enzyme_display_name: 3alpha-hydroxy bile acid-CoA-ester 3-dehydrogenase 1/3

proof_lines: kcat is 74 min(-1) with choloyl-CoA as substrate. kcat is 49 min(-1) with chenodeoxycholoyl-CoA as substrate. kcat is 44 min(-1) with lithocholoyl-CoA as substrate. kcat is 52 min(-1) with deoxycholoyl-CoA as substrate. kcat is 33 min(-1) w

substrate: choloyl-CoA (at pH 8.7 and 37 degrees Celsius)


organism: Clostridium scindens (strain JCM 10418 / VPI 12708)

substrate_name: chenodeoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius)

source_db: uniprot

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 8.7; cofactor CoA

data_origin: experimental

enzyme: 3alpha-hydroxy bile acid-CoA-ester 3-dehydrogenase 1/3

status: unverified

source: uniprot


substrate_name: lithocholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: deoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: 3-oxocholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: 3-oxochenodeoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: 3-oxolithocholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: 3-oxodeoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: NAD(+) (at pH 8.7 and 37 degrees Celsius)


substrate_name: NADP(+) (at pH 8.7 and 37 degrees Celsius)


organism: Actinomadura kijaniata

substrate_name: dTDP-glucose

proof_lines: kcat is 6.24 sec(-1) for dTDP-glucose as substrate.

substrate: dTDP-glucose


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


enzyme_display_name: D-3-phosphoglycerate dehydrogenase

organism: Escherichia coli (strain K12)

proof_lines: kcat is 0.55 sec(-1) for 3-phospho-D-glycerate oxidation. kcat is 27.8 sec(-1) for 3-phosphonooxypyruvate reduction. kcat is 33.3 sec(-1) for 2-oxoglutarate reduction. kcat is 0.71 sec(-1) for (R)-2-hydroxyglutarate oxidation. kcat is 0.25

enzyme: D-3-phosphoglycerate dehydrogenase


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


organism: Homo sapiens

proof_lines: kcat is 4.5 min(-1) for 3-phosphoglycerate oxidation. kcat is 10.6 min(-1) for oxaloacetate reduction. kcat is 4.7 min(-1) for 2-oxoglutarate reduction.


substrate_name: oxaloacetate

substrate: oxaloacetate


substrate_name: NAD(+)

substrate: NAD(+)


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


enzyme_display_name: 3alpha-hydroxysteroid dehydrogenase

organism: Mediterraneibacter gnavus (strain ATCC 29149 / DSM 114966 / JCM 6515 / VPI C7-9)

substrate_name: deoxycholate

proof_lines: kcat is 99.3 min(-1) with deoxycholate as substrate.

enzyme: 3alpha-hydroxysteroid dehydrogenase

substrate: deoxycholate


enzyme_display_name: 3beta-hydroxysteroid dehydrogenase

proof_lines: kcat is 9430 min(-1) with 12alpha-hydroxy-3-oxo-5beta-cholan-24-oate as substrate.

enzyme: 3beta-hydroxysteroid dehydrogenase


enzyme_display_name: D-3-phosphoglycerate dehydrogenase 1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

verification_status: verified

column_label: Table 3. Kinetic properties of the alpha-ketoglutarate reductase activity of Ser3 and Ser33, Table 3 / Ser3: Km=49 uM.

raw_value_unit_evidence: Km=49 uM

row_label: Table 3 / Ser3

enzyme: D-3-phosphoglycerate dehydrogenase 1

status: verified


enzyme_display_name: D-3-phosphoglycerate dehydrogenase 2

column_label: Table 3. Kinetic properties of the alpha-ketoglutarate reductase activity of Ser3 and Ser33, Table 3 / Ser33: Km=54 uM.

raw_value_unit_evidence: Km=54 uM

row_label: Table 3 / Ser33

enzyme: D-3-phosphoglycerate dehydrogenase 2


enzyme_display_name: (R)-2-hydroxyglutarate dehydrogenase

organism: Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4)

enzyme: (R)-2-hydroxyglutarate dehydrogenase


enzyme_display_name: 3alpha-hydroxybile acid CoA 3-dehydrogenase

organism: [Clostridium] scindens

substrate_name: lithocholoyl-CoA

source_db: oed

verification_status: corrected

assay_conditions_summary: pH 8.7; 310.15 K; cofactor CoA

column_label: Table II; row BaiA1 / LC-CoA; columns BaiA1 kcat, KM, kcat/KM report kcat 44, KM 22, and kcat/KM 2.000.

raw_value_unit_evidence: Table II BaiA1 / LC-CoA: kcat = 44 min^-1; KM = 22 uM; kcat/KM = 2.000 uM^-1 min^-1

row_label: BaiA1 / LC-CoA

table_label: Table II

substrate: lithocholoyl-CoA

status: corrected

source: oed


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P19337 and applied mutation signature E42A to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 8.7; 310.15 K; cofactor NAD+

column_label: Table IV; row BaiA2_E42A / NAD+; columns BaiA2_E42A kcat, KM, kcat/KM report kcat 19, KM 17, and kcat/KM 1.11.

raw_value_unit_evidence: Table IV BaiA2_E42A / NAD+: kcat = 19 min^-1; KM = 17 uM; kcat/KM = 1.11 uM^-1 min^-1

row_label: BaiA2_E42A / NAD+

table_label: Table IV

enzyme: 3alpha-hydroxybile acid CoA 3-dehydrogenase

substrate: NAD+


column_label: Table IV; row BaiA1 / NAD+; columns BaiA1 kcat, KM, kcat/KM report kcat 18, KM 17, and kcat/KM 1.06.

raw_value_unit_evidence: Table IV BaiA1 / NAD+: kcat = 18 min^-1; KM = 17 uM; kcat/KM = 1.06 uM^-1 min^-1

row_label: BaiA1 / NAD+


substrate_name: NADP+

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E42A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.7; 310.15 K; cofactor NADP+

substrate: NADP+


column_label: Table IV; row BaiA1 / NADP+; columns BaiA1 kcat, KM, kcat/KM report kcat 6.8, KM 883, and kcat/KM 0.008.

raw_value_unit_evidence: Table IV BaiA1 / NADP+: kcat = 6.8 min^-1; KM = 883 uM; kcat/KM = 0.008 uM^-1 min^-1

row_label: BaiA1 / NADP+


substrate_name: taurocholic acid

column_label: Table II; row BaiA1 / TCA; columns BaiA1 kcat, KM, kcat/KM report kcat 24, KM 329, and kcat/KM 0.073.

raw_value_unit_evidence: Table II BaiA1 / TCA: kcat = 24 min^-1; KM = 329 uM; kcat/KM = 0.073 uM^-1 min^-1

row_label: BaiA1 / TCA

substrate: taurocholic acid


enzyme_display_name: eugenol synthase

organism: Ocimum basilicum

substrate_name: coniferyl acetate

source_db: brenda

sequence_source: multiple

source_databases_merged: brenda uniprot

enzyme: eugenol synthase

substrate: coniferyl acetate

source: brenda


assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADPH

column_label: Package PDF/text Table 2 row ObaIEGS, substrate Coniferyl acetate, columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Km 0.7 mM; kcat 0.23 min^-1; kcat/Km 0.33 mM^-1 min^-1; paper exact kcat/Km=0.33 mM^-1 min^-1

row_label: ObaIEGS / Coniferyl acetate

table_label: Table 2, Values of kinetic parameters for four recombinant EGS


column_label: Table II; row BaiA1 / 3-oxo-CDC-CoA; columns BaiA1 kcat, KM, kcat/KM report kcat 24, KM 3.3, and kcat/KM 7.230.

raw_value_unit_evidence: Table II BaiA1 / 3-oxo-CDC-CoA: kcat = 24 min^-1; KM = 3.3 uM; kcat/KM = 7.230 uM^-1 min^-1

row_label: BaiA1 / 3-oxo-CDC-CoA


column_label: Table II; row BaiA1 / 3-oxo-C-CoA; columns BaiA1 kcat, KM, kcat/KM report kcat 33, KM 9.1, and kcat/KM 3.626.

raw_value_unit_evidence: Table II BaiA1 / 3-oxo-C-CoA: kcat = 33 min^-1; KM = 9.1 uM; kcat/KM = 3.626 uM^-1 min^-1

row_label: BaiA1 / 3-oxo-C-CoA


column_label: Table II; row BaiA1 / 3-oxo-DC-CoA; columns BaiA1 kcat, KM, kcat/KM report kcat 44, KM 5.6, and kcat/KM 7.860.

raw_value_unit_evidence: Table II BaiA1 / 3-oxo-DC-CoA: kcat = 44 min^-1; KM = 5.6 uM; kcat/KM = 7.860 uM^-1 min^-1

row_label: BaiA1 / 3-oxo-DC-CoA


column_label: Table II; row BaiA1 / 3-oxo-LC-CoA; columns BaiA1 kcat, KM, kcat/KM report kcat 42, KM 8.3, and kcat/KM 5.060.

raw_value_unit_evidence: Table II BaiA1 / 3-oxo-LC-CoA: kcat = 42 min^-1; KM = 8.3 uM; kcat/KM = 5.060 uM^-1 min^-1

row_label: BaiA1 / 3-oxo-LC-CoA


substrate_name: chenodeoxycholic acid

column_label: Table II, CDCA row under BaiA1 columns reports kcat 15, KM 555, and kcat/KM 0.027.

raw_value_unit_evidence: Table II BaiA1 row CDCA: kcat = 15 min^-1; KM = 555 uM; kcat/KM = 0.027 uM^-1 min^-1

row_label: BaiA1 / CDCA

substrate: chenodeoxycholic acid


substrate_name: chenodeoxycholoyl-CoA

column_label: Table II; row BaiA1 / CDC-CoA; columns BaiA1 kcat, KM, kcat/KM report kcat 49, KM 53, and kcat/KM 0.925.

raw_value_unit_evidence: Table II BaiA1 / CDC-CoA: kcat = 49 min^-1; KM = 53 uM; kcat/KM = 0.925 uM^-1 min^-1

row_label: BaiA1 / CDC-CoA

substrate: chenodeoxycholoyl-CoA


substrate_name: cholic acid

column_label: Table II, CA row under BaiA1 columns reports kcat 16, KM 1158, and kcat/KM 0.014.

raw_value_unit_evidence: Table II BaiA1 row CA: kcat = 16 min^-1; KM = 1158 uM; kcat/KM = 0.014 uM^-1 min^-1

row_label: BaiA1 / CA

substrate: cholic acid


substrate_name: choloyl-CoA

column_label: Table II, C-CoA row under BaiA1 columns reports kcat 74, KM 106, and kcat/KM 0.698.

raw_value_unit_evidence: Table II BaiA1 row C-CoA: kcat = 74 min^-1; KM = 106 uM; kcat/KM = 0.698 uM^-1 min^-1

row_label: BaiA1 / C-CoA

substrate: choloyl-CoA


substrate_name: deoxycholoyl-CoA

column_label: Table II; row BaiA1 / DC-CoA; columns BaiA1 kcat, KM, kcat/KM report kcat 52, KM 16, and kcat/KM 3.250.

raw_value_unit_evidence: Table II BaiA1 / DC-CoA: kcat = 52 min^-1; KM = 16 uM; kcat/KM = 3.250 uM^-1 min^-1

row_label: BaiA1 / DC-CoA

substrate: deoxycholoyl-CoA


substrate_name: glycocholic acid

column_label: Table II; row BaiA1 / GCA; columns BaiA1 kcat, KM, kcat/KM report kcat 25, KM 383, and kcat/KM 0.065.

raw_value_unit_evidence: Table II BaiA1 / GCA: kcat = 25 min^-1; KM = 383 uM; kcat/KM = 0.065 uM^-1 min^-1

row_label: BaiA1 / GCA

substrate: glycocholic acid


organism: Ocimum tenuiflorum

substrate_name: 4-coumaryl acetate

column_label: Package PDF/text Table 2 row OtIEGS, substrate Coumaryl acetate, columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Km 1.7 mM; kcat 0.8 min^-1; kcat/Km 0.47 mM^-1 min^-1; paper exact kcat/Km=0.47 mM^-1 min^-1

row_label: OtIEGS / Coumaryl acetate

substrate: 4-coumaryl acetate


column_label: Package PDF/text Table 2 row OtIEGS, substrate Coniferyl acetate, columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Km 1.17 mM; kcat 1.68 min^-1; kcat/Km 1.44 mM^-1 min^-1; paper exact kcat/Km=1.44 mM^-1 min^-1

row_label: OtIEGS / Coniferyl acetate


organism: Ocimum gratissimum

column_label: Package PDF/text Table 2 row OgIEGS, substrate Coumaryl acetate, columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Km 1.25 mM; kcat 0.2017 min^-1; kcat/Km 0.16 mM^-1 min^-1; paper exact kcat/Km=0.16 mM^-1 min^-1

row_label: OgIEGS / Coumaryl acetate


column_label: Package PDF/text Table 2 row OgIEGS, substrate Coniferyl acetate, columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Km 0.5 mM; kcat 0.68 min^-1; kcat/Km 1.36 mM^-1 min^-1; paper exact kcat/Km=1.36 mM^-1 min^-1

row_label: OgIEGS / Coniferyl acetate


organism: Ocimum kilimandscharicum

column_label: Package PDF/text Table 2 row OkEGS, substrate Coumaryl acetate, columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Km 0.55 mM; kcat 0.63 min^-1; kcat/Km 1.15 mM^-1 min^-1; paper exact kcat/Km=1.15 mM^-1 min^-1

row_label: OkEGS / Coumaryl acetate


column_label: Package PDF/text Table 2 row OkEGS, substrate Coniferyl acetate, columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Km 0.41 mM; kcat 0.18 min^-1; kcat/Km 0.44 mM^-1 min^-1; paper exact kcat/Km=0.44 mM^-1 min^-1

row_label: OkEGS / Coniferyl acetate


enzyme_display_name: isoeugenol synthase

organism: Pimpinella anisum

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

column_label: Table II, AIS1 row, Coumaryl acetate: Km column 134.9 +/- 36.4 uM; kcat column 0.07 +/- 0.01 s^-1; kcat/Km column 0.52 s^-1 mM^-1; footnote a = averages of three independent experiments +/- SE.

row_label: AIS1 / Coumaryl acetate

table_label: Table II - Kinetic parameters of AIS1 and AIMT1

enzyme: isoeugenol synthase


column_label: Table II, AIS1 row, Coniferyl acetate: Km column 229.9 +/- 46.2 uM; kcat column 1.02 +/- 0.17 s^-1; kcat/Km column 4.44 s^-1 mM^-1; footnote a = averages of three independent experiments +/- SE.

row_label: AIS1 / Coniferyl acetate


enzyme_display_name: Chanoclavine-I dehydrogenase easD

organism: Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371)

substrate_name: chanoclavine-I

assay_conditions_summary: cofactor NAD+

column_label: The abstract reports Km values for chanoclavine-I and NAD+ were 0.09 and 0.36 mM, respectively.

raw_value_unit_evidence: Km raw_value=0.09 mM raw_unit=mM

row_label: Prose segment: chanoclavine-I Km

table_label: PubMed PMID 22403186 abstract

enzyme: Chanoclavine-I dehydrogenase easD

substrate: chanoclavine-I


raw_value_unit_evidence: Km raw_value=0.36 mM raw_unit=mM

row_label: Prose segment: NAD+ Km


organism: Daucus carota subsp. sativus

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH


substrate_name: NADPH

substrate: NADPH


enzyme_display_name: chanoclavine-I dehydrogenase

organism: Aspergillus fumigatus

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

enzyme: chanoclavine-I dehydrogenase


substrate_name: Chanoclavine-I

substrate: Chanoclavine-I


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+


organism: Staphylococcus aureus

substrate_name: D-Ribulose 5-phosphate; NADPH; H+

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

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

substrate: D-Ribulose 5-phosphate; NADPH; H+


substrate_name: D-Ribulose 5-phosphate

substrate: D-Ribulose 5-phosphate


assay_conditions_summary: pH 7.2; 295.15 K; cofactor NADPH


enzyme_display_name: Bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase Bcs1

organism: Haemophilus influenzae

substrate_name: D-ribulose 5-phosphate

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

proof_lines: kcat is 22 sec(-1) for the reductase reaction. kcat is 13 sec(-1) for the cytidyltransferase reaction.

substrate: D-ribulose 5-phosphate


enzyme: Bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase Bcs1


substrate_name: D-ribitol 5-phosphate (for the cytidylyltransferase reaction)

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


substrate_name: CTP

substrate: CTP


organism: Chromobacterium violaceum


substrate_name: UDP-alpha-D-glucuronate

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

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

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

table_label: Table 3 Kinetic Parameters

substrate: UDP-alpha-D-glucuronate


enzyme_display_name: tetrachlorobenzoquinone reductase

organism: Sphingobium chlorophenolicum

assay_conditions_summary: pH 7.6; cofactor NADPH

proof_lines: kcat is 20.1 sec(-1) for NADH as substrate (with 90 uM cytochrome c). kcat is 14.1 sec(-1) for 2,6-dichloroindophenol (DCIP) as substrate (with 100 uM NADH). kcat is 9.1 sec(-1) for cytochrome c as substrate (with 100 uM NADH). kcat is 3.7

enzyme: tetrachlorobenzoquinone reductase


substrate_name: NADH

assay_conditions_summary: pH 7.6; cofactor NADH

substrate: NADH


enzyme_display_name: D-threitol dehydrogenase

organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate_name: D-threitol

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

proof_lines: kcat is 6.97 sec(-1) with D-threitol as substrate. kcat is 0.71 sec(-1) with D-threose as substrate. kcat is 7.32 sec(-1) with D-erythrulose as substrate.

enzyme: D-threitol dehydrogenase

substrate: D-threitol


substrate_name: D-threose

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

substrate: D-threose


substrate_name: D-erythrulose

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

substrate: D-erythrulose


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

substrate_name: UDP-GlcNAcA

column_label: Table 3 reports the P. aeruginosa row with Km (mM) UDP-GlcNAcA = 0.25 +/- 0.01 mM.

raw_value_unit_evidence: Km raw_value=0.25 +/- 0.01 raw_unit=mM

row_label: P. aeruginosa WlbA enzyme

table_label: PMID 20690587 Table 3, Kinetic Parameters

substrate: UDP-GlcNAcA


column_label: Table 3 reports the P. aeruginosa row with Km (mM) alpha-ketoglutarate = 1.35 +/- 0.10 mM.

raw_value_unit_evidence: Km raw_value=1.35 +/- 0.10 raw_unit=mM


organism: Sphingomonas sp.

assay_conditions_summary: pH 8

proof_lines: kcat is 51.8 min(-1) with 2-dehydro-3-deoxy-L-rhamnonate as substrate. kcat is 11 min(-1) with 2-dehydro-3-deoxy-L-lyxonate as substrate. kcat is 0.72 min(-1) with 2-dehydro-3-deoxy-L-mannonate as substrate.


enzyme_display_name: Ribulose-5-phosphate reductase

organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

enzyme: Ribulose-5-phosphate reductase


enzyme_display_name: D-altritol 5-dehydrogenase

organism: Agrobacterium fabrum

substrate_name: D-altritol

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

assay_conditions_summary: pH 9

enzyme: D-altritol 5-dehydrogenase

substrate: D-altritol


organism: Cereibacter sphaeroides

substrate_name: galactitol

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

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

source_databases_merged: brenda skid uniprot

substrate: galactitol


substrate_name: NAD+

substrate: NAD+


smiles: CCCCC(CO)O

assay_conditions_summary: pH 6.5; cofactor NAD+

column_label: Official article text lists apparent Km values and gives 1,2-hexandiol as 0-2 mM.

raw_value_unit_evidence: Km raw_value=0-2 raw_unit=mM

row_label: Rhodobacter sphaeroides D galactitol dehydrogenase with 1,2-hexanediol (paper spelling: 1,2-hexandiol)

table_label: Microbiology Society official article abstract/full-text summary, PMID 7551050


substrate_name: dihydroxyacetone

smiles: CC(=O)CO

substrate: dihydroxyacetone


substrate_name: acetoin

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

substrate: acetoin


substrate_name: L-erythrulose

substrate: L-erythrulose


enzyme_display_name: Bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase Acs1

substrate_name: D-ribulose 5-phosphate (in the presence of 50 uM CTP)

column_label: HTML prose names Km for ribulose 5-phosphate under 50 uM CTP condition

raw_value_unit_evidence: 50 uM with 50 uM CTP

row_label: CTP addition decreases ribulose 5-phosphate Km from 400 to 50 uM

table_label: PMC HTML Results section: Characterization and kinetic properties of Acs1 (prose)


substrate_name: NADPH

enzyme: Bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase Acs1

substrate: NADPH


assay_conditions_summary: cofactor NADP+

column_label: HTML prose names Km for ribitol 5-phosphate under pyrophosphorylase activity

raw_value_unit_evidence: 37 uM

row_label: Km for ribitol 5-phosphate reported as 37 uM

substrate: D-ribitol 5-phosphate (for the cytidylyltransferase reaction)


column_label: HTML prose names Km for CTP; UTP replacement reported inactive

row_label: Km for CTP reported as 150 uM


smiles: C(CCO)CC(CO)O

proof_lines: Also (S)-1,2,6-hexanetriol was oxidized by GDH


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

proof_lines: The diketone 2,3-hexanedione was only reduced


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


smiles: CCC(=O)CO

proof_lines: Reduction of hydroxyacetone or 1-hydroxy-2-butanone


smiles: CCC(CO)O

proof_lines: The oxidation of 1,2-butanediol occurred highly specific


smiles: CC(CO)O


substrate_name: Hydroxyacetone

substrate: Hydroxyacetone


substrate_name: D-Arabinose 5-phosphate

column_label: PDF page 4 Table 1 lists D-arabinose 5-phosphate under reductase: Km 3000 +/- 570 uM; kcat 2.3 +/- 0.3 s^-1; kcat/Km 0.0077 x10^5 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=2.3 normalized_unit=s^-1; Km normalized_value=3.0 normalized_unit=mM; kcat/Km normalized_value=0.7666666666666666 normalized_unit=s^-1*mM^-1 from the same table kcat and Km cells; printed table specificity constant is 0.0077 x10^5 M^-1 s^-1.

raw_value_unit_evidence: Table 1 D-arabinose 5-phosphate cells: Km raw_value=3000 +/- 570 raw_unit=uM; kcat raw_value=2.3 +/- 0.3 raw_unit=s^-1; kcat/Km raw_value=0.0077 raw_unit=x10^5 M^-1 s^-1.

row_label: (1) reductase / D-arabinose 5-phosphate

table_label: Table 1: Steady State Kinetic Parameters Describing Substrate Specificity of Reductase and Cytidylyltransferase Activities of Bcs1

substrate: D-Arabinose 5-phosphate


substrate_name: D-Ribose 5-phosphate

column_label: PDF page 4 Table 1 lists D-ribose 5-phosphate under reductase: Km 2200 +/- 280 uM; kcat 4.1 +/- 0.3 s^-1; kcat/Km 0.019 x10^5 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=4.1 normalized_unit=s^-1; Km normalized_value=2.2 normalized_unit=mM; kcat/Km normalized_value=1.8636363636363633 normalized_unit=s^-1*mM^-1 from the same table kcat and Km cells; printed table specificity constant is 0.019 x10^5 M^-1 s^-1.

raw_value_unit_evidence: Table 1 D-ribose 5-phosphate cells: Km raw_value=2200 +/- 280 raw_unit=uM; kcat raw_value=4.1 +/- 0.3 raw_unit=s^-1; kcat/Km raw_value=0.019 raw_unit=x10^5 M^-1 s^-1.

row_label: (1) reductase / D-ribose 5-phosphate

substrate: D-Ribose 5-phosphate


substrate_name: D-Ribulose

column_label: PDF page 4 Table 1 lists D-ribulose under reductase: Km 1100 +/- 180 uM; kcat 3.6 +/- 0.3 s^-1; kcat/Km 0.033 x10^5 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=3.6 normalized_unit=s^-1; Km normalized_value=1.1 normalized_unit=mM; kcat/Km normalized_value=3.2727272727272725 normalized_unit=s^-1*mM^-1 from the same table kcat and Km cells; printed table specificity constant is 0.033 x10^5 M^-1 s^-1.

raw_value_unit_evidence: Table 1 D-ribulose cells: Km raw_value=1100 +/- 180 raw_unit=uM; kcat raw_value=3.6 +/- 0.3 raw_unit=s^-1; kcat/Km raw_value=0.033 raw_unit=x10^5 M^-1 s^-1.

row_label: (1) reductase / D-ribulose

substrate: D-Ribulose


substrate_name: D-Ribulose 5-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K386A to reconstruct the assayed variant sequence.

substrate: D-Ribulose 5-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R18A to reconstruct the assayed variant sequence.


column_label: Table 1; reductase block; row D-ribulose 5-phosphate; columns Kma, kcata, kcat/Km.

normalized_value_unit_evidence: Km paper=0.076 mM; kcat paper=22 s^-1; kcat/Km paper=290 s^-1 mM^-1; export kcat=26.0 and kcat/Km=342.10526315789474.

row_label: D-ribulose 5-phosphate

table_label: Table 1. Steady State Kinetic Parameters Describing Substrate Specificity of Reductase and Cytidylyltransferase Activities of Bcs1


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADPH


column_label: Table 1; reductase block; row NADPH; columns Kma, kcata, kcat/Km.

normalized_value_unit_evidence: Km paper=0.044 mM; kcat paper=22 s^-1; kcat/Km paper=500 s^-1 mM^-1; export kcat=26.0 and kcat/Km=590.909090909091.

row_label: NADPH


substrate_name: D-Xylulose 5-phosphate

substrate: D-Xylulose 5-phosphate


assay_conditions_summary: pH 7.6; 295.15 K; cofactor NADH

column_label: Table 1 row DCIP (with 100 uM NADH), PcpD column reports kcat 14.1+/-0.6 s^-1, Km 38.3+/-2.5 uM, and kcat/Km (3.68+/-0.15)x10^5 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=14.1 normalized_unit=s^-1; Km normalized_value=0.0383 normalized_unit=mM; kcat/Km normalized_value=368.0 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=14.1+/-0.6 raw_unit=s^-1; Km raw_value=38.3+/-2.5 raw_unit=uM; kcat/Km raw_value=(3.68+/-0.15)x10^5 raw_unit=M^-1 s^-1

row_label: DCIP (with 100 uM NADH), PcpD column

table_label: PMC3683723 Table 1


substrate_name: NADH

column_label: Table 1, NADH (with 90 uM cytochrome c) row, full-length PcpD kcat, KM, and kcat/KM cells; the adjacent PcpD-FeS construct is excluded.

row_label: NADH (with 90 uM cytochrome c) / PcpD

table_label: Table 1. Kinetic parameters for reactions of PcpD with TCBQ, DCIP, and cytochrome c

substrate: NADH


assay_conditions_summary: pH 7.6; 295.15 K; cofactor NADPH

column_label: Table 1 row NADPH (with 90 uM cytochrome c), PcpD column reports kcat 3.7+/-0.3 s^-1, Km 1.21 mM, and kcat/Km (3.1+/-0.1)x10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=3.7 normalized_unit=s^-1; Km normalized_value=1.21 normalized_unit=mM; kcat/Km normalized_value=3.1 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=3.7+/-0.3 raw_unit=s^-1; Km raw_value=1.21 raw_unit=mM; kcat/Km raw_value=(3.1+/-0.1)x10^3 raw_unit=M^-1 s^-1


organism: Methanobrevibacter millerae

assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADH


substrate_name: sulfopyruvate

substrate: sulfopyruvate


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

organism: Saccharolobus solfataricus

substrate_name: beta-D-glucose

assay_conditions_summary: pH 7.5; 343.15 K; cofactor NAD+

column_label: Table II row D-Glucose / NAD+ gives Km 1.50, kcat 74.9, kcat/Km 49.9.

row_label: D-Glucose / NAD+

table_label: TABLE II. Kinetic parameters of glucose dehydrogenase from S. solfataricus at 70 C

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

substrate: beta-D-glucose


substrate_name: D-galactose

column_label: Table II row D-Galactose / NAD+ gives Km 0.57, kcat 61.3, kcat/Km 107.5.

row_label: D-Galactose / NAD+

substrate: D-galactose


organism: Escherichia coli (strain K12)

substrate_name: UDP-ManNAc (in the presence of 1 mM N-acetylglucosamine-1-P)


substrate_name: NAD(+)

substrate: NAD(+)


enzyme_display_name: Glucose/galactose 1-dehydrogenase

organism: Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)

substrate_name: D-glucose

enzyme: Glucose/galactose 1-dehydrogenase

substrate: D-glucose


substrate_name: NADP(+)

column_label: The Wiley full text states that kinetic analysis resulted in apparent Km values of 10 (+/- 1) mM for glucose at 5 mM NADP+ and 1.12 (+/- 0.2) mM for NADP+ at 50 mM glucose.

raw_value_unit_evidence: Km raw_value=1.12 raw_unit=mM

row_label: recombinant Picrophilus torridus GdhA / NADP+

table_label: Wiley full text PMID 15691337 GdhA kinetic analysis prose

substrate: NADP(+)


enzyme_display_name: glucose-6-phosphate 3-dehydrogenase

organism: Bacillus subtilis

substrate_name: D-glucose 6-phosphate

enzyme: glucose-6-phosphate 3-dehydrogenase

substrate: D-glucose 6-phosphate


substrate_name: NAD+

assay_conditions_summary: pH 9.5; 298.15 K; cofactor NAD+

substrate: NAD+


organism: Pseudomonas putida

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

column_label: Table 1 columns NAD, KM (uM), and kcat (s^-1); same row provides the primary values used to derive kcat/KM.

row_label: NAD

table_label: Table 1: Kinetic parameters obtained for PputG6PDH-1


substrate_name: NADP+

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

column_label: Table 1 columns NADP, KM (uM), and kcat (s^-1); same row provides the primary values used to derive kcat/KM.

row_label: NADP

substrate: NADP+


enzyme_display_name: UDP-N-acetylglucosamine 3-dehydrogenase

organism: Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)

substrate_name: UDP-GlcNAc

assay_conditions_summary: cofactor NAD+

enzyme: UDP-N-acetylglucosamine 3-dehydrogenase

substrate: UDP-GlcNAc


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

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

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


organism: Methanococcus maripaludis

substrate_name: UDP-N-acetyl-alpha-D-glucosamine

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+

substrate: UDP-N-acetyl-alpha-D-glucosamine


organism: Rhodococcus sp. AD45

assay_conditions_summary: pH 10; cofactor NAD+

column_label: Primary-paper PMC Results prose reports HGMB oxidation followed Michaelis-Menten kinetics and the Km for NAD+ was 0.07 mM at 7.5 mM HGMB.

raw_value_unit_evidence: NAD+ Km 0.07 mM at 7.5 mM HGMB

row_label: NAD+ substrate Km sentence

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


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

raw_value_unit_evidence: HGMB Km 1.4 mM

row_label: HGMB substrate Km sentence


organism: Sulfobacillus thermosulfidooxidans

assay_conditions_summary: pH 9.5; cofactor NAD+

proof_lines:
pH 9.5, 50°C
at pH 9.5 and 50°C


column_label: Abstract states the K m and V max values for L-KDR were 2.0 mM and 12.8 U/mg, respectively.

raw_value_unit_evidence: Km raw_value=2.0 mM raw_unit=mM

row_label: Sulth_3557 KDRDH / L-KDR

table_label: PubMed XML abstract


organism: Haloferax volcanii

assay_conditions_summary: pH 8; cofactor NAD+


assay_conditions_summary: pH 8


enzyme_display_name: Ribulose-5-phosphate reductase 2

organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

enzyme: Ribulose-5-phosphate reductase 2

substrate: NADPH


substrate_name: ribulose 5-phosphate

substrate: ribulose 5-phosphate


enzyme_display_name: 2-oxoglutarate reductase

organism: Homo sapiens

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

assay_conditions_summary: pH 7.6; 310.15 K; cofactor NADH

column_label: Table 1, reaction column 'α-ketoglutarate → 2-hydroxyglutarate': row 'Kcat (1/min)' cell = 4.7 (printed as '4.7 ± ...'), row 'Km, α-ketoglutarate (mM)' cell = 10.1. Table 1 prints no kcat/Km column; the kcat/Km entry is the quotient of those two cells, 4.7 (1/min) / 10.1 (mM).

normalized_value_unit_evidence: kcat raw 4.7 1/min normalizes to 0.07833333333333334 s^-1 (divide by 60); km raw 10.1 mM normalizes to 10.1 mM; kcat/Km = 0.07833333333333334 s^-1 / 10.1 mM = 0.007755775577557756 s^-1 mM^-1 (quotient of the two printed Table 1 cells; the paper prints no kcat/Km column).

raw_value_unit_evidence: Table 1; reaction column α-ketoglutarate → 2-hydroxyglutarate; column 'Kcat (1/min)'; raw value 4.7 1/min | Table 1; reaction column α-ketoglutarate → 2-hydroxyglutarate; column 'Km, α-ketoglutarate (mM)'; raw value 10.1 mM

row_label: α-ketoglutarate → 2-hydroxyglutarate | Km, α-ketoglutarate (mM)

table_label: Table 1. Michaelis-Menten Parameters of the Different Reactions Catalyzed by PHGDH, Compared to Intracellular Concentrations of the Corresponding Substrates and Products in Different Cell Lines.

enzyme: 2-oxoglutarate reductase


proof_lines:
PHGDH
NADH-dependent AKG reduction
high-affinity NAD(H) binding


enzyme_display_name: Ribulose-5-phosphate reductase 1

column_label: Table 2 lists TarIJ reductase NADPH Km (uM) as 6.74 +/- 1.64, which normalizes to 0.00674 mM and matches the exported NADPH Km.

raw_value_unit_evidence: Km raw_value=6.74 +/- 1.64 raw_unit=uM

row_label: TarIJ reductase / NADPH

table_label: Table 2: Summary of Kinetic Constants

enzyme: Ribulose-5-phosphate reductase 1


substrate_name: D-ribulose 5-phosphate

column_label: Table 2 lists TarIJ reductase ribulose-5-P Km (uM) as 28.5 +/- 13.1, which normalizes to 0.0285 mM and matches the exported D-ribulose 5-phosphate Km.

raw_value_unit_evidence: Km raw_value=28.5 +/- 13.1 raw_unit=uM

row_label: TarIJ reductase / ribulose-5-P

substrate: D-ribulose 5-phosphate


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

organism: Yamadazyma tenuis

substrate_name: D-Xylose

assay_conditions_summary: pH 6; 298.15 K; cofactor NADH

proof_lines:
BRENDA EC 1.1.1.307 entry
Yamadazyma tenuis CBS 4435
D-xylose

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

substrate: D-Xylose


enzyme_display_name: D-erythronate dehydrogenase

organism: Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)

proof_lines: kcat is 19 sec(-1) with NAD(+) as cosubstrate. kcat is 3.0 sec(-1) with NADP(+) as cosubstrate.

enzyme: D-erythronate dehydrogenase


enzyme_display_name: 4-phospho-D-threonate 3-dehydrogenase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: 4-hydroxy-L-threonine 4-phosphate

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

enzyme: 4-phospho-D-threonate 3-dehydrogenase

substrate: 4-hydroxy-L-threonine 4-phosphate


enzyme_display_name: 2-alkyl-3-oxoalkanoate reductase

organism: Stenotrophomonas maltophilia (strain K279a)

substrate_name: NADP

proof_lines: kcat is 122 min(-1) for syn-2-octyl-3-hydroxydodecanoic acid as substrate. kcat is 85 min(-1) for syn-2-decyl-3-hydroxytetradecanoic acid as substrate. kcat is 79 min(-1) for (2R,3S)-2-hexyl-3-hydroxydecanoic acid as substrate. kcat is 72 m

enzyme: 2-alkyl-3-oxoalkanoate reductase

substrate: NADP


substrate_name: (2R,3S)-2-hexyl-3-hydroxydecanoic acid

substrate: (2R,3S)-2-hexyl-3-hydroxydecanoic acid


enzyme_display_name: L-galactonate 5-dehydrogenase

organism: Phocaeicola vulgatus

substrate_name: L-gluconate

enzyme: L-galactonate 5-dehydrogenase

substrate: L-gluconate


substrate_name: D-tagaturonate

substrate: D-tagaturonate


substrate_name: L-fuconate

km_display: Not reported

substrate: L-fuconate


organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

substrate_name: NAD(+)

proof_lines: kcat is 1.9 sec(-1) with NAD(+) as cosubstrate. kcat is 0.88 sec(-1) with NADP(+) as cosubstrate.

substrate: NAD(+)


substrate_name: NADP(+)

substrate: NADP(+)


enzyme_display_name: L-threonate dehydrogenase

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

column_label: Table 1, Q6CZ26 (PaLtnD), l-Threonate, NAD+ row reports K_M 0.13 +/- 0.007.

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

table_label: Table 1

enzyme: L-threonate dehydrogenase


assay_conditions_summary: cofactor NADP+

column_label: Table 1, Q6CZ26 (PaLtnD), l-Threonate, NADP+ row reports K_M 0.97 +/- 0.1.

row_label: Q6CZ26 (PaLtnD), l-Threonate, NADP+


organism: Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)

proof_lines: kcat is 28 sec(-1) with NAD(+) as cosubstrate. kcat is 3.5 sec(-1) with NADP(+) as cosubstrate.


column_label: Table 1, Q0KBC7 (ReLtnD), l-Threonate, NAD+ row reports K_M 0.35 +/- 0.04.

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


column_label: Table 1, Q0KBC7 (ReLtnD), l-Threonate, NADP+ row reports K_M 0.30 +/- 0.04.

row_label: Q0KBC7 (ReLtnD), l-Threonate, NADP+


proof_lines: kcat is 9.7 sec(-1) with NAD(+) as cosubstrate. kcat is 2.9 sec(-1) with NADP(+) as cosubstrate.


enzyme_display_name: D-erythronate 2-dehydrogenase

organism: Cupriavidus necator

substrate_name: D-erythronate

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

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines:
cosubstrate NADP+, pH 8.0, 25°C
cosubstrate NAD+, pH 8.0, 25°C

enzyme: D-erythronate 2-dehydrogenase

substrate: D-erythronate


enzyme_display_name: noscapine synthase

organism: Papaver somniferum

substrate_name: narcotine hemiacetal

proof_lines:
pH 8.0, 30°C, cofactor NAD+
pH 8.0, 30°C, cofactor NADP+
cofactor NAD+, pH 8.0, 30°C

enzyme: noscapine synthase

substrate: narcotine hemiacetal


enzyme_display_name: L-threonate 2-dehydrogenase

organism: Pectobacterium atrosepticum

substrate_name: L-threonate

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

enzyme: L-threonate 2-dehydrogenase

substrate: L-threonate


organism: Escherichia coli (strain K12)

substrate_name: L-galactonate

column_label: Abstract reports the Km and kcat for L-galactonate were 19.5+/-0.6 mM and 0.51+/-0.03 s(-1), respectively.

raw_value_unit_evidence: Km raw_value=19.5+/-0.6 mM raw_unit=mM

row_label: E. coli YjjN / L-galactonate

table_label: PubMed XML abstract PMID 24861318

substrate: L-galactonate


substrate_name: NAD+

substrate: NAD+


substrate_name: NADP+

substrate: NADP+


column_label: Table 1; row Q0K4F5 (RePdxA2) / d-Threonate 4-phosphate; columns kcat (s^-1), KM (mM), kcat/KM (M^-1 s^-1); cells 3.4, 0.12, 2.9 x 10^4; normalized kcat/Km 29 s^-1 mM^-1

normalized_value_unit_evidence: kcat=3.4 s^-1; Km=0.12 mM; kcat/Km=29 s^-1 mM^-1 (explicit table value converted from M^-1 s^-1)

raw_value_unit_evidence: Q0K4F5 (RePdxA2) / d-Threonate 4-phosphate: kcat=3.4 s^-1; KM=0.12 mM; kcat/KM=2.9 x 10^4 M^-1 s^-1

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


column_label: Table 1; row Q0K4F5 (RePdxA2) / 4-Hydroxy-l-threonine 4-phosphate; columns kcat (s^-1), KM (mM), kcat/KM (M^-1 s^-1); cells 0.35, 0.20, 1.8 x 10^3; normalized kcat/Km 1.8 s^-1 mM^-1

normalized_value_unit_evidence: kcat=0.35 s^-1; Km=0.2 mM; kcat/Km=1.8 s^-1 mM^-1 (explicit table value converted from M^-1 s^-1)

raw_value_unit_evidence: Q0K4F5 (RePdxA2) / 4-Hydroxy-l-threonine 4-phosphate: kcat=0.35 s^-1; KM=0.2 mM; kcat/KM=1.8 x 10^3 M^-1 s^-1


row_label: Q0K4F5 (RePdxA2) / d-Threonate 4-phosphate


organism: Stenotrophomonas maltophilia

substrate_name: (2R/2S)-2-hexyl-3-oxodecanoic acid

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

proof_lines: Abstract supports the OleD substrate series and stereochemistry study.

proof_lines: No preserved row-level kinetic excerpt for (2R/2S)-2-hexyl-3-oxodecanoic acid.

substrate: (2R/2S)-2-hexyl-3-oxodecanoic acid


substrate_name: syn-2-decyl-3-hydroxytetradecanoic acid

proof_lines: Abstract identifies syn-2-decyl-3-hydroxytetradecanoic acid as the top substrate.

proof_lines: Saved evidence preserves relative catalytic efficiency, not the exact row constant.

substrate: syn-2-decyl-3-hydroxytetradecanoic acid


substrate_name: syn-2-octyl-3-hydroxydodecanoic acid

proof_lines: Abstract compares the octyl substrate with the decyl and hexyl analogs.

proof_lines: Saved evidence preserves only relative catalytic efficiency for the comparison set.

substrate: syn-2-octyl-3-hydroxydodecanoic acid


organism: Agrobacterium tumefaciens


substrate_name: D-xylonate

substrate: D-xylonate


substrate_name: L-Idonate

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

substrate: L-Idonate


substrate_name: D-gluconate

substrate: D-gluconate


substrate_name: D-Xylonate

proof_lines:
ThrDH homolog family
substrate-set context
D-Xylonate

substrate: D-Xylonate


substrate_name: D-Gluconate

proof_lines:
ThrDH homolog family
substrate-set context
D-Gluconate

substrate: D-Gluconate


substrate_name: 4-hydroxy-L-threonine 4-phosphate

column_label: Table 1; row P58718 (SePdxA2) / 4-Hydroxy-l-threonine 4-phosphate; columns kcat (s^-1), KM (mM), kcat/KM (M^-1 s^-1); cells 0.37, 0.19, 1.9 x 10^3; normalized kcat/Km 1.9 s^-1 mM^-1

normalized_value_unit_evidence: kcat=0.37 s^-1; Km=0.19 mM; kcat/Km=1.9 s^-1 mM^-1 (explicit table value converted from M^-1 s^-1)

raw_value_unit_evidence: P58718 (SePdxA2) / 4-Hydroxy-l-threonine 4-phosphate: kcat=0.37 s^-1; KM=0.19 mM; kcat/KM=1.9 x 10^3 M^-1 s^-1

substrate: 4-hydroxy-L-threonine 4-phosphate


column_label: Table 1; row P58718 (SePdxA2) / d-Threonate 4-phosphate; columns kcat (s^-1), KM (mM), kcat/KM (M^-1 s^-1); cells 8.9, 0.054, 1.6 x 10^5; normalized kcat/Km 160 s^-1 mM^-1

normalized_value_unit_evidence: kcat=8.9 s^-1; Km=0.054 mM; kcat/Km=160 s^-1 mM^-1 (explicit table value converted from M^-1 s^-1)

raw_value_unit_evidence: P58718 (SePdxA2) / d-Threonate 4-phosphate: kcat=8.9 s^-1; KM=0.054 mM; kcat/KM=1.6 x 10^5 M^-1 s^-1


substrate_name: D-tagaturonate

assay_conditions_summary: pH 7; 303.15 K; buffer pH 7; cofactor NADH

column_label: Table 1 row Bvu0222; D-tagaturonate row; kcat / KM / kcat/KM columns; footnote d reduction direction.

normalized_value_unit_evidence: 550 uM normalizes to 0.55 mM; 1.6 x 10^5 M^-1 s^-1 normalizes to 160 s^-1 mM^-1.

row_label: Bvu0222 / D-tagaturonate

table_label: Table 1: Catalytic Constants for Bvu0220, Bvu0219, and Bvu0222

substrate: D-tagaturonate


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

column_label: Table 1 row Bvu0222; L-galactonate row; kcat / KM / kcat/KM columns.

normalized_value_unit_evidence: 36 uM normalizes to 0.036 mM; 1.7 x 10^4 M^-1 s^-1 normalizes to 17 s^-1 mM^-1.

row_label: Bvu0222 / L-galactonate


substrate_name: L-gluconate

column_label: Table 1 row Bvu0222; L-gluconate row; kcat / KM / kcat/KM columns.

normalized_value_unit_evidence: 510 uM normalizes to 0.51 mM; 3.9 x 10^2 M^-1 s^-1 normalizes to 0.39 s^-1 mM^-1.

row_label: Bvu0222 / L-gluconate

substrate: L-gluconate


enzyme_display_name: Retinol dehydrogenase 16

assay_conditions_summary: pH 7.3; cofactor NAD+

column_label: Table I row Androsterone, column Km (microM), reports 0.14 +/- 0.02.

raw_value_unit_evidence: Androsterone Km 0.14 +/- 0.02 microM

row_label: Androsterone

table_label: Table I. Kinetic constants of RoDH-4 for steroid substrates, PMID 9677409

enzyme: Retinol dehydrogenase 16


organism: Mus musculus

column_label: Table II row Androsterone has Activity 3alpha-HSD, Product androstanedione, Km 0.1 uM, Rate 6, V/Km 60.

normalized_value_unit_evidence: 0.1 uM = 0.0001 mM; CatLog row stores 0.0002 mM.

raw_value_unit_evidence: Table II reports Androsterone Km = 0.1 uM.

row_label: Androsterone / 3alpha-HSD / androstanedione

table_label: JBC 272(52) Table II, steroid substrate kinetics for recombinant mouse CRAD


enzyme_display_name: Perakine reductase

organism: Rauvolfia serpentina

substrate_name: coniferyl aldehyde

enzyme: Perakine reductase

substrate: coniferyl aldehyde


enzyme_display_name: Benzil reductase ((S)-benzoin forming) NRE1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: benzil (with NADH as cosubstrate)

proof_lines: Nre1p benzil NADH

substrate: benzil (with NADH as cosubstrate)


enzyme_display_name: Eugenol synthase 1

organism: Ocimum basilicum

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

column_label: Full text reports for EGS1 the corresponding Km values were 5.1 mM for coniferyl acetate and 131 microM for NADPH.

raw_value_unit_evidence: Km raw_value=131 microM raw_unit=microM

row_label: Ocimum basilicum EGS1 / NADPH cofactor

table_label: PMC full text PMID 16782809 EGS1/IGS1 kinetic prose

enzyme: Eugenol synthase 1


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

organism: Ogataea glucozyma

substrate_name: benzil

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

proof_lines:
KRED1-Pglu
Pichia glucozyma
Ogataea glucozyma

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

substrate: benzil


organism: Sungouiella intermedia

substrate_name: xylitol

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

assay_conditions_summary: pH 7; cofactor NADP+

proof_lines:
cosubstrate NADP+, pH 7, 25°C
cosubstrate NAD+, pH 7, 25°C

substrate: xylitol


organism: Chlorobaculum tepidum

substrate_name: sepiapterin

proof_lines: For the reverse reaction, accepts L-threo-dihydrobiopterin, D-threo-dihydrobiopterin, L-threo-dihydroneopterin, dihydrotepidopterin and L-erythro-dihydrobiopterin as substrates.

substrate: sepiapterin


substrate_name: NADPH

assay_conditions_summary: pH 8.8; cofactor NADPH

substrate: NADPH


organism: Methanococcus maripaludis

substrate_name: NAD+

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+

substrate: NAD+


organism: Sphingobium sp. (strain NBRC 103272 / SYK-6)

substrate_name: NAD (with CHMS as substrate at 25 degrees Celsius and pH 8)

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

column_label: Official PMC Table 3 row NAD+ (200) lists CHMS Km=20.6 +/- 1.0 microM; the table footnote states that Km values are for the compounds shown in parentheses.

raw_value_unit_evidence: Km raw_value=20.6 +/- 1.0 microM raw_unit=microM for CHMS with NAD+

row_label: LigC / CHMS Km with NAD+ (200 microM cofactor)

table_label: PMC111406 Table 3, kinetic constants of the CHMS dehydrogenases


substrate_name: NADP (with CHMS as substrate at 25 degrees Celsius and pH 8)

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

column_label: Official PMC Table 3 row NADP+ (200) lists CHMS Km=26.0 +/- 0.5 microM; the table footnote states that Km values are for the compounds shown in parentheses.

raw_value_unit_evidence: Km raw_value=26.0 +/- 0.5 microM raw_unit=microM for CHMS with NADP+

row_label: LigC / CHMS Km with NADP+ (200 microM cofactor)


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

organism: Homo sapiens

substrate_name: estrone

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

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

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

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

substrate: estrone


organism: Weissella confusa

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


organism: Methanocaldococcus jannaschii

substrate_name: glyoxylate

proof_lines:
glyoxylate
lower efficiency

substrate: glyoxylate


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

substrate_name: NAD(+)

assay_conditions_summary: cofactor NAD+

substrate: NAD(+)


enzyme_display_name: L-sulfolactate dehydrogenase

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

substrate_name: oxopropanedioate (in the presence of NADH)

assay_conditions_summary: cofactor NADH

proof_lines:
glyoxylate
oxo propanedioic acid
lower efficiency

enzyme: L-sulfolactate dehydrogenase


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


organism: Streptomyces avermitilis

substrate_name: 1-deoxy-11beta-hydroxypentalenic acid

assay_conditions_summary: pH 8

substrate: 1-deoxy-11beta-hydroxypentalenic acid


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

organism: Arthrobacter sp. TS-15

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


substrate_name: isatin

substrate: isatin


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


substrate_name: NADH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

substrate: NADH


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

organism: Gluconobacter oxydans


enzyme_display_name: 5'-hydroxyaverantin dehydrogenase

organism: Aspergillus parasiticus

assay_conditions_summary: pH 7.5; buffer 60 mM potassium phosphate

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

raw_value_unit_evidence: Km raw_value=83 raw_unit=uM

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

table_label: PMC full text PMID 14602595 HAVN dehydrogenase kinetic prose

enzyme: 5'-hydroxyaverantin dehydrogenase


enzyme_display_name: UniProt A0A545BBS8

organism: Arthrobacter sp.

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt A0A545BBS8

source: skid


enzyme_display_name: pseudoephedrine dehydrogenase

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NAD+

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

row_label: PseDH / NAD+

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

enzyme: pseudoephedrine dehydrogenase


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

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

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

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


organism: Arthrobacter sp. Cr-7

substrate_name: Isopyridoxal

substrate: Isopyridoxal


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


substrate_name: ethyl 2-chlorobenzoylacetate

substrate: ethyl 2-chlorobenzoylacetate


substrate_name: methyl benzoylformate

substrate: methyl benzoylformate


enzyme_display_name: D-apiose dehydrogenase

organism: Klebsiella aerogenes

substrate_name: D-apiitol

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

enzyme: D-apiose dehydrogenase

substrate: D-apiitol


substrate_name: D-apiose

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

substrate: D-apiose


substrate_name: NAD+


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

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


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

organism: Arabidopsis thaliana

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


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

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


protein_accession_database: NCBI Protein

sequence_source: GenBank accession TQS88919 (pseudoephedrine dehydrogenase)


assay_conditions_summary: pH 7.8; cofactor NAD+

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

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


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


organism: Nepeta racemosa

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

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


enzyme_display_name: D-apionate oxidoisomerase

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

substrate_name: D-apionate

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

enzyme: D-apionate oxidoisomerase

substrate: D-apionate


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


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

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

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

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


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


enzyme_display_name: 3alpha-hydroxysteroid 3-dehydrogenase

organism: Comamonas testosteroni

assay_conditions_summary: pH 10.5; 283.15 K; cofactor NAD+

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

table_label: Results text / Supplementary kinetic tables S2-S3

enzyme: 3alpha-hydroxysteroid 3-dehydrogenase


enzyme_display_name: D-galacturonate reductase

organism: Hypocrea jecorina

substrate_name: NADP(+)

proof_lines:
Hypocrea jecorina
d-galacturonic acid reductase
enzyme kinetics

enzyme: D-galacturonate reductase

substrate: NADP(+)


enzyme_display_name: Glucose 1-dehydrogenase

organism: Saccharolobus solfataricus

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

assay_conditions_summary: 343.15 K; cofactor NADP+

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

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

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

row_label: Glucose-NADP+ / coenzyme Km column

enzyme: Glucose 1-dehydrogenase


enzyme_display_name: D-chiro-inositol 1-dehydrogenase

organism: Thermotoga maritima

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

enzyme: D-chiro-inositol 1-dehydrogenase


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

substrate_name: L-Arabinose

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

substrate: L-Arabinose


organism: Homo sapiens


enzyme_display_name: Aldo-keto reductase family 1 member A1

organism: Mus musculus

substrate_name: D-glucuronate

proof_lines:
D-glucuronate
L-gulonate
aldehyde reductase

enzyme: Aldo-keto reductase family 1 member A1

substrate: D-glucuronate


enzyme_display_name: L-gulonate 5-dehydrogenase

organism: Halomonas elongata

substrate_name: L-gulonate

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

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

row_label: HeGulDH / CsGulDH enzyme row with L-gulonate

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

enzyme: L-gulonate 5-dehydrogenase

substrate: L-gulonate


organism: Methanocaldococcus jannaschii

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

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

raw_value_unit_evidence: Km raw_value=4.6 raw_unit=mM

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

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


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

organism: Ignisphaera aggregans

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


substrate_name: pyruvate

assay_conditions_summary: pH 6.6; cofactor NADPH

substrate: pyruvate


organism: Rhodococcus sp. (strain AD45)

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

raw_value_unit_evidence: HGMB Km 1.4 mM

row_label: HGMB substrate Km sentence

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


organism: Mediterraneibacter gnavus

assay_conditions_summary: pH 7


enzyme_display_name: D-altritol 5-dehydrogenase

organism: Agrobacterium fabrum

substrate_name: D-Altritol

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

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

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

row_label: Atu ZnD / D-Altritol

table_label: PMC4661409 HTML Table 3

enzyme: D-altritol 5-dehydrogenase

substrate: D-Altritol


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

smiles: CC(C(C)O)O


enzyme_display_name: sulfoacetaldehyde reductase (NADH)

organism: Bifidobacterium catenulatum subsp. kashiwanohense

substrate_name: NADP+

assay_conditions_summary: pH 10; 303.15 K; cofactor NADP+

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

enzyme: sulfoacetaldehyde reductase (NADH)

substrate: NADP+


substrate_name: isethionate

substrate: isethionate


assay_conditions_summary: pH 10

proof_lines: pH 10, temperature not specified in the publication


assay_conditions_summary: pH 10; 303.15 K; cofactor NAD+

substrate: NAD+


assay_conditions_summary: pH 10; cofactor NAD+


substrate_name: NADH

assay_conditions_summary: pH 10; 303.15 K; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 7.5; cofactor NADH

proof_lines: pH 7.5, temperature not specified in the publication


substrate_name: NADPH

assay_conditions_summary: pH 10; 303.15 K; cofactor NADPH

substrate: NADPH


enzyme_display_name: L-fucose dehydrogenase

organism: Burkholderia multivorans (strain ATCC 17616 / 249)

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

enzyme: L-fucose dehydrogenase


organism: Xanthomonas campestris pv. campestris


organism: Burkholderia multivorans

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

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

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

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

row_label: Table 3, substrate row `NAD+`

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


substrate_name: beta-L-fucose

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

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

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

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

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

substrate: beta-L-fucose


substrate_name: L-galactose

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

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

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

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

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

substrate: L-galactose


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

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

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

row_label: Table 3, substrate row `NADP+`


substrate_name: D-arabinose

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

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

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

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

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

substrate: D-arabinose


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

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

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

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


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

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

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

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

row_label: Sulfoacetaldehyde

table_label: Table 2. Enzyme kinetic parameters


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

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

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

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

row_label: Isethionate


substrate_name: NAD+

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

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

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

row_label: NAD+


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

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

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

row_label: NADH


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

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

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

row_label: NADP+


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

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

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

row_label: NADPH


enzyme_display_name: L-threonate 2-dehydrogenase

organism: Cupriavidus necator

substrate_name: L-threonate

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

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

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

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

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

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

enzyme: L-threonate 2-dehydrogenase

substrate: L-threonate


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

organism: Streptomyces virginiae

substrate_name: 6-dehydro-Virginiae butanolide-A

assay_conditions_summary: pH 7.5; cofactor NADPH

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

raw_value_unit_evidence: Km raw_value=11.1 raw_unit=uM

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

table_label: PMC full text PMID 12193632 rBarS1 characterization prose

substrate: 6-dehydro-Virginiae butanolide-A


enzyme_display_name: D-erythronate 2-dehydrogenase

substrate_name: D-erythronate

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

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

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

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

enzyme: D-erythronate 2-dehydrogenase

substrate: D-erythronate


organism: Pectobacterium atrosepticum

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

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

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

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

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


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

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

substrate_name: D-lactate

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

assay_conditions_summary: cofactor NAD+

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

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

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

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

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

substrate: D-lactate


substrate_name: L-lactate

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

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

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

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

substrate: L-lactate


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

substrate_name: NAD(+)

substrate: NAD(+)


enzyme_display_name: polyprenol dehydrogenase [NAD(P)H]

organism: Cricetulus griseus

substrate_name: ditrans,polycis-polyprenol

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

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

enzyme: polyprenol dehydrogenase [NAD(P)H]

substrate: ditrans,polycis-polyprenol


assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

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


assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+


assay_conditions_summary: pH 8; 310.15 K; cofactor NADH


enzyme_display_name: Polyprenol dehydrogenase

organism: Homo sapiens

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

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

enzyme: Polyprenol dehydrogenase

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


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

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


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

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

assay_conditions_summary: pH 8.5; cofactor NAD+

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

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

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

row_label: IPMDH_Mj row; beta-Isopropylmalate K_m column

table_label: Table 3. Kinetic parameters for IPMDH homologs


substrate_name: D-malate

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

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

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

row_label: IPMDH_Mj row; d-Malate K_m column

substrate: D-malate


enzyme_display_name: (-)-trans-carveol dehydrogenase

organism: Rhodococcus erythropolis

enzyme: (-)-trans-carveol dehydrogenase


enzyme_display_name: Sulfoacetaldehyde reductase

organism: Bilophila wadsworthia (strain 3_1_6)

substrate_name: sulfoacetaldehyde

assay_conditions_summary: cofactor NADH

proof_lines:
Bilophila wadsworthia
SarD
sulfoacetaldehyde reductase

enzyme: Sulfoacetaldehyde reductase

substrate: sulfoacetaldehyde


organism: Arabidopsis thaliana

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

normalized_value_unit_evidence: Km central normalized_value=0.13 normalized_unit=mM.

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

row_label: Wild type Arabidopsis 3betaHSD/D

table_label: PMC2663740 Table II


enzyme_display_name: Glyoxylate/succinic semialdehyde reductase 1

substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: succinate semialdehyde

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

enzyme: Glyoxylate/succinic semialdehyde reductase 1

substrate: succinate semialdehyde


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


enzyme_display_name: sulfolactaldehyde 3-reductase

organism: Escherichia coli

substrate_name: NADH

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

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

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

enzyme: sulfolactaldehyde 3-reductase

substrate: NADH


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


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


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


substrate_name: Unknown

substrate: Unknown


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

organism: [Clostridium] scindens

substrate_name: NADP+

assay_conditions_summary: pH 8.7; 310.15 K; cofactor NADP+

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

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

substrate: NADP+


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

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

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


substrate_name: chenodeoxycholic acid

substrate: chenodeoxycholic acid


substrate_name: NAD+

assay_conditions_summary: pH 8.7; 310.15 K; cofactor NAD+

substrate: NAD+


substrate_name: cholic acid

substrate: cholic acid


assay_conditions_summary: pH 8.7; 310.15 K; cofactor CoA


substrate_name: glycocholic acid

substrate: glycocholic acid


substrate_name: taurocholic acid

substrate: taurocholic acid


substrate_name: deoxycholoyl-CoA

substrate: deoxycholoyl-CoA


substrate_name: choloyl-CoA

substrate: choloyl-CoA


substrate_name: lithocholoyl-CoA

substrate: lithocholoyl-CoA


substrate_name: chenodeoxycholoyl-CoA

substrate: chenodeoxycholoyl-CoA


enzyme_display_name: Peroxisomal multifunctional enzyme type 2

organism: Drosophila melanogaster

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

assay_conditions_summary: cofactor CoA

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


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

enzyme: Peroxisomal multifunctional enzyme type 2


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


enzyme_display_name: succinic semialdehyde reductase

organism: Mus musculus

assay_conditions_summary: pH 6.6; 298.15 K; cofactor NADPH

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

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

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

enzyme: succinic semialdehyde reductase


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

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


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

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

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


substrate_name: Camphorquinone

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

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

row_label: Camphorquinone

substrate: Camphorquinone


substrate_name: Dimethylglyoxal

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

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

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

row_label: Diacetyl

substrate: Dimethylglyoxal


substrate_name: Isatin

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

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

row_label: Isatin

substrate: Isatin


substrate_name: NADH

assay_conditions_summary: pH 6.6; 298.15 K; cofactor NADH

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

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


substrate_name: NADPH

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

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

substrate: NADPH


substrate_name: p-Nitrobenzaldehyde

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

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

substrate: p-Nitrobenzaldehyde


substrate_name: Succinate semialdehyde

smiles: O=CCCC(=O)O

substrate: Succinate semialdehyde


substrate_name: Trans, trans-muconaldehyde

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

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

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

row_label: Trans, trans-muconaldehyde

substrate: Trans, trans-muconaldehyde


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


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


assay_conditions_summary: pH 6.7; 298.15 K; cofactor NADPH

proof_lines: hAFAR shows high affinity for succinic semialdehyde


enzyme_display_name: Succinic semialdehyde reductase

organism: Metallosphaera sedula

substrate_name: NADPH; Succinate semialdehyde; H+

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

enzyme: Succinic semialdehyde reductase

substrate: NADPH; Succinate semialdehyde; H+


assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADPH


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

row_label: SSA; fixed substrate NADPH

table_label: Table 1


enzyme_display_name: Glyoxylate/succinic semialdehyde reductase 2, chloroplastic

substrate_name: glyoxylate (check for NADPH)

assay_conditions_summary: pH 7.6; cofactor NADPH

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

row_label: Glyoxylate; fixed substrate NADPH

substrate: glyoxylate (check for NADPH)


substrate_name: succinate semialdehyde

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

enzyme: Glyoxylate/succinic semialdehyde reductase 2, chloroplastic

substrate: succinate semialdehyde


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

assay_conditions_summary: cofactor NADPH


enzyme_display_name: Aflatoxin B1 aldehyde reductase member 2

substrate_name: succinic semialdehyde

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

normalized_value_unit_evidence: Km 0.02 mM from 20 uM.

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

row_label: Succinic semialdehyde / AKR7A2

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

substrate: succinic semialdehyde


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

normalized_value_unit_evidence: Km 0.017 mM from 17 uM.

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

row_label: 2-Carboxybenzaldehyde / AKR7A2

enzyme: Aflatoxin B1 aldehyde reductase member 2


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

normalized_value_unit_evidence: Km 0.008 mM from 8 uM.

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

row_label: 9,10-Phenanthrenequinone / AKR7A2


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

normalized_value_unit_evidence: Km 0.102 mM from 102 uM.

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

row_label: 1,2-Naphthoquinone / AKR7A2


organism: Rattus norvegicus

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


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


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


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

substrate_name: estradiol

proof_lines:
Ke 6
HSD17B8
estradiol

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

substrate: estradiol


substrate_name: testosterone

proof_lines:
Ke 6
HSD17B8
testosterone

substrate: testosterone


substrate_name: estrone

proof_lines:
Ke 6
HSD17B8
estrone

substrate: estrone


substrate_name: dihydrotestosterone

proof_lines:
Ke 6
HSD17B8
dihydrotestosterone

substrate: dihydrotestosterone


assay_conditions_summary: pH 8.5; cofactor CoA

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

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

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


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

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


substrate_name: NAD

proof_lines:
HSD17B4
dehydrogenase reactions
Table II

substrate: NAD


substrate: NADH


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

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

row_label: Wild-type AKR7A5 / SSA

table_label: Table 2, PMID 16460003 PDF


enzyme_display_name: UniProt P00175

organism: Saccharomyces cerevisiae

substrate_name: FAD

enzyme: UniProt P00175

substrate: FAD


enzyme_display_name: methanol dehydrogenase (cytochrome c)

organism: Methyloversatilis universalis

substrate_name: methanol

smiles: CO

enzyme: methanol dehydrogenase (cytochrome c)

substrate: methanol


substrate_name: ethanol

smiles: CCO

substrate: ethanol


substrate_name: n-Propanol

smiles: CCCO

substrate: n-Propanol


substrate_name: n-butanol

smiles: CCCCO

substrate: n-butanol


organism: Methylibium petroleiphilum


organism: Methylophilus methylotrophus

substrate_name: PQQ; Methanol

substrate: PQQ; Methanol


enzyme_display_name: mannitol dehydrogenase (cytochrome)

organism: Komagataeibacter xylinus

substrate_name: D-mannitol

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

proof_lines: with phenanzine methosulfate as electron acceptor

enzyme: mannitol dehydrogenase (cytochrome)

substrate: D-mannitol


substrate_name: Unknown

substrate: Unknown


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

organism: Nitratidesulfovibrio vulgaris

substrate_name: D-lactate

substrate: D-lactate


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


organism: Gluconobacter oxydans

substrate_name: D-arabitol

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

substrate: D-arabitol


substrate_name: D-sorbitol

substrate: D-sorbitol


enzyme_display_name: L-lactate dehydrogenase (cytochrome)

organism: Satureja hortensis

substrate_name: (S)-lactate

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication

enzyme: L-lactate dehydrogenase (cytochrome)

substrate: (S)-lactate


substrate_name: potassium ferricyanide

proof_lines: pH 9.5, temperature not specified in the publication

substrate: potassium ferricyanide


organism: Rhodovulum steppense

proof_lines: pH and temperature not specified in the publication


organism: Crocus sativus

substrate_name: ferricyanide

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

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

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

substrate: ferricyanide


organism: Arabidopsis thaliana


organism: Ogataea angusta

substrate_name: L-lactate

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

proof_lines: biosensor based on recombinant yeast FCb2cells

substrate: L-lactate


enzyme_display_name: D-lactate dehydrogenase (cytochrome)

organism: Megasphaera elsdenii

proof_lines:
with ferricyanide
with complete electron transport system

enzyme: D-lactate dehydrogenase (cytochrome)


organism: Helianthus tuberosus


organism: Methylomicrobium sp. HG-1

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

assay_conditions_summary: pH 9

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


substrate_name: Heptanol

smiles: CCCCCCCO

substrate: Heptanol


substrate_name: Hexanol

smiles: CCCCCCO

substrate: Hexanol


substrate_name: Pentanol

smiles: CCCCCO

substrate: Pentanol


substrate_name: Propanol

substrate: Propanol


substrate_name: butanol

substrate: butanol


enzyme_display_name: Quinoprotein ethanol dehydrogenase

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

substrate_name: ethanol

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

enzyme: Quinoprotein ethanol dehydrogenase

substrate: ethanol


smiles: CC(C)O


smiles: CCC(C)O


substrate_name: ethanal

smiles: CC=O

substrate: ethanal


substrate_name: methanol

substrate: methanol


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

assay_conditions_summary: pH 7

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


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

smiles: C(CO)CO

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


substrate_name: 1-butanol (at pH 9)

substrate: 1-butanol (at pH 9)


substrate_name: FAD

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

assay_conditions_summary: pH 7; cofactor FAD

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

substrate: FAD


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

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


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

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


enzyme_display_name: D-lactate dehydrogenase [cytochrome], mitochondrial

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

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

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


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

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

enzyme: D-lactate dehydrogenase [cytochrome], mitochondrial


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


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


substrate_name: glycolate (with cytochrome c as acceptor molecule)

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


substrate_name: L-lactate

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

source_databases_merged: skid uniprot


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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

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


substrate_name: pyruvate

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

substrate: pyruvate


substrate_name: (R)-lactate

substrate: (R)-lactate


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


organism: Methylophaga aminisulfidivorans

smiles: CO

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

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

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


organism: Saccharomyces cerevisiae

substrate_name: Ferricytochrome c

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

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

substrate: Ferricytochrome c


substrate_name: L-Lactate

proof_lines:
L-lactate dehydrogenation
cytochrome c reduction
R289K

substrate: L-Lactate


substrate_name: L-Phenyllactate

substrate: L-Phenyllactate


substrate_name: cytochrome c

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

substrate: cytochrome c


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


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


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


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


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


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


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


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


assay_conditions_summary: pH 7; 303.15 K; cofactor FAD


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


enzyme_display_name: Quinoprotein alcohol dehydrogenase PedE

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

substrate_name: ethanol

smiles: CCO

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

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

row_label: PedE, ethanol

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

enzyme: Quinoprotein alcohol dehydrogenase PedE


substrate_name: acetaldehyde

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

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

row_label: PedE, acetaldehyde

substrate: acetaldehyde


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

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

row_label: PedE, 2-phenylethanol


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


enzyme_display_name: alcohol dehydrogenase (cytochrome c)

organism: Methylacidiphilum fumariolicum

substrate_name: methanol

enzyme: alcohol dehydrogenase (cytochrome c)


substrate_name: Phenyllactate

proof_lines:
Y254F mutant enzyme
Y254F mutant

substrate: Phenyllactate


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

substrate: L-lactate


substrate_name: ferricyanide

substrate: ferricyanide


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


substrate_name: (S)-mandelate

substrate: (S)-mandelate


enzyme_display_name: 3-hydroxy acid dehydrogenase

organism: Escherichia coli

substrate_name: L-Glycerate

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

enzyme: 3-hydroxy acid dehydrogenase

substrate: L-Glycerate


substrate_name: D-glycerate

substrate: D-glycerate


substrate_name: D-serine

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

substrate: D-serine


substrate_name: L-allo-threonine

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

substrate: L-allo-threonine


substrate_name: NADP+

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

substrate: NADP+


enzyme_display_name: UniProt Q44467

organism: Aerococcus viridans

substrate_name: glycerate

enzyme: UniProt Q44467

substrate: glycerate


substrate_name: L-lactate

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


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


substrate_name: (S)-mandelic acid

substrate: (S)-mandelic acid


smiles: O=O

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


enzyme_display_name: glucose oxidase

organism: Talaromyces variabilis

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

enzyme: glucose oxidase


organism: Talaromyces funiculosus

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


substrate_name: D-xylose

substrate: D-xylose


substrate_name: D-maltose

substrate: D-maltose


substrate_name: D-fructose

substrate: D-fructose


enzyme_display_name: Carbohydrate oxidase

organism: Microdochium nivale

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

enzyme: Carbohydrate oxidase


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


organism: Pseudomonas putida

substrate_name: ethanol

substrate: ethanol


smiles: CCCCO


smiles: CC(CO)O

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


organism: Streptomyces coelicolor

substrate_name: D-mannitol

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

substrate: D-mannitol


substrate_name: xylitol

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

substrate: xylitol


enzyme_display_name: L-lactate oxidase

enzyme: L-lactate oxidase


organism: Methylotenera mobilis

smiles: CCCCCCO

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


smiles: CCCO


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


smiles: CCCC(CO)N


smiles: C=CCCO


smiles: CCC(CO)O


smiles: C=CC(CO)O


smiles: CCCC(CO)O


substrate_name: glycerol

smiles: C(C(CO)O)O

substrate: glycerol


substrate_name: L-arabinose

substrate: L-arabinose


smiles: CCCCC(CO)O