is 8.6 min(-1) with (11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate and (5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate as substrates.

substrate: prostaglandin E1


substrate_name: prostaglandin A1

substrate: prostaglandin A1


substrate_name: prostaglandin A2

substrate: prostaglandin A2


substrate_name: NAD in the presence of prostaglandin E1

substrate: NAD in the presence of prostaglandin E1


source_db: oed

source: oed


substrate_name: dehydroepiandrosterone

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P195R to reconstruct the assayed variant sequence.

substrate: dehydroepiandrosterone


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


substrate_name: NAD+

substrate: NAD+


assay_conditions_summary: pH 7.4; 300.15 K; cofactor NADH


organism: Mesocricetus auratus

verification_status: corrected

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

column_label: PMID 14973125 Table I, Reduction of 7-ketocholesterol, Hamster row, Km (nM) = 384 +/- 44.

normalized_value_unit_evidence: Km normalized_value=0.000384 mM; exported 0.00038 mM is rounded from the printed nM cell.

raw_value_unit_evidence: Table I row Reduction of 7-ketocholesterol / Hamster, Km column: 384 +/- 44 nM.

table_label: Table I. Oxidation and reduction by lysates from HEK-293 cells expressing recombinant 11beta-HSD1

source_databases_merged: brenda uniprot

status: corrected


column_label: PMID 14973125 Table I, Reduction of 11-dehydrocorticosterone, Hamster row, Km (nM) = 396 +/- 82.

normalized_value_unit_evidence: Km normalized_value=0.000396 mM; exported 0.0004 mM is rounded from the printed nM cell.

raw_value_unit_evidence: Table I row Reduction of 11-dehydrocorticosterone / Hamster, Km column: 396 +/- 82 nM.


proof_lines: 37°C, pH 7.4, in HEK-293 lysates expressing 11beta-HSD1


substrate_name: corticosterone

column_label: PMID 14973125 Table II, Oxidation of corticosterone, Hamster row, Km (nM) = 321 +/- 48.

normalized_value_unit_evidence: Km normalized_value=0.000321 mM.

raw_value_unit_evidence: Table II row Oxidation of corticosterone / Hamster, Km column: 321 +/- 48 nM.

row_label: Oxidation of corticosterone / Hamster

table_label: Table II. Oxidation and reduction of glucocorticoids and 7-oxycholesterols in intact HEK-293 cells expressing recombinant 11beta-HSD1

substrate: corticosterone


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q240R with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 27°C, recombinant isozyme 3beta-HSD1 mutant Q240R


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q105M with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 27°C, recombinant isozyme 3beta-HSD1 mutant Q105M

proof_lines: pH 7.4, 27°C, recombinant isozyme 3beta-HSD2 mutant Q105M


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P26439 and applied mutation signature R240Q to reconstruct the assayed variant sequence.

column_label: Table 3 (Cofactor kinetics for the 3β-HSD and isomerase activities of the purified mutant and wild-type enzymes), enzyme row R240Q2, 3β-HSD NAD+ column group; column Km uM = 37.2; column kcat min^-1 = 11.2; column kcat/Km min^-1 uM^-1 = 0.30.

raw_value_unit_evidence: Table 3, enzyme row R240Q2, 3β-HSD NAD+ column group: Km = 37.2 uM; kcat = 11.2 min^-1; printed kcat/Km = 0.30 min^-1 uM^-1.

table_label: Table 3: Cofactor kinetics for the 3β-HSD and isomerase activities of the purified mutant and wild-type enzymes (J Biol Chem 2005, 280(22):21321-21328)


column_label: Table 2 (Substrate kinetics for the 3β-HSD and isomerase activities of the purified mutant and wild-type enzymes), enzyme row R240Q2, 3β-HSD1 column group; column Km uM = 32.7; column kcat min^-1 = 13.0; column kcat/Km min^-1 uM^-1 = 0.40.

raw_value_unit_evidence: Table 2, enzyme row R240Q2, 3β-HSD1 column group: Km = 32.7 uM; kcat = 13.0 min^-1; printed kcat/Km = 0.40 min^-1 uM^-1.

table_label: Table 2: Substrate kinetics for the 3β-HSD and isomerase activities of the purified mutant and wild-type enzymes (J Biol Chem 2005, 280(22):21321-21328)


smiles: CCCCCC=CC=CC(CC=CCC=CCCCC(=O)[O-])O


smiles: CCCCCC(C=CC=CCC=CCC=CCCCC(=O)[O-])O


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature V186K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'V186K'; column 'Km (uM)' = 22; column 'kcat (s^-1)' = 35; column 'kcat/Km (M^-1 s^-1)' = 1.6 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 22 uM; 22 / 1000 = 0.022 mM. kcat: printed Table 2 cell 35 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 35 s^(-1). kcat/Km: printed Table 2 cell 1.6 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.6 x 10^6 / 1000 = 1600 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row V186K: the Km (uM) cell prints 22, the kcat (s^-1) cell prints 35, and the kcat/Km (M^-1 s^-1) cell prints 1.6 x 10^6.

row_label: Table 2, NAD+ block, row V186K

table_label: Table 2: Km, kcat, and kcat/Km values for 15-PGDH mutants (Archives of Biochemistry and Biophysics 433 (2005) 447-453)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature V186A to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'V186A'; column 'Km (uM)' = 24; column 'kcat (s^-1)' = 70; column 'kcat/Km (M^-1 s^-1)' = 2.9 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 24 uM; 24 / 1000 = 0.024 mM. kcat: printed Table 2 cell 70 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 70 s^(-1). kcat/Km: printed Table 2 cell 2.9 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.9 x 10^6 / 1000 = 2900 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row V186A: the Km (uM) cell prints 24, the kcat (s^-1) cell prints 70, and the kcat/Km (M^-1 s^-1) cell prints 2.9 x 10^6.

row_label: Table 2, NAD+ block, row V186A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature V186I to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'V186I'; column 'Km (uM)' = 272; column 'kcat (s^-1)' = 247; column 'kcat/Km (M^-1 s^-1)' = 0.9 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 272 uM; 272 / 1000 = 0.272 mM. kcat: printed Table 2 cell 247 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 247 s^(-1). kcat/Km: printed Table 2 cell 0.9 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.9 x 10^6 / 1000 = 900 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row V186I: the Km (uM) cell prints 272, the kcat (s^-1) cell prints 247, and the kcat/Km (M^-1 s^-1) cell prints 0.9 x 10^6.

row_label: Table 2, NAD+ block, row V186I


enzyme_display_name: Alcohol dehydrogenase 2

organism: Tanacetum cinerariifolium

substrate_name: trans-chrysanthemol

proof_lines: kcat is 0.75 sec(-1) with trans-chrysanthemol as substrate (in the presence of NAD(+)) (PubMed:29122986). kcat is 0.64 sec(-1) with NAD(+) as substrate (in the presence of trans-chrysanthemol) (PubMed:29122986).

enzyme: Alcohol dehydrogenase 2

substrate: trans-chrysanthemol


substrate_name: NAD(+)

substrate: NAD(+)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R195P with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S123A to reconstruct the assayed variant sequence.


substrate_name: prostaglandin E2

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

substrate: prostaglandin E2


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H156Y with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

proof_lines:
mutant H156Y, pH 7.4, 27°C
27°C, pH 7.4, H156Y mutant 3beta-HSD1
pH 7.4, 27°C, recombinant mutant H156Y


organism: Cavia porcellus

proof_lines: 37°C, pH 7.4, recombinant 11beta-HSD1 expressed in Escherichia coli


substrate_name: cortisone

proof_lines: 37°C, pH 7.4, recombinant 11beta-HSD1 measured in intact COS cells transfected with 11beta-HSD1

proof_lines: 37°C, pH 7.4, recombinant 11beta-HSD1 expressed in Pichia pastoris

substrate: cortisone


proof_lines:
27°C, pH 7.4, H156Y mutant 3beta-HSD1
27°C, pH 7.4, H156Y mutant


enzyme_display_name: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1

organism: Rattus norvegicus

substrate_name: dihydrotestosterone (in the presence of NADPH)

column_label: Abstract reports with NADPH the type I isoform has Km value 1.18 microM for DHT.

raw_value_unit_evidence: Km raw_value=1.18 microM raw_unit=microM

row_label: Rat type I 3 beta-HSD / dihydrotestosterone with NADPH

table_label: PubMed XML abstract PMID 1537836


organism: Mycobacterium tuberculosis

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

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+

proof_lines: cosubstrate dehydroepiandrosterone, pH 8.5, 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature I17A to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'I17A'; column 'Km (uM)' = 555; column 'kcat (s^-1)' = 129; column 'kcat/Km (M^-1 s^-1)' = 0.2 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 555 uM; 555 / 1000 = 0.555 mM. kcat: printed Table 2 cell 129 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 129 s^(-1). kcat/Km: printed Table 2 cell 0.2 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.2 x 10^6 / 1000 = 200 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row I17A: the Km (uM) cell prints 555, the kcat (s^-1) cell prints 129, and the kcat/Km (M^-1 s^-1) cell prints 0.2 x 10^6.

row_label: Table 2, NAD+ block, row I17A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature I17L to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'I17L'; column 'Km (uM)' = 59; column 'kcat (s^-1)' = 165; column 'kcat/Km (M^-1 s^-1)' = 2.8 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 59 uM; 59 / 1000 = 0.059 mM. kcat: printed Table 2 cell 165 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 165 s^(-1). kcat/Km: printed Table 2 cell 2.8 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.8 x 10^6 / 1000 = 2800 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row I17L: the Km (uM) cell prints 59, the kcat (s^-1) cell prints 165, and the kcat/Km (M^-1 s^-1) cell prints 2.8 x 10^6.

row_label: Table 2, NAD+ block, row I17L


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature I17V to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'I17V'; column 'Km (uM)' = 98; column 'kcat (s^-1)' = 110; column 'kcat/Km (M^-1 s^-1)' = 1.1 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 98 uM; 98 / 1000 = 0.098 mM. kcat: printed Table 2 cell 110 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 110 s^(-1). kcat/Km: printed Table 2 cell 1.1 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^6 / 1000 = 1100 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row I17V: the Km (uM) cell prints 98, the kcat (s^-1) cell prints 110, and the kcat/Km (M^-1 s^-1) cell prints 1.1 x 10^6.

row_label: Table 2, NAD+ block, row I17V


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature N91A to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'N91A'; column 'Km (uM)' = 719; column 'kcat (s^-1)' = 91; column 'kcat/Km (M^-1 s^-1)' = 0.1 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 719 uM; 719 / 1000 = 0.719 mM. kcat: printed Table 2 cell 91 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 91 s^(-1). kcat/Km: printed Table 2 cell 0.1 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.1 x 10^6 / 1000 = 100 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row N91A: the Km (uM) cell prints 719, the kcat (s^-1) cell prints 91, and the kcat/Km (M^-1 s^-1) cell prints 0.1 x 10^6.

row_label: Table 2, NAD+ block, row N91A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature N91D to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'N91D'; column 'Km (uM)' = 32; column 'kcat (s^-1)' = 42; column 'kcat/Km (M^-1 s^-1)' = 1.3 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 32 uM; 32 / 1000 = 0.032 mM. kcat: printed Table 2 cell 42 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 42 s^(-1). kcat/Km: printed Table 2 cell 1.3 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 x 10^6 / 1000 = 1300 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row N91D: the Km (uM) cell prints 32, the kcat (s^-1) cell prints 42, and the kcat/Km (M^-1 s^-1) cell prints 1.3 x 10^6.

row_label: Table 2, NAD+ block, row N91D


column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'Wild type'; column 'Km (uM)' = 38; column 'kcat (s^-1)' = 47; column 'kcat/Km (M^-1 s^-1)' = 1.2 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 38 uM; 38 / 1000 = 0.038 mM. kcat: printed Table 2 cell 47 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 47 s^(-1). kcat/Km: printed Table 2 cell 1.2 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 x 10^6 / 1000 = 1200 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row Wild type: the Km (uM) cell prints 38, the kcat (s^-1) cell prints 47, and the kcat/Km (M^-1 s^-1) cell prints 1.2 x 10^6.

row_label: Table 2, NAD+ block, row Wild type


substrate_name: Prostaglandin E2

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), PGE2 substrate block, row 'I17A'; column 'Km (uM)' = 11.0; column 'kcat (s^-1)' = 127; column 'kcat/Km (M^-1 s^-1)' = 1.2 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 11.0 uM; 11.0 / 1000 = 0.011 mM. kcat: printed Table 2 cell 127 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 127 s^(-1). kcat/Km: printed Table 2 cell 1.2 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 x 10^7 / 1000 = 12000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, PGE2 block, row I17A: the Km (uM) cell prints 11.0, the kcat (s^-1) cell prints 127, and the kcat/Km (M^-1 s^-1) cell prints 1.2 x 10^7.

row_label: Table 2, PGE2 block, row I17A

substrate: Prostaglandin E2


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D241N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D265N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D36A/K37R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 300.15 K; cofactor NADP+

column_label: PMID 12832414 Table IV. Comparison of substrate kinetics of purified D36A/K37R and wild-type 3beta-HSD and isomerase activities using NAD(H) and NADP(H) as cofactor; row D36A/K37R / DHEA / NADP+ / 3beta-HSD; columns Km (uM), Kcat (min^-1); same-row normalized tuple kcat=0.01833333333333333333333333333 s^-1, Km=0.0048 mM, kcat/Km=3.819444444444444444444444444 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=0.01833333333333333333333333333 normalized_unit=s^-1; Km normalized_value=0.0048 normalized_unit=mM; kcat/Km normalized_value=3.819444444444444444444444444 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table IV row DHEA, cofactor NADP+, activity 3beta-HSD, D36A/K37R columns: Km 4.8 uM; Kcat 1.1 min^-1.

row_label: D36A/K37R / DHEA / NADP+ / 3beta-HSD


substrate_name: NADP+

column_label: PMID 12832414 Table III. Comparison of NAD(H) and NADP(H) cofactor kinetics for the 3beta-HSD and isomerase activities of the purified D36A/K37R and wild-type enzymes; row D36A/K37R / NADP+ / 3beta-HSD; columns Km (uM), Kcat (min^-1); same-row normalized tuple kcat=0.02166666666666666666666666667 s^-1, Km=0.0206 mM, kcat/Km=1.051779935275080906148867314 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=0.02166666666666666666666666667 normalized_unit=s^-1; Km normalized_value=0.0206 normalized_unit=mM; kcat/Km normalized_value=1.051779935275080906148867314 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table III row D36A/K37R, cofactor NADP+, activity 3beta-HSD: Km 20.6 uM; Kcat 1.3 min^-1.

row_label: D36A/K37R / NADP+ / 3beta-HSD

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q148E with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q148H with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q148N with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


enzyme_display_name: sorbitol-6-phosphate 2-dehydrogenase

organism: Erwinia amylovora

substrate_name: D-fructose 6-phosphate

assay_conditions_summary: pH 9; cofactor NADH

column_label: Primary Table 3 row d-Fructose 6-phosphate has columns Km [mM], kcat [s^-1], and kcat/Km with values 2.0 +/- 0.4, 0.56, and 0.28.

raw_value_unit_evidence: Table 3 row d-Fructose 6-phosphate: Km [mM] 2.0 +/- 0.4; kcat [s^-1] 0.56; kcat/Km column 0.28 with table header rendered as uM^-1 s^-1

row_label: d-Fructose 6-phosphate

table_label: ScienceDirect full text Table 3, Kinetic parameters for SrlD (Mw = 28.13 KDa)

enzyme: sorbitol-6-phosphate 2-dehydrogenase

substrate: D-fructose 6-phosphate


substrate_name: D-sorbitol 6-phosphate

assay_conditions_summary: pH 9; cofactor NAD+

column_label: Primary Table 3 row d-Sorbitol 6-phosphate has columns Km [mM], kcat [s^-1], and kcat/Km with values 9.0 +/- 1.3, 5.6, and 0.62.

raw_value_unit_evidence: Table 3 row d-Sorbitol 6-phosphate: Km [mM] 9.0 +/- 1.3; kcat [s^-1] 5.6; kcat/Km column 0.62 with table header rendered as uM^-1 s^-1

row_label: d-Sorbitol 6-phosphate

substrate: D-sorbitol 6-phosphate


substrate_name: NADH

column_label: Primary Table 3 row NADH has Km [mM] value 0.048 +/- 0.006.

raw_value_unit_evidence: Table 3 row NADH, column Km [mM]: 0.048 +/- 0.006

row_label: NADH

substrate: NADH


assay_conditions_summary: pH 9; cofactor NADP+

column_label: Primary Table 3 row NAD+ has Km [mM] value 1.6 +/- 0.2*; footnote marks Kmapp.

normalized_value_unit_evidence: Km 1.6 mM

raw_value_unit_evidence: Table 3 row NAD+, column Km [mM]: 1.6 +/- 0.2*; footnote * Kmapp

row_label: NAD+


assay_conditions_summary: pH 9; 295.15 K; cofactor NAD+

column_label: Primary Table 3 row d-Sorbitol 6-phosphate has kcat/Km value 0.62; Km 9.0 mM and kcat 5.6 s^-1 provide the same precise expected ratio.

raw_value_unit_evidence: Table 3 row d-Sorbitol 6-phosphate, kcat/Km column: 0.62 with table header rendered as uM^-1 s^-1


substrate_name: D-Fructose 6-phosphate

assay_conditions_summary: pH 9; 295.15 K; cofactor NADH

column_label: Primary Table 3 row d-Fructose 6-phosphate has kcat/Km value 0.28; Km 2.0 mM and kcat 0.56 s^-1 match the same expected ratio.

raw_value_unit_evidence: Table 3 row d-Fructose 6-phosphate, kcat/Km column: 0.28 with table header rendered as uM^-1 s^-1

substrate: D-Fructose 6-phosphate


column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), PGE2 substrate block, row 'I17L'; column 'Km (uM)' = 11.8; column 'kcat (s^-1)' = 210; column 'kcat/Km (M^-1 s^-1)' = 1.8 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 11.8 uM; 11.8 / 1000 = 0.0118 mM. kcat: printed Table 2 cell 210 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 210 s^(-1). kcat/Km: printed Table 2 cell 1.8 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.8 x 10^7 / 1000 = 18000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, PGE2 block, row I17L: the Km (uM) cell prints 11.8, the kcat (s^-1) cell prints 210, and the kcat/Km (M^-1 s^-1) cell prints 1.8 x 10^7.

row_label: Table 2, PGE2 block, row I17L


column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), PGE2 substrate block, row 'I17V'; column 'Km (uM)' = 11.2; column 'kcat (s^-1)' = 143; column 'kcat/Km (M^-1 s^-1)' = 1.3 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 11.2 uM; 11.2 / 1000 = 0.0112 mM. kcat: printed Table 2 cell 143 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 143 s^(-1). kcat/Km: printed Table 2 cell 1.3 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 x 10^7 / 1000 = 13000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, PGE2 block, row I17V: the Km (uM) cell prints 11.2, the kcat (s^-1) cell prints 143, and the kcat/Km (M^-1 s^-1) cell prints 1.3 x 10^7.

row_label: Table 2, PGE2 block, row I17V


column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), PGE2 substrate block, row 'N91A'; column 'Km (uM)' = 6.1; column 'kcat (s^-1)' = 73; column 'kcat/Km (M^-1 s^-1)' = 1.2 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 6.1 uM; 6.1 / 1000 = 0.0061 mM. kcat: printed Table 2 cell 73 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 73 s^(-1). kcat/Km: printed Table 2 cell 1.2 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 x 10^7 / 1000 = 12000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, PGE2 block, row N91A: the Km (uM) cell prints 6.1, the kcat (s^-1) cell prints 73, and the kcat/Km (M^-1 s^-1) cell prints 1.2 x 10^7.

row_label: Table 2, PGE2 block, row N91A


column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), PGE2 substrate block, row 'N91D'; column 'Km (uM)' = 2.6; column 'kcat (s^-1)' = 45; column 'kcat/Km (M^-1 s^-1)' = 1.7 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 2.6 uM; 2.6 / 1000 = 0.0026 mM. kcat: printed Table 2 cell 45 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 45 s^(-1). kcat/Km: printed Table 2 cell 1.7 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.7 x 10^7 / 1000 = 17000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, PGE2 block, row N91D: the Km (uM) cell prints 2.6, the kcat (s^-1) cell prints 45, and the kcat/Km (M^-1 s^-1) cell prints 1.7 x 10^7.

row_label: Table 2, PGE2 block, row N91D


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature V186A to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), PGE2 substrate block, row 'V186A'; column 'Km (uM)' = 4.5; column 'kcat (s^-1)' = 78; column 'kcat/Km (M^-1 s^-1)' = 1.7 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 4.5 uM; 4.5 / 1000 = 0.0045 mM. kcat: printed Table 2 cell 78 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 78 s^(-1). kcat/Km: printed Table 2 cell 1.7 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.7 x 10^7 / 1000 = 17000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, PGE2 block, row V186A: the Km (uM) cell prints 4.5, the kcat (s^-1) cell prints 78, and the kcat/Km (M^-1 s^-1) cell prints 1.7 x 10^7.

row_label: Table 2, PGE2 block, row V186A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature V186I to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), PGE2 substrate block, row 'V186I'; column 'Km (uM)' = 21.8; column 'kcat (s^-1)' = 262; column 'kcat/Km (M^-1 s^-1)' = 1.2 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 21.8 uM; 21.8 / 1000 = 0.0218 mM. kcat: printed Table 2 cell 262 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 262 s^(-1). kcat/Km: printed Table 2 cell 1.2 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 x 10^7 / 1000 = 12000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, PGE2 block, row V186I: the Km (uM) cell prints 21.8, the kcat (s^-1) cell prints 262, and the kcat/Km (M^-1 s^-1) cell prints 1.2 x 10^7.

row_label: Table 2, PGE2 block, row V186I


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature V186K to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), PGE2 substrate block, row 'V186K'; column 'Km (uM)' = 3.5; column 'kcat (s^-1)' = 37; column 'kcat/Km (M^-1 s^-1)' = 1.1 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 3.5 uM; 3.5 / 1000 = 0.0035 mM. kcat: printed Table 2 cell 37 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 37 s^(-1). kcat/Km: printed Table 2 cell 1.1 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^7 / 1000 = 11000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, PGE2 block, row V186K: the Km (uM) cell prints 3.5, the kcat (s^-1) cell prints 37, and the kcat/Km (M^-1 s^-1) cell prints 1.1 x 10^7.

row_label: Table 2, PGE2 block, row V186K


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R195P with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 300.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R195R with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P26439 and applied mutation signature D61N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 300.15 K; buffer 0.02 M potassium phosphate; cofactor NADH

column_label: Table 6 (cofactor kinetics for the 3beta-HSD and isomerase activities of the purified mutant and wild-type enzymes), printed column heads Purified Enzyme | Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the NAD 3beta-HSD1 block and Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the NADH Isomerase2 block. Table 6, enzyme row D61N, NADH Isomerase2 block; columns Km uM, kcat min^-1 and kcat/Km min^-1 uM^-1 of the NADH Isomerase2 block; Km cell = 7.2 uM; kcat cell = 46.1 min^-1; kcat/Km cell = 6.4.

raw_value_unit_evidence: Table 6, enzyme row D61N, NADH Isomerase2 block: Km = 7.2 uM; kcat = 46.1 min^-1; kcat/Km = 6.4 under the printed column head kcat/Km min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P26439 and applied mutation signature E192A to reconstruct the assayed variant sequence.

column_label: Table 6 (cofactor kinetics for the 3beta-HSD and isomerase activities of the purified mutant and wild-type enzymes), printed column heads Purified Enzyme | Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the NAD 3beta-HSD1 block and Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the NADH Isomerase2 block. Table 6, enzyme row E192A, NADH Isomerase2 block; columns Km uM, kcat min^-1 and kcat/Km min^-1 uM^-1 of the NADH Isomerase2 block; Km cell = 2.5 uM; kcat cell = 18.8 min^-1; kcat/Km cell = 7.5.

raw_value_unit_evidence: Table 6, enzyme row E192A, NADH Isomerase2 block: Km = 2.5 uM; kcat = 18.8 min^-1; kcat/Km = 7.5 under the printed column head kcat/Km min^-1 uM^-1.


organism: Klebsiella aerogenes

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

assay_conditions_summary: pH 7.1; buffer pH 7; cofactor NADH

column_label: Table VIII, D-sorbitol 6-phosphate dehydrogenase column, row K_m (DPNH) = 1.8 x 10^-4 M; DPNH is historical NADH label; normalized to 0.18 mM.

normalized_value_unit_evidence: Km=0.18 mM after M -> mM conversion

raw_value_unit_evidence: Km=1.8 x 10^-4 M (paper unit M)

row_label: K_m (DPNH)

table_label: Table VIII: Michaelis-Menten constants of reactants in D-sorbitol 6-phosphate and D-mannitol 1-phosphate dehydrogenases


assay_conditions_summary: pH 9; buffer pH 9; cofactor NAD+

column_label: Table VIII, D-sorbitol 6-phosphate dehydrogenase column, row K_m (DPN) = 4.2 x 10^-4 M; DPN is historical NAD+ label; normalized to 0.42 mM.

normalized_value_unit_evidence: Km=0.42 mM after M -> mM conversion

raw_value_unit_evidence: Km=4.2 x 10^-4 M (paper unit M)

row_label: K_m (DPN)


substrate_name: sorbitol 6-phosphate

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

assay_conditions_summary: pH 9; buffer pH 9

column_label: Table VIII, D-sorbitol 6-phosphate dehydrogenase column, row K_m (D-sorbitol 6-phosphate) = 6.25 x 10^-3 M; normalized to 6.25 mM.

normalized_value_unit_evidence: Km=6.25 mM after M -> mM conversion

raw_value_unit_evidence: Km=6.25 x 10^-3 M (paper unit M)

row_label: K_m (D-sorbitol 6-phosphate)

substrate: sorbitol 6-phosphate


assay_conditions_summary: pH 7.1; buffer pH 7

column_label: Table VIII, D-sorbitol 6-phosphate dehydrogenase column, row K_m (D-fructose 6-phosphate) = 1.05 x 10^-2 M; normalized to 10.5 mM.

normalized_value_unit_evidence: Km=10.5 mM after M -> mM conversion

raw_value_unit_evidence: Km=1.05 x 10^-2 M (paper unit M)

row_label: K_m (D-fructose 6-phosphate)


column_label: Table 5 (substrate kinetics for the 3beta-HSD and isomerase activities of the purified mutant and wild-type enzymes), printed column heads Purified Enzyme | Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the 3beta-HSD1 substrate block and Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the Isomerase2 substrate block. Table 5, enzyme row D61N, 3beta-HSD1 block; columns Km uM, kcat min^-1 and kcat/Km min^-1 uM^-1 of the 3beta-HSD1 block; Km cell = 4.7 uM; kcat cell = 2.8 min^-1; kcat/Km cell = 0.60.

raw_value_unit_evidence: Table 5, enzyme row D61N, 3beta-HSD1 block: Km = 4.7 uM; kcat = 2.8 min^-1; kcat/Km = 0.60 under the printed column head kcat/Km min^-1 uM^-1.


column_label: Table 5 (substrate kinetics for the 3beta-HSD and isomerase activities of the purified mutant and wild-type enzymes), printed column heads Purified Enzyme | Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the 3beta-HSD1 substrate block and Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the Isomerase2 substrate block. Table 5, enzyme row E192A, 3beta-HSD1 block; columns Km uM, kcat min^-1 and kcat/Km min^-1 uM^-1 of the 3beta-HSD1 block; Km cell = 30.4 uM; kcat cell = 1.8 min^-1; kcat/Km cell = 0.06.

raw_value_unit_evidence: Table 5, enzyme row E192A, 3beta-HSD1 block: Km = 30.4 uM; kcat = 1.8 min^-1; kcat/Km = 0.06 under the printed column head kcat/Km min^-1 uM^-1.


column_label: Table 6 (cofactor kinetics for the 3beta-HSD and isomerase activities of the purified mutant and wild-type enzymes), printed column heads Purified Enzyme | Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the NAD 3beta-HSD1 block and Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the NADH Isomerase2 block. Table 6, enzyme row D61N, NAD 3beta-HSD1 block; columns Km uM, kcat min^-1 and kcat/Km min^-1 uM^-1 of the NAD 3beta-HSD1 block; Km cell = 64.3 uM; kcat cell = 3.7 min^-1; kcat/Km cell = 0.06.

raw_value_unit_evidence: Table 6, enzyme row D61N, NAD 3beta-HSD1 block: Km = 64.3 uM; kcat = 3.7 min^-1; kcat/Km = 0.06 under the printed column head kcat/Km min^-1 uM^-1.


column_label: Table 6 (cofactor kinetics for the 3beta-HSD and isomerase activities of the purified mutant and wild-type enzymes), printed column heads Purified Enzyme | Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the NAD 3beta-HSD1 block and Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the NADH Isomerase2 block. Table 6, enzyme row E192A, NAD 3beta-HSD1 block; columns Km uM, kcat min^-1 and kcat/Km min^-1 uM^-1 of the NAD 3beta-HSD1 block; Km cell = 35.1 uM; kcat cell = 1.6 min^-1; kcat/Km cell = 0.05.

raw_value_unit_evidence: Table 6, enzyme row E192A, NAD 3beta-HSD1 block: Km = 35.1 uM; kcat = 1.6 min^-1; kcat/Km = 0.05 under the printed column head kcat/Km min^-1 uM^-1.


enzyme_display_name: 11-beta-hydroxysteroid dehydrogenase 1

enzyme: 11-beta-hydroxysteroid dehydrogenase 1


assay_conditions_summary: cofactor NADPH

column_label: PMID 14973125 Table II, Reduction of 7-ketocholesterol, Rat row, Km (nM) = 776 +/- 154.

normalized_value_unit_evidence: Km normalized_value=0.000776 mM.

raw_value_unit_evidence: Table II row Reduction of 7-ketocholesterol / Rat, Km column: 776 +/- 154 nM.

row_label: Reduction of 7-ketocholesterol / Rat


assay_conditions_summary: pH 7.8; 303.15 K; cofactor NAD+

proof_lines:
Bbg-3βHSD
dehydroepiandrosterone
Bufo gargarizans


substrate_name: pregnenolone

proof_lines:
Bbg-3βHSD
pregnenolone
Bufo gargarizans

substrate: pregnenolone


proof_lines:
kcat could not be accurately determined
pregnenolone


proof_lines:
second-order rate constants (kcat/Km)
dehydroepiandrosterone


organism: Mus musculus

column_label: Table 2 reports 7-Ketocholesterol / Reduction Km = 1269 +/- 282 uM.

raw_value_unit_evidence: Km raw_value=1269 uM raw_unit=uM

row_label: Recombinant protein / 7-Ketocholesterol / Reduction

table_label: PMC3694296 Table 2


assay_conditions_summary: cofactor NADP+

column_label: Table 2 reports Corticosterone / Oxidation Km = 1.78 +/- 0.56 uM.

raw_value_unit_evidence: Km raw_value=1.78 uM raw_unit=uM

row_label: Recombinant protein / Corticosterone / Oxidation


substrate_name: cortisol

substrate: cortisol


substrate_name: Cortisol

assay_conditions_summary: pH 9.2; 310.15 K; cofactor NADP+

column_label: Table II; Human row; cortisol columns Km, kcat, kcat/Km

row_label: Human; enzyme s, delta_tm; cortisol columns

table_label: Table II

substrate: Cortisol


assay_conditions_summary: pH 6; 310.15 K; cofactor NADPH

column_label: Table II; Human row; cortisone columns Km, kcat, kcat/Km

normalized_value_unit_evidence: Km 0.0008 mM; kcat 0.027 s^-1 after rounding; paper kcat_over_km 25.0 s^-1 mM^-1

row_label: Human; enzyme s, delta_tm; cortisone columns


substrate_name: dehydroepiandrosterone

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H156Y with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

substrate: dehydroepiandrosterone


organism: Saimiri sciureus


column_label: Table II; Guinea pig row; cortisone columns Km, kcat, kcat/Km

row_label: Guinea pig; enzyme s, delta_tm; cortisone columns


substrate_name: corticosterone

column_label: Table IV row 1F, Oxidation column group, Km column = 163 +/- 18 nM for corticosterone oxidation.

raw_value_unit_evidence: Km raw_value=163 raw_unit=nM

row_label: 1F; oxidation of corticosterone

table_label: Table IV


column_label: Table IV row 1F, Oxoreduction column group, Km column = 594 +/- 127 nM for 11-dehydrocorticosterone reduction.

raw_value_unit_evidence: Km raw_value=594 raw_unit=nM

row_label: 1F; oxoreduction of 11-dehydrocorticosterone


substrate_name: dihydrotestosterone (in the presence of NADH)

assay_conditions_summary: cofactor NADH

enzyme: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1


proof_lines:
11-oxygenated steroids
substrate efficiencies
Km values


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q105M with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


enzyme_display_name: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2


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

row_label: Reduction of 7-ketocholesterol / Human

column_label: Km

metric: Km

raw_unit: nM

normalized_unit: mM

assay_condition: Intact HEK-293 cells transiently expressing human recombinant 11beta-HSD1 in steroid-free medium; reduction of 7-ketocholesterol; data are mean +/- S.D. from at least four independent experiments; apparent Km calculated using the Eadie-Hofstee equation assuming first-order rate kinetics.


assay_conditions_summary: pH 6; cofactor NADPH

column_label: Results prose reports the Km for 11-DHC (11beta-reductase) was 120 +/- 10 nM in wild-type liver.

raw_value_unit_evidence: Km raw_value=120 +/- 10 nM raw_unit=nM

row_label: Wild-type mouse liver homogenate / 11-DHC (11beta-reductase)

table_label: Official PMC Results prose: 11beta-HSD-1 knockout liver 11-DHC reductase Km


column_label: PDF p.624 states 11beta-HSD1 catalysed reduction of 7-oxoLCA with apparent Km=980 +/- 210 nM.

normalized_value_unit_evidence: 980 nM converts to 0.00098 mM.

raw_value_unit_evidence: Results text reports apparent Km of 980 +/- 210 nM for 7-oxoLCA.

row_label: Human 11beta-HSD1 / 7-oxoLCA reduction

table_label: Biochemical Journal PDF p.624 Results / Figure 4 kinetic text


enzyme_display_name: UniProt A7A7R9

organism: Bifidobacterium adolescentis

assay_conditions_summary: pH 5

enzyme: UniProt A7A7R9


enzyme_display_name: 20alpha-hydroxysteroid dehydrogenase

organism: Tetrahymena thermophila

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

enzyme: 20alpha-hydroxysteroid dehydrogenase


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


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


substrate_name: ethyl acetoacetate

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

substrate: ethyl acetoacetate


substrate_name: acetoacetyl-CoA

assay_conditions_summary: cofactor CoA

substrate: acetoacetyl-CoA


substrate_name: ethyl pyruvate

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

substrate: ethyl pyruvate


substrate_name: ethyl 4-chloroacetoacetate

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

substrate: ethyl 4-chloroacetoacetate


substrate_name: isatin

substrate: isatin


substrate_name: methyl acetoacetate

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

substrate: methyl acetoacetate


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


substrate_name: ethyl 3-oxovalerate

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

substrate: ethyl 3-oxovalerate


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


substrate_name: acetoin

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

substrate: acetoin


substrate_name: ethyl benzoylacetate

substrate: ethyl benzoylacetate


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


substrate_name: D-glyceraldehyde

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

substrate: D-glyceraldehyde


substrate_name: D-Lactaldehyde

smiles: CC(C=O)O

substrate: D-Lactaldehyde


substrate_name: DL-glyceraldehyde 3-phosphate

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

substrate: DL-glyceraldehyde 3-phosphate


substrate_name: (S)-ethyl 3-hydroxybutyrate

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

substrate: (S)-ethyl 3-hydroxybutyrate


substrate_name: n-octyl acetoacetate

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

substrate: n-octyl acetoacetate


substrate_name: NADPH

substrate: NADPH


substrate_name: n-hexyl acetoacetate

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

substrate: n-hexyl acetoacetate


substrate_name: n-butyl acetoacetate

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

substrate: n-butyl acetoacetate


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


substrate_name: benzyl acetoacetate

substrate: benzyl acetoacetate


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


substrate_name: NADP+

substrate: NADP+


substrate_name: ethyl 2-methylacetoacetate

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

substrate: ethyl 2-methylacetoacetate


substrate_name: (S)-methyl 3-hydroxybutyrate

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

substrate: (S)-methyl 3-hydroxybutyrate


smiles: CC(C(C)O)O


enzyme_display_name: estradiol 17alpha-dehydrogenase

organism: Oryctolagus cuniculus

substrate_name: Epitestosterone

enzyme: estradiol 17alpha-dehydrogenase

substrate: Epitestosterone


substrate_name: 17alpha-estradiol 3-glucuronide

substrate: 17alpha-estradiol 3-glucuronide


organism: Chlorobaculum tepidum


substrate_name: sepiapterin

substrate: sepiapterin


substrate_name: diacetyl

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

substrate: diacetyl


organism: Eubacterium sp.


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


enzyme_display_name: ureidoglycolate dehydrogenase [NAD(P)+]

organism: Arthrobacter allantoicus

enzyme: ureidoglycolate dehydrogenase [NAD(P)+]


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


substrate_name: (R,S)-ureidoglycolate

substrate: (R,S)-ureidoglycolate


organism: Sus scrofa

assay_conditions_summary: 277.15 K; cofactor NADPH

proof_lines: 10 mM cysteine, at 4°C until activity decreases to half of the initial value


substrate_name: NADH

assay_conditions_summary: 277.15 K; cofactor NADH

substrate: NADH


enzyme_display_name: 21-hydroxysteroid dehydrogenase (NAD+)

organism: Ovis aries aries

proof_lines:
NAD dehydrogenase I
NAD dehydrogenase II

enzyme: 21-hydroxysteroid dehydrogenase (NAD+)


enzyme_display_name: 21-hydroxysteroid dehydrogenase (NADP+)

enzyme: 21-hydroxysteroid dehydrogenase (NADP+)


organism: Gallus gallus


organism: Equus caballus


proof_lines:
isozyme HSD-I
isozyme HSD-II


organism: Bos taurus


organism: Ovis aries

substrate_name: NADH; 21-Dehydrocortisone; H+

substrate: NADH; 21-Dehydrocortisone; H+


substrate_name: 21-Dehydrocortisone; H+; NADPH

substrate: 21-Dehydrocortisone; H+; NADPH


organism: Rattus norvegicus


substrate_name: D,L-glyceraldehyde

assay_conditions_summary: pH 6; 298.15 K; buffer and the printed 25 C; cofactor NADPH

column_label: Table 3 (Kinetic constants of 20alpha-HSD for endogenous steroids and aldose reductase substrates) prints a substrate column, a cofactor column and three numeric columns whose printed heads are kcat (min^-1), Km (uM) and kcat/Km (min^-1 uM^-1) in that order. The cited cell set is Table 3, substrate row D,L-Glyceraldehyde, cofactor NADPH: kcat (min^-1) = 12.9; Km (uM) = 120000; kcat/Km (min^-1 uM^-1) = 0.00011. The printed uncertainty of that row is kcat 12.9 +/- 0.3; the Km cell and the efficiency cell are printed with no uncertainty.

normalized_value_unit_evidence: kcat: printed Table 3 cell 12.9 min^-1; 12.9 / 60 = 0.215 s^(-1), and the catalog carries 0.215 s^(-1). Km: printed Table 3 cell 120000 uM; 120000 / 1000 = 120.0 mM, and the catalog carries 120.0 mM. kcat/Km: printed Table 3 cell 0.00011 min^-1 uM^-1; 1 min^-1 uM^-1 is (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 0.00011 x 16.666666666666668 = 0.0018333333333333335 s^(-1)*mM^(-1). The catalog carries the full-precision quotient of the two printed component cells, 0.215 / 120.0 = 0.0017916666666666667 s^(-1)*mM^(-1), and that quotient written to the five decimal places the printed efficiency column uses is 0.00011 min^-1 uM^-1, the printed cell itself, so the printed cell corroborates the held quotient at the paper's own precision.

raw_value_unit_evidence: Table 3, substrate row D,L-Glyceraldehyde, cofactor NADPH: kcat cell 12.9 in the column headed kcat, printed unit min^-1; Km cell 120000 in the column headed Km, printed unit uM; kcat/Km cell 0.00011 in the column headed kcat/Km, printed unit min^-1 uM^-1.

table_label: Table 3: Kinetic constants of 20alpha-HSD for endogenous steroids and aldose reductase substrates (Biochem. J. 1999, 341(Pt 3):853-859)

substrate: D,L-glyceraldehyde


assay_conditions_summary: pH 7.8; 298.15 K; buffer and the printed 25 C; cofactor NADP+

column_label: Table 3 (Kinetic constants of 20alpha-HSD for endogenous steroids and aldose reductase substrates) prints a substrate column, a cofactor column and three numeric columns whose printed heads are kcat (min^-1), Km (uM) and kcat/Km (min^-1 uM^-1) in that order. The cited cell set is Table 3, substrate row 20alpha-OH-5alpha-pregnan-3-one (CNS steroid), cofactor NADP+: kcat (min^-1) = 47.1; Km (uM) = 13.8; kcat/Km (min^-1 uM^-1) = 3.4. The printed uncertainties of that row are kcat 47.1 +/- 4.3 and Km 13.8 +/- 3.5; the efficiency cell is printed with no uncertainty, and the Results paragraph of the paper prints the same efficiency again in words as 3.4 min^-1 uM^-1 for 20alpha-hydroxy-5alpha-pregnan-3-one.

normalized_value_unit_evidence: kcat: printed Table 3 cell 47.1 min^-1; 47.1 / 60 = 0.785 s^(-1), the value the catalog already carries. Km: printed Table 3 cell 13.8 uM; 13.8 / 1000 = 0.0138 mM, and the catalog carries 0.013 mM, so the paper cell supplies 0.0138 mM. kcat/Km: printed Table 3 cell 3.4 min^-1 uM^-1; 1 min^-1 uM^-1 is (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 3.4 x 16.666666666666668 = 56.66666666666667 s^(-1)*mM^(-1), which the paper prints as its own efficiency cell and which this record adopts in place of the held 60.38461538461539 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row 20alpha-OH-5alpha-pregnan-3-one (CNS steroid), cofactor NADP+: kcat cell 47.1 in the column headed kcat, printed unit min^-1; Km cell 13.8 in the column headed Km, printed unit uM; kcat/Km cell 3.4 in the column headed kcat/Km, printed unit min^-1 uM^-1.


substrate_name: NADPH

assay_conditions_summary: pH 6.8; cofactor NADPH

substrate: NADPH


assay_conditions_summary: pH 6.8; cofactor NADP+


substrate_name: progesterone

substrate: progesterone


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature S157A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.4; buffer 50 mM phosphate; cofactor NADPH

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row S157A; columns Km Redox (uM), kcat Redox (min^-1) and kcat/Km Redox (min^-1 uM^-1); Km cell = 3.2 uM; kcat cell = 0.92 min^-1; kcat/Km cell = 0.29 under the printed column head kcat/Km Redox (min^-1 uM^-1). captured primary segment: 9,10-phenanthrenequinone | S157A hSPR, the site-directed S157A single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km Redox 3.2 uM | Table 5 kcat Redox 0.92 min^-1 | Table 5 kcat/Km Redox printed cell 0.29 under the column head kcat/Km Redox (min^-1 uM^-1) | redox cycling assayed with 9,10-phenanthrenequinone by quantifying the formation of H2O2 in 50 mM phosphate buffer, pH 7.8, with 0.2 mM NADPH

normalized_value_unit_evidence: Km: printed Km Redox cell 3.2 uM; 1 uM is 1/1000 mM, so 3.2 / 1000 = 0.0032 mM; the export stores 0.0032 mM. kcat: printed kcat Redox cell 0.92 min^-1; the printed turnover column is per MINUTE, so 0.92 / 60 = 0.015333333333333334 s^(-1); the export stores 0.0048 s^(-1). kcat/Km: printed kcat/Km Redox cell 0.29 under the column head kcat/Km Redox (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.29 x 16.666666666666668 = 4.833333333333333 s^-1 mM^-1; the export stores 1.4999999999999998 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row S157A, Redox columns: Km = 3.2 uM; kcat = 0.92 min^-1; kcat/Km = 0.29 under the printed column head kcat/Km Redox (min^-1 uM^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature N99A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.4; 310.15 K; buffer 100 mM potassium phosphate; cofactor NADPH

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row N99A; columns Km SPR (uM), kcat SPR (min^-1) and kcat/Km SPR (min^-1 uM^-1); Km cell = 94.1 uM; kcat cell = 3.3 min^-1; kcat/Km cell = 0.04 under the printed column head kcat/Km SPR (min^-1 uM^-1). captured primary segment: sepiapterin | N99A hSPR, the site-directed N99A single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km SPR 94.1 uM | Table 5 kcat SPR 3.3 min^-1 | Table 5 kcat/Km SPR printed cell 0.04 under the column head kcat/Km SPR (min^-1 uM^-1) | sepiapterin reduction assayed by formation of BH2 from sepiapterin by HPLC in 100 mM potassium phosphate buffer, pH 6.4, with 100 uM NADPH and 50 uM sepiapterin at 37 C

normalized_value_unit_evidence: Km: printed Km SPR cell 94.1 uM; 1 uM is 1/1000 mM, so 94.1 / 1000 = 0.0941 mM; the export stores 0.094 mM. kcat: printed kcat SPR cell 3.3 min^-1; the printed turnover column is per MINUTE, so 3.3 / 60 = 0.05499999999999999 s^(-1); the export stores 0.0053 s^(-1). kcat/Km: printed kcat/Km SPR cell 0.04 under the column head kcat/Km SPR (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.04 x 16.666666666666668 = 0.6666666666666667 s^-1 mM^-1; the export stores 0.05638297872340425 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row N99A, SPR columns: Km = 94.1 uM; kcat = 3.3 min^-1; kcat/Km = 0.04 under the printed column head kcat/Km SPR (min^-1 uM^-1).

row_label: Table 5, enzyme row N99A, SPR columns


column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row S157A; columns Km SPR (uM), kcat SPR (min^-1) and kcat/Km SPR (min^-1 uM^-1); Km cell = 50.3 uM; kcat cell = 3.5 min^-1; kcat/Km cell = 0.07 under the printed column head kcat/Km SPR (min^-1 uM^-1). captured primary segment: sepiapterin | S157A hSPR, the site-directed S157A single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km SPR 50.3 uM | Table 5 kcat SPR 3.5 min^-1 | Table 5 kcat/Km SPR printed cell 0.07 under the column head kcat/Km SPR (min^-1 uM^-1) | sepiapterin reduction assayed by formation of BH2 from sepiapterin by HPLC in 100 mM potassium phosphate buffer, pH 6.4, with 100 uM NADPH and 50 uM sepiapterin at 37 C

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row S157A, SPR columns: Km = 50.3 uM; kcat = 3.5 min^-1; kcat/Km = 0.07 under the printed column head kcat/Km SPR (min^-1 uM^-1).

row_label: Table 5, enzyme row S157A, SPR columns


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Δ257 to reconstruct the assayed variant sequence.

mutation_type: deletion


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature K174L to reconstruct the assayed variant sequence.

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row K174L; columns Km Redox (uM), kcat Redox (min^-1) and kcat/Km Redox (min^-1 uM^-1); Km cell = 27.7 uM; kcat cell = 1.79 min^-1; kcat/Km cell = 0.06 under the printed column head kcat/Km Redox (min^-1 uM^-1). captured primary segment: 9,10-phenanthrenequinone | K174L hSPR, the site-directed K174L single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km Redox 27.7 uM | Table 5 kcat Redox 1.79 min^-1 | Table 5 kcat/Km Redox printed cell 0.06 under the column head kcat/Km Redox (min^-1 uM^-1) | redox cycling assayed with 9,10-phenanthrenequinone by quantifying the formation of H2O2 in 50 mM phosphate buffer, pH 7.8, with 0.2 mM NADPH

normalized_value_unit_evidence: Km: printed Km Redox cell 27.7 uM; 1 uM is 1/1000 mM, so 27.7 / 1000 = 0.0277 mM; the export stores 0.027 mM. kcat: printed kcat Redox cell 1.79 min^-1; the printed turnover column is per MINUTE, so 1.79 / 60 = 0.029833333333333333 s^(-1); the export stores 0.027 s^(-1). kcat/Km: printed kcat/Km Redox cell 0.06 under the column head kcat/Km Redox (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.06 x 16.666666666666668 = 1.0 s^-1 mM^-1; the export stores 1.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row K174L, Redox columns: Km = 27.7 uM; kcat = 1.79 min^-1; kcat/Km = 0.06 under the printed column head kcat/Km Redox (min^-1 uM^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature G18D to reconstruct the assayed variant sequence.

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row G18D; columns Km Redox (uM), kcat Redox (min^-1) and kcat/Km Redox (min^-1 uM^-1); Km cell = 464.1 uM; kcat cell = 2.90 min^-1; kcat/Km cell = 0.01 under the printed column head kcat/Km Redox (min^-1 uM^-1). captured primary segment: 9,10-phenanthrenequinone | G18D hSPR, the site-directed G18D single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km Redox 464.1 uM | Table 5 kcat Redox 2.90 min^-1 | Table 5 kcat/Km Redox printed cell 0.01 under the column head kcat/Km Redox (min^-1 uM^-1) | redox cycling assayed with 9,10-phenanthrenequinone by quantifying the formation of H2O2 in 50 mM phosphate buffer, pH 7.8, with 0.2 mM NADPH

normalized_value_unit_evidence: Km: printed Km Redox cell 464.1 uM; 1 uM is 1/1000 mM, so 464.1 / 1000 = 0.4641 mM; the export stores 0.464 mM. kcat: printed kcat Redox cell 2.90 min^-1; the printed turnover column is per MINUTE, so 2.90 / 60 = 0.04833333333333333 s^(-1); the export stores 0.048 s^(-1). kcat/Km: printed kcat/Km Redox cell 0.01 under the column head kcat/Km Redox (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.01 x 16.666666666666668 = 0.16666666666666669 s^-1 mM^-1; the export stores 0.10344827586206896 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row G18D, Redox columns: Km = 464.1 uM; kcat = 2.90 min^-1; kcat/Km = 0.01 under the printed column head kcat/Km Redox (min^-1 uM^-1).

row_label: Table 5, enzyme row G18D, Redox columns


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature R42G to reconstruct the assayed variant sequence.

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row R42G; columns Km SPR (uM), kcat SPR (min^-1) and kcat/Km SPR (min^-1 uM^-1); Km cell = 45.7 uM; kcat cell = 3.2 min^-1; kcat/Km cell = 0.07 under the printed column head kcat/Km SPR (min^-1 uM^-1). captured primary segment: sepiapterin | R42G hSPR, the site-directed R42G single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km SPR 45.7 uM | Table 5 kcat SPR 3.2 min^-1 | Table 5 kcat/Km SPR printed cell 0.07 under the column head kcat/Km SPR (min^-1 uM^-1) | sepiapterin reduction assayed by formation of BH2 from sepiapterin by HPLC in 100 mM potassium phosphate buffer, pH 6.4, with 100 uM NADPH and 50 uM sepiapterin at 37 C

normalized_value_unit_evidence: Km: printed Km SPR cell 45.7 uM; 1 uM is 1/1000 mM, so 45.7 / 1000 = 0.0457 mM; the export stores 0.045 mM. kcat: printed kcat SPR cell 3.2 min^-1; the printed turnover column is per MINUTE, so 3.2 / 60 = 0.05333333333333334 s^(-1); the export stores 0.053 s^(-1). kcat/Km: printed kcat/Km SPR cell 0.07 under the column head kcat/Km SPR (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.07 x 16.666666666666668 = 1.166666666666667 s^-1 mM^-1; the export stores 1.1777777777777778 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row R42G, SPR columns: Km = 45.7 uM; kcat = 3.2 min^-1; kcat/Km = 0.07 under the printed column head kcat/Km SPR (min^-1 uM^-1).

row_label: Table 5, enzyme row R42G, SPR columns


column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row K174L; columns Km SPR (uM), kcat SPR (min^-1) and kcat/Km SPR (min^-1 uM^-1); Km cell = 169.8 uM; kcat cell = 5.4 min^-1; kcat/Km cell = 0.03 under the printed column head kcat/Km SPR (min^-1 uM^-1). captured primary segment: sepiapterin | K174L hSPR, the site-directed K174L single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km SPR 169.8 uM | Table 5 kcat SPR 5.4 min^-1 | Table 5 kcat/Km SPR printed cell 0.03 under the column head kcat/Km SPR (min^-1 uM^-1) | sepiapterin reduction assayed by formation of BH2 from sepiapterin by HPLC in 100 mM potassium phosphate buffer, pH 6.4, with 100 uM NADPH and 50 uM sepiapterin at 37 C

normalized_value_unit_evidence: Km: printed Km SPR cell 169.8 uM; 1 uM is 1/1000 mM, so 169.8 / 1000 = 0.1698 mM; the export stores 0.169 mM. kcat: printed kcat SPR cell 5.4 min^-1; the printed turnover column is per MINUTE, so 5.4 / 60 = 0.09000000000000001 s^(-1); the export stores 0.09 s^(-1). kcat/Km: printed kcat/Km SPR cell 0.03 under the column head kcat/Km SPR (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.03 x 16.666666666666668 = 0.5 s^-1 mM^-1; the export stores 0.5325443786982248 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row K174L, SPR columns: Km = 169.8 uM; kcat = 5.4 min^-1; kcat/Km = 0.03 under the printed column head kcat/Km SPR (min^-1 uM^-1).

row_label: Table 5, enzyme row K174L, SPR columns


column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row R42G; columns Km Redox (uM), kcat Redox (min^-1) and kcat/Km Redox (min^-1 uM^-1); Km cell = 50.1 uM; kcat cell = 5.90 min^-1; kcat/Km cell = 0.32 under the printed column head kcat/Km Redox (min^-1 uM^-1). captured primary segment: 9,10-phenanthrenequinone | R42G hSPR, the site-directed R42G single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km Redox 50.1 uM | Table 5 kcat Redox 5.90 min^-1 | Table 5 kcat/Km Redox printed cell 0.32 under the column head kcat/Km Redox (min^-1 uM^-1) | redox cycling assayed with 9,10-phenanthrenequinone by quantifying the formation of H2O2 in 50 mM phosphate buffer, pH 7.8, with 0.2 mM NADPH

normalized_value_unit_evidence: Km: printed Km Redox cell 50.1 uM; 1 uM is 1/1000 mM, so 50.1 / 1000 = 0.0501 mM; the export stores 0.0501 mM. kcat: printed kcat Redox cell 5.90 min^-1; the printed turnover column is per MINUTE, so 5.90 / 60 = 0.09833333333333334 s^(-1); the export stores 0.098 s^(-1). kcat/Km: printed kcat/Km Redox cell 0.32 under the column head kcat/Km Redox (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.32 x 16.666666666666668 = 5.333333333333334 s^-1 mM^-1; the export stores 1.9560878243512976 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row R42G, Redox columns: Km = 50.1 uM; kcat = 5.90 min^-1; kcat/Km = 0.32 under the printed column head kcat/Km Redox (min^-1 uM^-1).

row_label: Table 5, enzyme row R42G, Redox columns


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature D257H to reconstruct the assayed variant sequence.

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row D257H; columns Km Redox (uM), kcat Redox (min^-1) and kcat/Km Redox (min^-1 uM^-1); Km cell = 1.9 uM; kcat cell = 6.44 min^-1; kcat/Km cell = 3.39 under the printed column head kcat/Km Redox (min^-1 uM^-1). captured primary segment: 9,10-phenanthrenequinone | D257H hSPR, the site-directed D257H single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km Redox 1.9 uM | Table 5 kcat Redox 6.44 min^-1 | Table 5 kcat/Km Redox printed cell 3.39 under the column head kcat/Km Redox (min^-1 uM^-1) | redox cycling assayed with 9,10-phenanthrenequinone by quantifying the formation of H2O2 in 50 mM phosphate buffer, pH 7.8, with 0.2 mM NADPH

normalized_value_unit_evidence: Km: printed Km Redox cell 1.9 uM; 1 uM is 1/1000 mM, so 1.9 / 1000 = 0.0019 mM; the export stores 0.0019 mM. kcat: printed kcat Redox cell 6.44 min^-1; the printed turnover column is per MINUTE, so 6.44 / 60 = 0.10733333333333334 s^(-1); the export stores 0.107 s^(-1). kcat/Km: printed kcat/Km Redox cell 3.39 under the column head kcat/Km Redox (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 3.39 x 16.666666666666668 = 56.50000000000001 s^-1 mM^-1; the export stores 56.31578947368421 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row D257H, Redox columns: Km = 1.9 uM; kcat = 6.44 min^-1; kcat/Km = 3.39 under the printed column head kcat/Km Redox (min^-1 uM^-1).


column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row D257H; columns Km SPR (uM), kcat SPR (min^-1) and kcat/Km SPR (min^-1 uM^-1); Km cell = 60.6 uM; kcat cell = 9.4 min^-1; kcat/Km cell = 0.16 under the printed column head kcat/Km SPR (min^-1 uM^-1). captured primary segment: sepiapterin | D257H hSPR, the site-directed D257H single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km SPR 60.6 uM | Table 5 kcat SPR 9.4 min^-1 | Table 5 kcat/Km SPR printed cell 0.16 under the column head kcat/Km SPR (min^-1 uM^-1) | sepiapterin reduction assayed by formation of BH2 from sepiapterin by HPLC in 100 mM potassium phosphate buffer, pH 6.4, with 100 uM NADPH and 50 uM sepiapterin at 37 C

normalized_value_unit_evidence: Km: printed Km SPR cell 60.6 uM; 1 uM is 1/1000 mM, so 60.6 / 1000 = 0.0606 mM; the export stores 0.0606 mM. kcat: printed kcat SPR cell 9.4 min^-1; the printed turnover column is per MINUTE, so 9.4 / 60 = 0.15666666666666668 s^(-1); the export stores 0.156 s^(-1). kcat/Km: printed kcat/Km SPR cell 0.16 under the column head kcat/Km SPR (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.16 x 16.666666666666668 = 2.666666666666667 s^-1 mM^-1; the export stores 2.5742574257425743 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row D257H, SPR columns: Km = 60.6 uM; kcat = 9.4 min^-1; kcat/Km = 0.16 under the printed column head kcat/Km SPR (min^-1 uM^-1).

row_label: Table 5, enzyme row D257H, SPR columns


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature M205G to reconstruct the assayed variant sequence.

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row M205G; columns Km Redox (uM), kcat Redox (min^-1) and kcat/Km Redox (min^-1 uM^-1); Km cell = 13.4 uM; kcat cell = 13.45 min^-1; kcat/Km cell = 1.08 under the printed column head kcat/Km Redox (min^-1 uM^-1). captured primary segment: 9,10-phenanthrenequinone | M205G hSPR, the site-directed M205G single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km Redox 13.4 uM | Table 5 kcat Redox 13.45 min^-1 | Table 5 kcat/Km Redox printed cell 1.08 under the column head kcat/Km Redox (min^-1 uM^-1) | redox cycling assayed with 9,10-phenanthrenequinone by quantifying the formation of H2O2 in 50 mM phosphate buffer, pH 7.8, with 0.2 mM NADPH

normalized_value_unit_evidence: Km: printed Km Redox cell 13.4 uM; 1 uM is 1/1000 mM, so 13.4 / 1000 = 0.0134 mM; the export stores 0.0133 mM. kcat: printed kcat Redox cell 13.45 min^-1; the printed turnover column is per MINUTE, so 13.45 / 60 = 0.22416666666666665 s^(-1); the export stores 0.22 s^(-1). kcat/Km: printed kcat/Km Redox cell 1.08 under the column head kcat/Km Redox (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 1.08 x 16.666666666666668 = 18.000000000000004 s^-1 mM^-1; the export stores 16.54135338345865 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row M205G, Redox columns: Km = 13.4 uM; kcat = 13.45 min^-1; kcat/Km = 1.08 under the printed column head kcat/Km Redox (min^-1 uM^-1).


column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row N99A; columns Km Redox (uM), kcat Redox (min^-1) and kcat/Km Redox (min^-1 uM^-1); Km cell = 126.0 uM; kcat cell = 17.40 min^-1; kcat/Km cell = 0.14 under the printed column head kcat/Km Redox (min^-1 uM^-1). captured primary segment: 9,10-phenanthrenequinone | N99A hSPR, the site-directed N99A single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km Redox 126.0 uM | Table 5 kcat Redox 17.40 min^-1 | Table 5 kcat/Km Redox printed cell 0.14 under the column head kcat/Km Redox (min^-1 uM^-1) | redox cycling assayed with 9,10-phenanthrenequinone by quantifying the formation of H2O2 in 50 mM phosphate buffer, pH 7.8, with 0.2 mM NADPH

normalized_value_unit_evidence: Km: printed Km Redox cell 126.0 uM; 1 uM is 1/1000 mM, so 126.0 / 1000 = 0.126 mM; the export stores 0.126 mM. kcat: printed kcat Redox cell 17.40 min^-1; the printed turnover column is per MINUTE, so 17.40 / 60 = 0.29 s^(-1); the export stores 0.29 s^(-1). kcat/Km: printed kcat/Km Redox cell 0.14 under the column head kcat/Km Redox (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.14 x 16.666666666666668 = 2.333333333333334 s^-1 mM^-1; the export stores 2.3015873015873014 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row N99A, Redox columns: Km = 126.0 uM; kcat = 17.40 min^-1; kcat/Km = 0.14 under the printed column head kcat/Km Redox (min^-1 uM^-1).

row_label: Table 5, enzyme row N99A, Redox columns


column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row M205G; columns Km SPR (uM), kcat SPR (min^-1) and kcat/Km SPR (min^-1 uM^-1); Km cell = 133.8 uM; kcat cell = 25.7 min^-1; kcat/Km cell = 0.19 under the printed column head kcat/Km SPR (min^-1 uM^-1). captured primary segment: sepiapterin | M205G hSPR, the site-directed M205G single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km SPR 133.8 uM | Table 5 kcat SPR 25.7 min^-1 | Table 5 kcat/Km SPR printed cell 0.19 under the column head kcat/Km SPR (min^-1 uM^-1) | sepiapterin reduction assayed by formation of BH2 from sepiapterin by HPLC in 100 mM potassium phosphate buffer, pH 6.4, with 100 uM NADPH and 50 uM sepiapterin at 37 C

normalized_value_unit_evidence: Km: printed Km SPR cell 133.8 uM; 1 uM is 1/1000 mM, so 133.8 / 1000 = 0.1338 mM; the export stores 0.133 mM. kcat: printed kcat SPR cell 25.7 min^-1; the printed turnover column is per MINUTE, so 25.7 / 60 = 0.4283333333333333 s^(-1); the export stores 0.428 s^(-1). kcat/Km: printed kcat/Km SPR cell 0.19 under the column head kcat/Km SPR (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.19 x 16.666666666666668 = 3.166666666666667 s^-1 mM^-1; the export stores 3.2180451127819545 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row M205G, SPR columns: Km = 133.8 uM; kcat = 25.7 min^-1; kcat/Km = 0.19 under the printed column head kcat/Km SPR (min^-1 uM^-1).

row_label: Table 5, enzyme row M205G, SPR columns


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature Y259A to reconstruct the assayed variant sequence.

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row Y259A; columns Km SPR (uM), kcat SPR (min^-1) and kcat/Km SPR (min^-1 uM^-1); Km cell = 25.5 uM; kcat cell = 36.2 min^-1; kcat/Km cell = 1.42 under the printed column head kcat/Km SPR (min^-1 uM^-1). captured primary segment: sepiapterin | Y259A hSPR, the site-directed Y259A single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km SPR 25.5 uM | Table 5 kcat SPR 36.2 min^-1 | Table 5 kcat/Km SPR printed cell 1.42 under the column head kcat/Km SPR (min^-1 uM^-1) | sepiapterin reduction assayed by formation of BH2 from sepiapterin by HPLC in 100 mM potassium phosphate buffer, pH 6.4, with 100 uM NADPH and 50 uM sepiapterin at 37 C

normalized_value_unit_evidence: Km: printed Km SPR cell 25.5 uM; 1 uM is 1/1000 mM, so 25.5 / 1000 = 0.0255 mM; the export stores 0.025 mM. kcat: printed kcat SPR cell 36.2 min^-1; the printed turnover column is per MINUTE, so 36.2 / 60 = 0.6033333333333334 s^(-1); the export stores 0.6 s^(-1). kcat/Km: printed kcat/Km SPR cell 1.42 under the column head kcat/Km SPR (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 1.42 x 16.666666666666668 = 23.666666666666668 s^-1 mM^-1; the export stores 23.999999999999996 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row Y259A, SPR columns: Km = 25.5 uM; kcat = 36.2 min^-1; kcat/Km = 1.42 under the printed column head kcat/Km SPR (min^-1 uM^-1).

row_label: Table 5, enzyme row Y259A, SPR columns


column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row Y259A; columns Km Redox (uM), kcat Redox (min^-1) and kcat/Km Redox (min^-1 uM^-1); Km cell = 19.6 uM; kcat cell = 48.30 min^-1; kcat/Km cell = 2.46 under the printed column head kcat/Km Redox (min^-1 uM^-1). captured primary segment: 9,10-phenanthrenequinone | Y259A hSPR, the site-directed Y259A single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km Redox 19.6 uM | Table 5 kcat Redox 48.30 min^-1 | Table 5 kcat/Km Redox printed cell 2.46 under the column head kcat/Km Redox (min^-1 uM^-1) | redox cycling assayed with 9,10-phenanthrenequinone by quantifying the formation of H2O2 in 50 mM phosphate buffer, pH 7.8, with 0.2 mM NADPH

normalized_value_unit_evidence: Km: printed Km Redox cell 19.6 uM; 1 uM is 1/1000 mM, so 19.6 / 1000 = 0.0196 mM; the export stores 0.0196 mM. kcat: printed kcat Redox cell 48.30 min^-1; the printed turnover column is per MINUTE, so 48.30 / 60 = 0.8049999999999999 s^(-1); the export stores 0.805 s^(-1). kcat/Km: printed kcat/Km Redox cell 2.46 under the column head kcat/Km Redox (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 2.46 x 16.666666666666668 = 41.0 s^-1 mM^-1; the export stores 41.07142857142858 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row Y259A, Redox columns: Km = 19.6 uM; kcat = 48.30 min^-1; kcat/Km = 2.46 under the printed column head kcat/Km Redox (min^-1 uM^-1).


substrate_name: cortisol

proof_lines: pH 5.0, temperature not specified in the publication

substrate: cortisol


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


substrate_name: (S)-tetralol

substrate: (S)-tetralol


enzyme_display_name: UniProt Q04828

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

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

source_databases_merged: skid uniprot

enzyme: UniProt Q04828


enzyme_display_name: Aldo-keto reductase family 1 member C1

enzyme: Aldo-keto reductase family 1 member C1


organism: Tetrahymena pyriformis

sequence: LAKTVPLNDGTNFPIFGG

wild_type_sequence: LAKTVPLNDGTNFPIFGG

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: 20-oxo and 20alpha-hydroxy-steroids, pH 7.0


substrate_name: NADP+

assay_conditions_summary: pH 7; cofactor NADP+

substrate: NADP+


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; columns Km (uM), 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 catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 20alpha-Hydroxyprogesterone oxidation / AKR1C1: Km 14.7 uM; kcat 1.20 min^-1; kcat/Km 82 min^-1 mM^-1.


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)


substrate_name: testosterone (oxidation)

column_label: Table 3. Kinetic parameters for 17-ketosteroid reduction and 17beta-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Testosterone oxidation / AKR1C1 (R); columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 3. Kinetic parameters for 17-ketosteroid reduction and 17beta-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Testosterone oxidation / AKR1C1 (R): Km 39.8 uM; kcat 0.044 min^-1; kcat/Km 1.1 min^-1 mM^-1.

row_label: Testosterone oxidation / AKR1C1 (R)

substrate: testosterone (oxidation)


enzyme_display_name: Sepiapterin reductase

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 1.1 sec(-1) with sepiapterin as substrate (PubMed:10350607). kcat is 1.1 sec(-1) with NADPH as substrate (PubMed:10350607).

enzyme: Sepiapterin reductase


assay_conditions_summary: pH 7.5; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H222S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T307V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D309L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y305F with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E127D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H222I to reconstruct the assayed variant sequence.


substrate_name: dihydrotestosterone

substrate: dihydrotestosterone


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R304L with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


proof_lines: +/-0.4, A, B and C loop changed, totally converted enzyme

proof_lines: +/-0.4, A and C loop changed, bifunctional enzyme


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

assay_conditions_summary: pH 7


proof_lines:
pH 7.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7
Raw SKiD Env: Temp=25°C, pH=7.4

source_databases_merged: brenda skid uniprot


proof_lines: kcat is 9.7 sec(-1) with sepiapterin as substrate (PubMed:10350607). kcat is 11.1 sec(-1) with NADPH as substrate (PubMed:10350607).


proof_lines:
NADPH, intact cells
pH 7.0, 25°C
NADPH, cell homogenate


substrate_name: thionicotinamide adenine dinucleotide phosphate


substrate_name: 3-acetylpyridine adenine dinucleotide phosphate


organism: [Clostridium] scindens

sequence: AVKVAINGFGR

wild_type_sequence: AVKVAINGFGR

assay_conditions_summary: cofactor NADH


substrate_name: all-trans-retinal

assay_conditions_summary: pH 7.4; buffer 0.1 M potassium phosphate; cofactor NADPH

column_label: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone.; row label: all- trans -Retinal; columns: Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone. row all- trans -Retinal reports Km=8.9 uM, kcat=0.51 min^-1, and kcat/Km=0.057 min^-1 uM^-1.

row_label: all- trans -Retinal

substrate: all-trans-retinal


smiles: CCCCCC(C=CC=O)O

column_label: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone.; row label: 4-Hydroxy-2-nonenal; columns: Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone. row 4-Hydroxy-2-nonenal reports Km=5.3 uM, kcat=0.52 min^-1, and kcat/Km=0.098 min^-1 uM^-1.


column_label: Table 2. Kinetic Constants for Hydroxysteroids and Other Alcohols Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) 17β-Hydroxysteroids 5β-Androstane-3α,17β-diol 1.4 15 11 5α-Androstane-3α,17β-diol 4.2 16 3.8 5-Androstene-3β,17β-diol 3.1 6.0 1.9 5β-Androstan-17β-ol-3-one 6.2 9.2 1.5 5α-Androstane-3β,17β-diol 2.2 1.9 0.86 5β-Androstane-3β,17β-diol 2.5 2.0 0.80 Testosterone 13 3.4 0.26 17β-Estradiol 1.3 0.67 0.52 5α-Dihydrotestosterone 18 2.8 0.16 20α-Hydroxysteroids 5β-Pregnane-3α,20α-diol 7.8 17 2.2 5α-Pregnane-3α,20α-diol 0.8 1.5 1.8 5β-Pregnan-20α-ol-3-one 5.7 9.2 1.6 20α-Hydroxyprogesterone 2.2 2.9 1.3 5α-Pregnan-20α-ol-3-one 11 9.5 0.86 Non-steroidal alcohols β-Ionol 18 14 0.61 ( S )-1-Tetralol 112 13 0.12 ( S )-1-Indanol 131 12 0.092 4-Chromanol 152 4.1 0.027 trans -Benzene dihydrodiol 260 6.5 0.025 Geraniol 180 2.0 0.011; row label: 17β-Estradiol; columns: Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table 2. Kinetic Constants for Hydroxysteroids and Other Alcohols Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) 17β-Hydroxysteroids 5β-Androstane-3α,17β-diol 1.4 15 11 5α-Androstane-3α,17β-diol 4.2 16 3.8 5-Androstene-3β,17β-diol 3.1 6.0 1.9 5β-Androstan-17β-ol-3-one 6.2 9.2 1.5 5α-Androstane-3β,17β-diol 2.2 1.9 0.86 5β-Androstane-3β,17β-diol 2.5 2.0 0.80 Testosterone 13 3.4 0.26 17β-Estradiol 1.3 0.67 0.52 5α-Dihydrotestosterone 18 2.8 0.16 20α-Hydroxysteroids 5β-Pregnane-3α,20α-diol 7.8 17 2.2 5α-Pregnane-3α,20α-diol 0.8 1.5 1.8 5β-Pregnan-20α-ol-3-one 5.7 9.2 1.6 20α-Hydroxyprogesterone 2.2 2.9 1.3 5α-Pregnan-20α-ol-3-one 11 9.5 0.86 Non-steroidal alcohols β-Ionol 18 14 0.61 ( S )-1-Tetralol 112 13 0.12 ( S )-1-Indanol 131 12 0.092 4-Chromanol 152 4.1 0.027 trans -Benzene dihydrodiol 260 6.5 0.025 Geraniol 180 2.0 0.011 row 17β-Estradiol reports Km=1.3 uM, kcat=0.67 min^-1, and kcat/Km=0.52 min^-1 uM^-1.


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

column_label: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone.; row label: 4-Oxo-2-hexenal; columns: Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone. row 4-Oxo-2-hexenal reports Km=5.9 uM, kcat=0.69 min^-1, and kcat/Km=0.11 min^-1 uM^-1.