organism: Paracoccus denitrificans

substrate_name: succinyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D3JV03 and applied mutation signature A282V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; buffer pH 7; cofactor CoA

column_label: Table 2. Michaelis-Menten kinetic parameters for the wildtype and mutant RsMCD with either (2S)-methylsuccinyl-CoA or succinyl-CoA as substrate; row RsMCD A282V / Succinyl-CoA; columns kcat s^-1 raw 0.30 +/- 0.04, Km(app) uM raw 57 +/- 20, kcat/Km s^-1 M^-1 raw 5.3 x 10^3 +/- 2.0 x 10^3; normalized kcat 0.3 s^-1, Km 0.057 mM, same-row kcat/Km 5.263157894736842 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.3 normalized_unit=s^-1; Km normalized_value=0.057 normalized_unit=mM from 57 +/- 20 uM / 1000; kcat/Km normalized_value=5.263157894736842 normalized_unit=s^-1*mM^-1 from same-row kcat/Km; printed efficiency=5.3 x 10^3 +/- 2.0 x 10^3 s^-1 M^-1

raw_value_unit_evidence: kcat raw_value=0.30 +/- 0.04 raw_unit=s^-1; Km raw_value=57 +/- 20 raw_unit=uM; kcat/Km raw_value=5.3 x 10^3 +/- 2.0 x 10^3 raw_unit=s^-1 M^-1

row_label: RsMCD A282V / Succinyl-CoA

substrate: succinyl-CoA


enzyme_display_name: (2S)-methylsuccinyl-CoA dehydrogenase

source_db: brenda

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

column_label: Table 2. Michaelis-Menten kinetic parameters for the wildtype and mutant RsMCD with either (2S)-methylsuccinyl-CoA or succinyl-CoA as substrate; row RsMCD WT / Succinyl-CoA; columns kcat s^-1 raw 0.32 +/- 0.06, Km(app) uM raw 141 +/- 52, kcat/Km s^-1 M^-1 raw 2.3 x 10^3 +/- 0.9 x 10^3; normalized kcat 0.32 s^-1, Km 0.141 mM, same-row kcat/Km 2.269503546099291 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.32 normalized_unit=s^-1; Km normalized_value=0.141 normalized_unit=mM from 141 +/- 52 uM / 1000; kcat/Km normalized_value=2.269503546099291 normalized_unit=s^-1*mM^-1 from same-row kcat/Km; printed efficiency=2.3 x 10^3 +/- 0.9 x 10^3 s^-1 M^-1

raw_value_unit_evidence: kcat raw_value=0.32 +/- 0.06 raw_unit=s^-1; Km raw_value=141 +/- 52 raw_unit=uM; kcat/Km raw_value=2.3 x 10^3 +/- 0.9 x 10^3 raw_unit=s^-1 M^-1

row_label: RsMCD WT / Succinyl-CoA

data_origin: experimental

enzyme: (2S)-methylsuccinyl-CoA dehydrogenase

status: verified

source: brenda


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D3JV03 and applied mutation signature A282F/F284A to reconstruct the assayed variant sequence.

column_label: Table 2. Michaelis-Menten kinetic parameters for the wildtype and mutant RsMCD with either (2S)-methylsuccinyl-CoA or succinyl-CoA as substrate; row RsMCD A282F/F284A / (2S)-methylsuccinyl-CoA; columns kcat s^-1 raw 0.71 +/- 0.03, Km(app) uM raw 439 +/- 49, kcat/Km s^-1 M^-1 raw 1.6 x 10^3 +/- 0.2 x 10^3; normalized kcat 0.71 s^-1, Km 0.439 mM, same-row kcat/Km 1.6173120728929384 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.71 normalized_unit=s^-1; Km normalized_value=0.439 normalized_unit=mM from 439 +/- 49 uM / 1000; kcat/Km normalized_value=1.6173120728929384 normalized_unit=s^-1*mM^-1 from same-row kcat/Km; printed efficiency=1.6 x 10^3 +/- 0.2 x 10^3 s^-1 M^-1

raw_value_unit_evidence: kcat raw_value=0.71 +/- 0.03 raw_unit=s^-1; Km raw_value=439 +/- 49 raw_unit=uM; kcat/Km raw_value=1.6 x 10^3 +/- 0.2 x 10^3 raw_unit=s^-1 M^-1


mutation_type: substitution

column_label: Table 2. Michaelis-Menten kinetic parameters for the wildtype and mutant RsMCD with either (2S)-methylsuccinyl-CoA or succinyl-CoA as substrate; row RsMCD A282V / (2S)-methylsuccinyl-CoA; columns kcat s^-1 raw 31.8 +/- 0.6, Km(app) uM raw 64 +/- 5, kcat/Km s^-1 M^-1 raw 0.5 x 10^6 +/- 0.04 x 10^6; normalized kcat 31.8 s^-1, Km 0.064 mM, same-row kcat/Km 496.875 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=31.8 normalized_unit=s^-1; Km normalized_value=0.064 normalized_unit=mM from 64 +/- 5 uM / 1000; kcat/Km normalized_value=496.875 normalized_unit=s^-1*mM^-1 from same-row kcat/Km; printed efficiency=0.5 x 10^6 +/- 0.04 x 10^6 s^-1 M^-1

raw_value_unit_evidence: kcat raw_value=31.8 +/- 0.6 raw_unit=s^-1; Km raw_value=64 +/- 5 raw_unit=uM; kcat/Km raw_value=0.5 x 10^6 +/- 0.04 x 10^6 raw_unit=s^-1 M^-1

row_label: RsMCD A282V / (2S)-methylsuccinyl-CoA


column_label: Table 2. Michaelis-Menten kinetic parameters for the wildtype and mutant RsMCD with either (2S)-methylsuccinyl-CoA or succinyl-CoA as substrate; row RsMCD WT / (2S)-methylsuccinyl-CoA; columns kcat s^-1 raw 82.3 +/- 1.4, Km(app) uM raw 80 +/- 5, kcat/Km s^-1 M^-1 raw 1.0 x 10^6 +/- 0.1 x 10^6; normalized kcat 82.3 s^-1, Km 0.08 mM, same-row kcat/Km 1028.75 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=82.3 normalized_unit=s^-1; Km normalized_value=0.08 normalized_unit=mM from 80 +/- 5 uM / 1000; kcat/Km normalized_value=1028.75 normalized_unit=s^-1*mM^-1 from same-row kcat/Km; printed efficiency=1.0 x 10^6 +/- 0.1 x 10^6 s^-1 M^-1

raw_value_unit_evidence: kcat raw_value=82.3 +/- 1.4 raw_unit=s^-1; Km raw_value=80 +/- 5 raw_unit=uM; kcat/Km raw_value=1.0 x 10^6 +/- 0.1 x 10^6 raw_unit=s^-1 M^-1

row_label: RsMCD WT / (2S)-methylsuccinyl-CoA


organism: Cereibacter sphaeroides

source_db: uniprot

verification_status: unverified

kcat_display: Not reported

kcat_over_km_display: Not reported

assay_conditions_summary: cofactor CoA

status: unverified

source: uniprot


enzyme_display_name: Dihydroorotate dehydrogenase (fumarate)

organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)

substrate_name: dihydroorotate

enzyme: Dihydroorotate dehydrogenase (fumarate)

substrate: dihydroorotate


substrate_name: fumarate

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

assay_conditions_summary: pH 8

column_label: Figure 9 caption reports Vmax 8.5 s^-1, Km for DHO 14 microM, and Km for fumarate 80 microM.

raw_value_unit_evidence: Km raw_value=80 microM raw_unit=microM

row_label: T. brucei DHODH / fumarate-dependent activity

table_label: Official PMC full-text Figure 9 caption

substrate: fumarate


enzyme_display_name: dihydroorotate oxidase (fumarate)

organism: Saccharomyces cerevisiae

substrate_name: Fumarate

source_db: oed

proof_lines:
fumarate
dihydroorotate
electron acceptors

enzyme: dihydroorotate oxidase (fumarate)

substrate: Fumarate

source: oed


substrate_name: L-Dihydroorotate

proof_lines: dihydroorotate DHOD orotate

substrate: L-Dihydroorotate


enzyme_display_name: crotonobetainyl-CoA reductase

organism: Escherichia coli

substrate_name: crotonobetaine

enzyme: crotonobetainyl-CoA reductase

substrate: crotonobetaine


enzyme_display_name: Dihydroorotate dehydrogenase A (fumarate)

organism: Lactococcus lactis subsp. cremoris (strain MG1363)

column_label: Table II, row Native, column Kapp for DHO (uM), cell 18 +/- 4. The table caption states these are apparent KM values for DHO using fumarate as electron acceptor.

normalized_value_unit_evidence: Expected export Km 0.018 mM; Table II Kapp for DHO 18 uM = 0.018 mM.

raw_value_unit_evidence: Table II row Native: Kapp for DHO = 18 +/- 4 uM.

row_label: Native

table_label: Table II: Dissociation constants for orotate and kinetic data for native and mutant enzymes using fumarate as electron acceptor


proof_lines:
Lactococcus lactis DHODA
dihydroorotate
orotate

enzyme: Dihydroorotate dehydrogenase A (fumarate)


enzyme_display_name: dihydroorotate dehydrogenase (fumarate)

organism: Lactococcus lactis

substrate_name: O2; L-Dihydroorotate

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

enzyme: dihydroorotate dehydrogenase (fumarate)

substrate: O2; L-Dihydroorotate


organism: Rattus norvegicus

ki_unit: mM


substrate_name: L-Dihydroorotate; O2

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

sequence_source: multiple

substrate: L-Dihydroorotate; O2


organism: Saccharomyces kluyveri

substrate_name: L-Dihydroorotate; Fumarate

substrate: L-Dihydroorotate; Fumarate


enzyme_display_name: UniProt A9XWD7

organism: Sterolibacterium denitrificans

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt A9XWD7

source: skid


enzyme_display_name: UniProt Q9RA02

organism: Rhodococcus erythropolis

substrate_name: cortisone

enzyme: UniProt Q9RA02

substrate: cortisone


substrate_name: testosterone

substrate: testosterone


substrate_name: progesterone

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=30°C, pH=7.4

substrate: progesterone


substrate_name: cortexolone

substrate: cortexolone


proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=22°C, pH=8
Raw SKiD Env: Temp=30°C, pH=7.4


enzyme_display_name: Coproheme decarboxylase

organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: chlorite

smiles: [O-]Cl=O

proof_lines: kcat is 0.77 sec(-1) with chlorite and 0.52 sec(-1) with hydrogen peroxide. The kcat values are at least 1000 times lower than those observed for well-characterized chlorite dismutases, and the specific activity is even lower.

enzyme: Coproheme decarboxylase

substrate: chlorite


substrate_name: hydrogen peroxide

smiles: OO

substrate: hydrogen peroxide


organism: Enterococcus faecalis


enzyme_display_name: hydrogen peroxide-dependent heme synthase

organism: Listeria monocytogenes

proof_lines:
Listeria monocytogenes
HemQ
coproheme


column_label: PMID 15196933 Table 2. Kinetic constants of the purified full-length and truncated yeast DHODH. Row group Fumarate variable + DHO / DHODH Skcyt; columns kcat (s^-1), kcat/Km (M^-1 s^-1), Km (uM).

normalized_value_unit_evidence: kcat=2.7 s^-1; kcat_over_km=64.28571428571429 s^-1 mM^-1; same Table 2 row explicitly reports kcat/Km=6.4 x 10^4 M^-1 s^-1; Km=0.042 mM

row_label: Fumarate variable + DHO / DHODH Skcyt


column_label: PMID 15196933 Table 2. Kinetic constants of the purified full-length and truncated yeast DHODH. Row group DHO variable + fumarate / DHODH SKcyt; columns kcat (s^-1), kcat/Km (M^-1 s^-1), Km (uM).

normalized_value_unit_evidence: kcat=2.6 s^-1; kcat_over_km=130.0 s^-1 mM^-1; same Table 2 row explicitly reports kcat/Km=1.3 x 10^5 M^-1 s^-1; Km=0.02 mM

row_label: DHO variable + fumarate / DHODH SKcyt


enzyme_display_name: UniProt Q4D3W2

organism: Trypanosoma cruzi

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

source_databases_merged: skid uniprot

enzyme: UniProt Q4D3W2


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A282F/F284A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer pH 7; cofactor CoA

row_label: RsMCD A282F/F284A / (2S)-methylsuccinyl-CoA

table_label: Table 2. Michaelis-Menten kinetic parameters for the wildtype and mutant RsMCD with either (2S)-methylsuccinyl-CoA or succinyl-CoA as substrate


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +4, so it is treated as a source-provided variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA


enzyme_display_name: 3-oxosteroid 1-dehydrogenase

organism: Pimelobacter simplex

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

proof_lines:
pH 7.0, 30°C, recombinant isozyme KsdD3
pH 7.5, 35°C, recombinant isozyme KsdD3

enzyme: 3-oxosteroid 1-dehydrogenase


substrate_name: cortisone acetate

substrate: cortisone acetate


proof_lines:
pH 7.5, 35°C, recombinant isozyme KsdD3
pH 7.0, 30°C, recombinant isozyme KsdD3


substrate_name: canrenone

substrate: canrenone


enzyme_display_name: dihydroorotate dehydrogenase

organism: Plasmodium falciparum

km_display: Not reported

proof_lines: at saturating concentration of dihydroorotate

enzyme: dihydroorotate dehydrogenase


organism: Candida albicans

substrate_name: L-dihydroorotate

substrate: L-dihydroorotate


organism: Homo sapiens

proof_lines: type II isozyme, pH not specified in the publication, temperature not specified in the publication

proof_lines: type I isozyme, pH not specified in the publication, temperature not specified in the publication


organism: Mesocricetus auratus

proof_lines: Srd5a2, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: 2-furoyl-CoA dehydrogenase

organism: Pseudomonas putida

enzyme: 2-furoyl-CoA dehydrogenase


substrate_name: Unknown

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

substrate: Unknown


organism: Mycolicibacterium smegmatis


enzyme_display_name: 3-oxo-5beta-steroid 4-dehydrogenase

organism: [Clostridium] innocuum

enzyme: 3-oxo-5beta-steroid 4-dehydrogenase


enzyme_display_name: coproporphyrinogen dehydrogenase

organism: Niallia circulans

substrate_name: S-adenosyl-L-methionine

proof_lines: apparent value, in 50 mM HEPES-NaOH (pH 8.0) in the presence of 10 mM sodium dithionite at 28°C

proof_lines: apparent value, in the presence of sodium dithionite (10 mM), at room temperature

enzyme: coproporphyrinogen dehydrogenase

substrate: S-adenosyl-L-methionine


proof_lines: in 50 mM HEPES-NaOH (pH 8.0) in the presence of 10 mM sodium dithionite at 28°C


organism: Rhodococcus jostii

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q0S4Q9 and applied mutation signature W136F to reconstruct the assayed variant sequence.

column_label: Table 3 (apparent kinetic parameters of the R. jostii Ro05698 Delta4-(5alpha)-KSTD, 1-(5alpha)-AD as substrate), printed enzyme line 'W136F'; column 'Km (uM)' = 66; column 'kcat (s^-1)' = 0.7; column 'kcat/Km (s^-1 M^-1)' = 1 x 10^4; column 'Vmax (nmol mg^-1 min^-1)' = 8 x 10^2.

normalized_value_unit_evidence: Km: printed Table 3 cell 66 in a column headed Km (uM); 1 uM is 0.001 mM, so 66 uM / 1000 = 0.066 mM. kcat: printed Table 3 cell 0.7 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.7 s^(-1). kcat/Km: printed Table 3 cell 1 x 10^4 in a column headed kcat/Km (s^-1 M^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1 x 10^4 / 1000 = 10.0 s^(-1)*mM^(-1). The catalog side of this record carries kcat 0.7 s^(-1), Km 0.066 mM and kcat_over_km 10.606060606060606 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, printed enzyme line 'W136F': Km (uM) = 66; kcat (s^-1) = 0.7; kcat/Km (s^-1 M^-1) = 1 x 10^4.

row_label: Table 3, printed enzyme line 'W136F'

table_label: Table 3: Apparent kinetic parameters of the R. jostii Ro05698 Delta4-(5alpha)-KSTD wild type and active site mutants using 1-(5alpha)-AD as substrate (J Biol Chem 2012, 287(37):30975-30983). Printed column heads, in printed order: (enzyme, unlabelled first column); Vmax in nmol mg^-1 min^-1; Km in uM; kcat in s^-1; kcat/Km in s^-1 M^-1. Footnote b of the table reads that ND means not detectable.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q0S4Q9 and applied mutation signature S468T to reconstruct the assayed variant sequence.

column_label: Table 3 (apparent kinetic parameters of the R. jostii Ro05698 Delta4-(5alpha)-KSTD, 1-(5alpha)-AD as substrate), printed enzyme line 'S468T'; column 'Km (uM)' = 17 x 10^1; column 'kcat (s^-1)' = 1.6; column 'kcat/Km (s^-1 M^-1)' = 9 x 10^3; column 'Vmax (nmol mg^-1 min^-1)' = 19 x 10^2.

normalized_value_unit_evidence: Km: printed Table 3 cell 17 x 10^1 in a column headed Km (uM); 1 uM is 0.001 mM, so 17 x 10^1 uM / 1000 = 0.17 mM. kcat: printed Table 3 cell 1.6 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 1.6 s^(-1). kcat/Km: printed Table 3 cell 9 x 10^3 in a column headed kcat/Km (s^-1 M^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9 x 10^3 / 1000 = 9.0 s^(-1)*mM^(-1). The catalog side of this record carries kcat 1.6 s^(-1), Km 0.17 mM and kcat_over_km 9.411764705882353 s^(-1)*mM^(-1).

row_label: Table 3, printed enzyme line 'S468T'


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


enzyme_display_name: UniProt Q0S4Q9

proof_lines: kcat is 2.4 sec(-1) with 5alpha-androst-1-ene-3,17-dione as substrate.

enzyme: UniProt Q0S4Q9


organism: Rattus norvegicus


enzyme_display_name: 3-oxo-5-alpha-steroid 4-dehydrogenase

organism: Rhodococcus jostii (strain RHA1)

enzyme: 3-oxo-5-alpha-steroid 4-dehydrogenase


organism: Comamonas testosteroni


source_databases_merged: brenda uniprot


verification_status: corrected

column_label: Table 2 row Cortexolone under MsKstD1 columns: Km 93.3 +/- 8.6 uM; kcat 94.2 +/- 7.2 /s; kcat/Km 1.0 x 10^6 /s/M.

normalized_value_unit_evidence: kcat 94.2 s^-1; Km 0.0933 mM; kcat/Km 1000.0 s^-1 mM^-1 from the explicit Table 2 kcat/Km column

raw_value_unit_evidence: Table 2 row cortexolone: kcat 94.2 s^-1; Km 93.3 uM; kcat/Km 1000000.0 s^-1 M^-1.

row_label: Cortexolone / MsKstD1

table_label: Table 2

status: corrected


column_label: Table 2 row AD under MsKstD1 columns: Km 138.5 +/- 11.3 uM; kcat 51.5 +/- 4.5 /s; kcat/Km 3.7 x 10^5 /s/M.

normalized_value_unit_evidence: kcat 51.5 s^-1; Km 0.1385 mM; kcat/Km 370.0 s^-1 mM^-1 from the explicit Table 2 kcat/Km column

raw_value_unit_evidence: Table 2 row 4-androstene-3,17-dione: kcat 51.5 s^-1; Km 138.5 uM; kcat/Km 370000.0 s^-1 M^-1.

row_label: AD / MsKstD1


column_label: Table 2 row 17alpha-OH-P under MsKstD1 columns: Km 91.7 +/- 8.0 uM; kcat 110.4 +/- 9.3 /s; kcat/Km 1.2 x 10^6 /s/M.

normalized_value_unit_evidence: kcat 110.4 s^-1; Km 0.0917 mM; kcat/Km 1200.0 s^-1 mM^-1 from the explicit Table 2 kcat/Km column

raw_value_unit_evidence: Table 2 row 17alpha-hydroxypregn-4-ene-3,20-dione: kcat 110.4 s^-1; Km 91.7 uM; kcat/Km 1200000.0 s^-1 M^-1.

row_label: 17alpha-OH-P / MsKstD1


column_label: Table 2 row 17-Carboxylic acid under MsKstD1 columns: Km 210.2 +/- 18.3 uM; kcat 94.1 +/- 7.6 /s; kcat/Km 4.5 x 10^5 /s/M.

normalized_value_unit_evidence: kcat 94.1 s^-1; Km 0.2102 mM; kcat/Km 450.0 s^-1 mM^-1 from the explicit Table 2 kcat/Km column

raw_value_unit_evidence: Table 2 row 4-androsten-3-one-5-ene-17-carboxylic acid: kcat 94.1 s^-1; Km 210.2 uM; kcat/Km 450000.0 s^-1 M^-1.

row_label: 17-Carboxylic acid / MsKstD1


column_label: Table 2 row Progesterone under MsKstD1 columns: Km 66.7 +/- 8.8 uM; kcat 127.8 +/- 12.1 /s; kcat/Km 1.9 x 10^6 /s/M.

normalized_value_unit_evidence: kcat 127.8 s^-1; Km 0.0667 mM; kcat/Km 1900.0 s^-1 mM^-1 from the explicit Table 2 kcat/Km column

raw_value_unit_evidence: Table 2 row progesterone: kcat 127.8 s^-1; Km 66.7 uM; kcat/Km 1900000.0 s^-1 M^-1.

row_label: Progesterone / MsKstD1


organism: Sterolibacterium denitrificans


enzyme_display_name: Dihydroorotate dehydrogenase (fumarate)

organism: Trypanosoma cruzi (strain CL Brener)

substrate_name: dihydroorotate

proof_lines: The attached memo points to a fumarate context, not this row's dihydroorotate measurement.

substrate: dihydroorotate


organism: Rhodococcus erythropolis


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y119F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y487F to reconstruct the assayed variant sequence.


organism: Gordonia rubripertincta


substrate_name: androsterone

substrate: androsterone


substrate_name: testololactone

substrate: testololactone


proof_lines: i.e. 4-pregnene-11alpha-ol-3,20-dione, 11beta-hydroxy-4-androstene-3,17-dione, 4-estren-3,17-dione


substrate_name: corticosterone

substrate: corticosterone


substrate_name: hydrocorticosterone

substrate: hydrocorticosterone


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: progesterone (at pH 7.4 and 30 degrees Celsius)


substrate_name: 5alpha-androstane-3,17-dione (5alpha-AD)(at pH 7.4 and 30 degrees Celsius)


organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)

smiles: [Ho]

assay_conditions_summary: pH 7


enzyme_display_name: dihydroorotate dehydrogenase (quinone)

organism: Bos taurus

substrate_name: menadione

enzyme: dihydroorotate dehydrogenase (quinone)

substrate: menadione


substrate_name: coenzyme Q6

substrate: coenzyme Q6


substrate_name: methyl-dihydroorotate

substrate: methyl-dihydroorotate


organism: Mycolicibacterium neoaurum

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

proof_lines:
recombinant enzyme, pH 8.0, 40°C
pH 7.0, 30°C


enzyme_display_name: butyryl-CoA dehydrogenase

substrate_name: Butanoyl-CoA; Acceptor

enzyme: butyryl-CoA dehydrogenase

substrate: Butanoyl-CoA; Acceptor


enzyme_display_name: medium-chain acyl-CoA dehydrogenase

substrate_name: decanoyl-CoA

enzyme: medium-chain acyl-CoA dehydrogenase

substrate: decanoyl-CoA


substrate_name: octanoyl-CoA

substrate: octanoyl-CoA


substrate_name: hexanoyl-CoA

substrate: hexanoyl-CoA


column_label: Table 2 row Hydrocortisone under ReKstD columns: Km 46.3 +/- 4.3 uM; kcat 50.2 +/- 5.2 /s; kcat/Km 1.1 x 10^6 /s/M.

normalized_value_unit_evidence: kcat 50.2 s^-1; Km 0.0463 mM; kcat/Km 1100.0 s^-1 mM^-1 from the explicit Table 2 kcat/Km column

raw_value_unit_evidence: Table 2 row 11beta,17alpha,21-trihydroxypregn-4-ene-3,20-dione: kcat 50.2 s^-1; Km 46.3 uM; kcat/Km 1100000.0 s^-1 M^-1.

row_label: Hydrocortisone / ReKstD


assay_conditions_summary: pH 8; 303.15 K; buffer 50 mM Tris-HCl

column_label: Table label: Table 2 Kinetic parameters of the purified MsKstD1 and ReKstD. Row: HA. Enzyme column group: ReKstD. Columns read: K m (μM) cell 23.2, k cat (/s) cell 20.3, k cat / K m (/s/M) cell 8.8 x 10^5. metric: kcat; raw value: 20.3; raw unit: s^-1; normalized value: 20.3 s^(-1); metric: Km; raw value: 23.2; raw unit: uM; normalized value: 0.0232 mM; metric: kcat/Km; raw value: 8.8 × 10^5; raw unit: /s/M; normalized value: 880 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified recombinant ReKstD (KstD cloned from Rhodococcus erythropolis WY1406, expressed in E. coli). Kinetic constants were determined in a 1 mL reaction mixture containing 1.5 mM PMS, 40 μM DCPIP, purified enzyme and varying steroid substrate concentrations in 50 mM Tris-HCl buffer; reaction rates were read as DCPIP absorbance at 600 nm on a multi-detection microplate reader at 30 C, and Km and Vmax were obtained by fitting the Michaelis-Menten equation. Export row conditions: pH 8; 303.15 K.

normalized_value_unit_evidence: ReKstD columns of Table 2 row HA: kcat 20.3 /s = 20.3 s^(-1); Km 23.2 μM = 0.0232 mM (1 uM = 0.001 mM); kcat/Km primary cell 8.8 × 10^5 /s/M = 880 s^-1 mM^-1 (1 /s/M = 0.001 s^-1 mM^-1). In the text extraction of the publisher PDF the multiplication sign renders as ×, the micro sign as μ, the plus-minus as ±, and superscript exponents are flattened onto the mantissa, so the printed cell `8.8 × 105` is the paper's 8.8 x 10^5 /s/M = 880.0000000000001 s^-1 mM^-1 (1 /s/M = 0.001 s^-1 mM^-1).

raw_value_unit_evidence: Table 2 Kinetic parameters of the purified MsKstD1 and ReKstD | column group header row of Table 2: Substrate MsKstD1 ReKstD | metric header row: Km (μM) kcat (/s) kcat/Km (/s/M) Km (μM) kcat (/s) kcat/Km (/s/M) (first metric triplet = MsKstD1, second metric triplet = ReKstD) | row: HA 100.3 ± 12.1 77.2 ± 6.1 7.7 × 105 23.2 ± 2.8 20.3 ± 1.6 8.8 × 105 | ReKstD cells read: K m = 23.2 μM; k cat = 20.3 /s; k cat / K m = 8.8 x 10^5 /s/M

row_label: ReKstD | HA


column_label: Table label: Table 2 Kinetic parameters of the purified MsKstD1 and ReKstD. Row: 17α-OH-P. Enzyme column group: ReKstD. Columns read: K m (μM) cell 18.2, k cat (/s) cell 21.4, k cat / K m (/s/M) cell 1.2 x 10^6. metric: kcat; raw value: 21.4; raw unit: s^-1; normalized value: 21.4 s^(-1); metric: Km; raw value: 18.2; raw unit: uM; normalized value: 0.0182 mM; metric: kcat/Km; raw value: 1.2 × 10^6; raw unit: /s/M; normalized value: 1200 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified recombinant ReKstD (KstD cloned from Rhodococcus erythropolis WY1406, expressed in E. coli). Kinetic constants were determined in a 1 mL reaction mixture containing 1.5 mM PMS, 40 μM DCPIP, purified enzyme and varying steroid substrate concentrations in 50 mM Tris-HCl buffer; reaction rates were read as DCPIP absorbance at 600 nm on a multi-detection microplate reader at 30 C, and Km and Vmax were obtained by fitting the Michaelis-Menten equation. Export row conditions: pH 8; 303.15 K.

normalized_value_unit_evidence: ReKstD columns of Table 2 row 17α-OH-P: kcat 21.4 /s = 21.4 s^(-1); Km 18.2 μM = 0.0182 mM (1 uM = 0.001 mM); kcat/Km primary cell 1.2 × 10^6 /s/M = 1200 s^-1 mM^-1 (1 /s/M = 0.001 s^-1 mM^-1). In the text extraction of the publisher PDF the multiplication sign renders as ×, the micro sign as μ, the plus-minus as ±, and superscript exponents are flattened onto the mantissa, so the printed cell `1.2 × 106` is the paper's 1.2 x 10^6 /s/M = 1200.0 s^-1 mM^-1 (1 /s/M = 0.001 s^-1 mM^-1).

raw_value_unit_evidence: Table 2 Kinetic parameters of the purified MsKstD1 and ReKstD | column group header row of Table 2: Substrate MsKstD1 ReKstD | metric header row: Km (μM) kcat (/s) kcat/Km (/s/M) Km (μM) kcat (/s) kcat/Km (/s/M) (first metric triplet = MsKstD1, second metric triplet = ReKstD) | row: 17α-OH-P 91.7 ± 8.0 110.4 ± 9.3 1.2 × 106 18.2 ± 1.1 21.4 ± 1.8 1.2 × 106 | ReKstD cells read: K m = 18.2 μM; k cat = 21.4 /s; k cat / K m = 1.2 x 10^6 /s/M

row_label: ReKstD | 17α-OH-P


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


column_label: Table label: Table 2 Kinetic parameters of the purified MsKstD1 and ReKstD. Row: 21-Cl. Enzyme column group: ReKstD. Columns read: K m (μM) cell 19.3, k cat (/s) cell 12.8, k cat / K m (/s/M) cell 6.6 x 10^5. metric: kcat; raw value: 12.8; raw unit: s^-1; normalized value: 12.8 s^(-1); metric: Km; raw value: 19.3; raw unit: uM; normalized value: 0.0193 mM; metric: kcat/Km; raw value: 6.6 × 10^5; raw unit: /s/M; normalized value: 660 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified recombinant ReKstD (KstD cloned from Rhodococcus erythropolis WY1406, expressed in E. coli). Kinetic constants were determined in a 1 mL reaction mixture containing 1.5 mM PMS, 40 μM DCPIP, purified enzyme and varying steroid substrate concentrations in 50 mM Tris-HCl buffer; reaction rates were read as DCPIP absorbance at 600 nm on a multi-detection microplate reader at 30 C, and Km and Vmax were obtained by fitting the Michaelis-Menten equation. Export row conditions: pH 8; 303.15 K.

normalized_value_unit_evidence: ReKstD columns of Table 2 row 21-Cl: kcat 12.8 /s = 12.8 s^(-1); Km 19.3 μM = 0.0193 mM (1 uM = 0.001 mM); kcat/Km primary cell 6.6 × 10^5 /s/M = 660 s^-1 mM^-1 (1 /s/M = 0.001 s^-1 mM^-1). In the text extraction of the publisher PDF the multiplication sign renders as ×, the micro sign as μ, the plus-minus as ±, and superscript exponents are flattened onto the mantissa, so the printed cell `6.6 × 105` is the paper's 6.6 x 10^5 /s/M = 660.0 s^-1 mM^-1 (1 /s/M = 0.001 s^-1 mM^-1).

raw_value_unit_evidence: Table 2 Kinetic parameters of the purified MsKstD1 and ReKstD | column group header row of Table 2: Substrate MsKstD1 ReKstD | metric header row: Km (μM) kcat (/s) kcat/Km (/s/M) Km (μM) kcat (/s) kcat/Km (/s/M) (first metric triplet = MsKstD1, second metric triplet = ReKstD) | row: 21-Cl 98.5 ± 9.3 63.5 ± 5.8 6.5 × 105 19.3 ± 2.6 12.8 ± 1.5 6.6 × 105 | ReKstD cells read: K m = 19.3 μM; k cat = 12.8 /s; k cat / K m = 6.6 x 10^5 /s/M

row_label: ReKstD | 21-Cl


column_label: Table label: Table 2 Kinetic parameters of the purified MsKstD1 and ReKstD. Row: 17-Carboxylic acid. Enzyme column group: ReKstD. Columns read: K m (μM) cell 246.2, k cat (/s) cell 40.8, k cat / K m (/s/M) cell 1.7 x 10^5. metric: kcat; raw value: 40.8; raw unit: s^-1; normalized value: 40.8 s^(-1); metric: Km; raw value: 246.2; raw unit: uM; normalized value: 0.2462 mM; metric: kcat/Km; raw value: 1.7 × 10^5; raw unit: /s/M; normalized value: 170 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified recombinant ReKstD (KstD cloned from Rhodococcus erythropolis WY1406, expressed in E. coli). Kinetic constants were determined in a 1 mL reaction mixture containing 1.5 mM PMS, 40 μM DCPIP, purified enzyme and varying steroid substrate concentrations in 50 mM Tris-HCl buffer; reaction rates were read as DCPIP absorbance at 600 nm on a multi-detection microplate reader at 30 C, and Km and Vmax were obtained by fitting the Michaelis-Menten equation. Export row conditions: pH 8; 303.15 K.

normalized_value_unit_evidence: ReKstD columns of Table 2 row 17-Carboxylic acid: kcat 40.8 /s = 40.8 s^(-1); Km 246.2 μM = 0.2462 mM (1 uM = 0.001 mM); kcat/Km primary cell 1.7 × 10^5 /s/M = 170 s^-1 mM^-1 (1 /s/M = 0.001 s^-1 mM^-1). In the text extraction of the publisher PDF the multiplication sign renders as ×, the micro sign as μ, the plus-minus as ±, and superscript exponents are flattened onto the mantissa, so the printed cell `1.7 × 105` is the paper's 1.7 x 10^5 /s/M = 170.0 s^-1 mM^-1 (1 /s/M = 0.001 s^-1 mM^-1).

raw_value_unit_evidence: Table 2 Kinetic parameters of the purified MsKstD1 and ReKstD | column group header row of Table 2: Substrate MsKstD1 ReKstD | metric header row: Km (μM) kcat (/s) kcat/Km (/s/M) Km (μM) kcat (/s) kcat/Km (/s/M) (first metric triplet = MsKstD1, second metric triplet = ReKstD) | row: 17-Carboxylic acid 210.2 ± 18.3 94.1 ± 7.6 4.5 × 105 246.2 ± 20.1 40.8 ± 4.2 1.7 × 105 | ReKstD cells read: K m = 246.2 μM; k cat = 40.8 /s; k cat / K m = 1.7 x 10^5 /s/M

row_label: ReKstD | 17-Carboxylic acid


column_label: Table label: Table 2 Kinetic parameters of the purified MsKstD1 and ReKstD. Row: 9-OH-AD. Enzyme column group: ReKstD. Columns read: K m (μM) cell 50.9, k cat (/s) cell 21.4, k cat / K m (/s/M) cell 4.2 x 10^5. metric: kcat; raw value: 21.4; raw unit: s^-1; normalized value: 21.4 s^(-1); metric: Km; raw value: 50.9; raw unit: uM; normalized value: 0.0509 mM; metric: kcat/Km; raw value: 4.2 × 10^5; raw unit: /s/M; normalized value: 420 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified recombinant ReKstD (KstD cloned from Rhodococcus erythropolis WY1406, expressed in E. coli). Kinetic constants were determined in a 1 mL reaction mixture containing 1.5 mM PMS, 40 μM DCPIP, purified enzyme and varying steroid substrate concentrations in 50 mM Tris-HCl buffer; reaction rates were read as DCPIP absorbance at 600 nm on a multi-detection microplate reader at 30 C, and Km and Vmax were obtained by fitting the Michaelis-Menten equation. Export row conditions: pH 8; 303.15 K.

normalized_value_unit_evidence: ReKstD columns of Table 2 row 9-OH-AD: kcat 21.4 /s = 21.4 s^(-1); Km 50.9 μM = 0.0509 mM (1 uM = 0.001 mM); kcat/Km primary cell 4.2 × 10^5 /s/M = 420 s^-1 mM^-1 (1 /s/M = 0.001 s^-1 mM^-1). In the text extraction of the publisher PDF the multiplication sign renders as ×, the micro sign as μ, the plus-minus as ±, and superscript exponents are flattened onto the mantissa, so the printed cell `4.2 × 105` is the paper's 4.2 x 10^5 /s/M = 420.0 s^-1 mM^-1 (1 /s/M = 0.001 s^-1 mM^-1).

raw_value_unit_evidence: Table 2 Kinetic parameters of the purified MsKstD1 and ReKstD | column group header row of Table 2: Substrate MsKstD1 ReKstD | metric header row: Km (μM) kcat (/s) kcat/Km (/s/M) Km (μM) kcat (/s) kcat/Km (/s/M) (first metric triplet = MsKstD1, second metric triplet = ReKstD) | row: 9-OH-AD 36.9 ± 4.6 58.7 ± 4.7 1.6 × 106 50.9 ± 3.3 21.4 ± 1.8 4.2 × 105 | ReKstD cells read: K m = 50.9 μM; k cat = 21.4 /s; k cat / K m = 4.2 x 10^5 /s/M

row_label: ReKstD | 9-OH-AD


column_label: Table 2 row Diene under ReKstD columns: Km 14 +/- 1.9 uM; kcat 22.3 +/- 2.1 /s; kcat/Km 1.6 x 10^6 /s/M.

normalized_value_unit_evidence: kcat 22.3 s^-1; Km 0.014 mM; kcat/Km 1600.0 s^-1 mM^-1 from the explicit Table 2 kcat/Km column

row_label: Diene / ReKstD


substrate_name: cortexolone

column_label: Table 2 row Cortexolone under ReKstD columns: Km 12.3 +/- 0.8 uM; kcat 20.6 +/- 2.3 /s; kcat/Km 1.7 x 10^6 /s/M.

normalized_value_unit_evidence: kcat 20.6 s^-1; Km 0.0123 mM; kcat/Km 1700.0 s^-1 mM^-1 from the explicit Table 2 kcat/Km column

raw_value_unit_evidence: Table 2 row cortexolone: kcat 20.6 s^-1; Km 12.3 uM; kcat/Km 1700000.0 s^-1 M^-1.

row_label: Cortexolone / ReKstD

substrate: cortexolone


substrate_name: cortisone

column_label: Table label: Table 2 Kinetic parameters of the purified MsKstD1 and ReKstD. Row: Cortisone. Enzyme column group: ReKstD. Columns read: K m (μM) cell 27.2, k cat (/s) cell 24.6, k cat / K m (/s/M) cell 9.0 x 10^5. metric: kcat; raw value: 24.6; raw unit: s^-1; normalized value: 24.6 s^(-1); metric: Km; raw value: 27.2; raw unit: uM; normalized value: 0.0272 mM; metric: kcat/Km; raw value: 9.0 × 10^5; raw unit: /s/M; normalized value: 900 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified recombinant ReKstD (KstD cloned from Rhodococcus erythropolis WY1406, expressed in E. coli). Kinetic constants were determined in a 1 mL reaction mixture containing 1.5 mM PMS, 40 μM DCPIP, purified enzyme and varying steroid substrate concentrations in 50 mM Tris-HCl buffer; reaction rates were read as DCPIP absorbance at 600 nm on a multi-detection microplate reader at 30 C, and Km and Vmax were obtained by fitting the Michaelis-Menten equation. Export row conditions: pH 8; 303.15 K.

normalized_value_unit_evidence: ReKstD columns of Table 2 row Cortisone: kcat 24.6 /s = 24.6 s^(-1); Km 27.2 μM = 0.0272 mM (1 uM = 0.001 mM); kcat/Km primary cell 9.0 × 10^5 /s/M = 900 s^-1 mM^-1 (1 /s/M = 0.001 s^-1 mM^-1). In the text extraction of the publisher PDF the multiplication sign renders as ×, the micro sign as μ, the plus-minus as ±, and superscript exponents are flattened onto the mantissa, so the printed cell `9.0 × 105` is the paper's 9.0 x 10^5 /s/M = 900.0 s^-1 mM^-1 (1 /s/M = 0.001 s^-1 mM^-1).

raw_value_unit_evidence: Table 2 Kinetic parameters of the purified MsKstD1 and ReKstD | column group header row of Table 2: Substrate MsKstD1 ReKstD | metric header row: Km (μM) kcat (/s) kcat/Km (/s/M) Km (μM) kcat (/s) kcat/Km (/s/M) (first metric triplet = MsKstD1, second metric triplet = ReKstD) | row: Cortisone 85.3 ± 7.8 52.2 ± 4.1 6.1 × 105 27.2 ± 2.8 24.6 ± 2.9 9.0 × 105 | ReKstD cells read: K m = 27.2 μM; k cat = 24.6 /s; k cat / K m = 9.0 x 10^5 /s/M

row_label: ReKstD | Cortisone

substrate: cortisone


enzyme_display_name: short-chain acyl-CoA dehydrogenase

organism: Clostridioides difficile

substrate_name: butyryl-CoA

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: short-chain acyl-CoA dehydrogenase

substrate: butyryl-CoA


substrate_name: NADH

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH

substrate: NADH


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


substrate_name: reduced ferredoxin

substrate: reduced ferredoxin


enzyme_display_name: succinate dehydrogenase

organism: Escherichia coli

substrate_name: menaquinol

proof_lines:
mutant R28N, pH 8.0, 30°C
mutant R28N, pH 7.0, 30°C

enzyme: succinate dehydrogenase

substrate: menaquinol


proof_lines:
mutant R28L, pH 8.0, 30°C
mutant R28L, pH 7.0, 30°C


proof_lines:
mutant R81K, pH 7.0, 30°C
mutant R81K, pH 8.0, 30°C


proof_lines:
wild-type, pH 8.0, 30°C
wild-type, pH 7.0, 30°C


enzyme_display_name: isovaleryl-CoA dehydrogenase

organism: Homo sapiens

substrate_name: isovaleryl-CoA

enzyme: isovaleryl-CoA dehydrogenase

substrate: isovaleryl-CoA


proof_lines: purified V342A mutant, electron acceptor: dichlorophenol indophenol

proof_lines: purified V342A mutant, electron acceptor: electron-transferring flavoprotein


proof_lines: purified R382L mutant, electron acceptor: dichlorophenol indophenol

proof_lines: purified R382L mutant, electron acceptor: electron-transferring flavoprotein


proof_lines: purified A282V mutant, electron acceptor: electron-transferring flavoprotein

proof_lines: purified A282V mutant, electron acceptor: dichlorophenol indophenol


proof_lines: purified wild-type enzyme, electron acceptor: electron-transferring flavoprotein

proof_lines: purified wild-type enzyme, electron acceptor: dichlorophenol indophenol


organism: Rhodococcus ruber

substrate_name: deoxycorticosterone

substrate: deoxycorticosterone


substrate_name: progesterone

substrate: progesterone


substrate_name: testosterone

substrate: testosterone


substrate_name: 4-pregnen-3-one-20beta-carboxylic acid

substrate: 4-pregnen-3-one-20beta-carboxylic acid


substrate_name: corticosterone

substrate: corticosterone


column_label: Table label: Table 2 Kinetic parameters of the purified MsKstD1 and ReKstD. Row: Progesterone. Enzyme column group: ReKstD. Columns read: K m (μM) cell 20.2, k cat (/s) cell 25.4, k cat / K m (/s/M) cell 1.3 x 10^6. metric: kcat; raw value: 25.4; raw unit: s^-1; normalized value: 25.4 s^(-1); metric: Km; raw value: 20.2; raw unit: uM; normalized value: 0.0202 mM; metric: kcat/Km; raw value: 1.3 × 10^6; raw unit: /s/M; normalized value: 1300 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified recombinant ReKstD (KstD cloned from Rhodococcus erythropolis WY1406, expressed in E. coli). Kinetic constants were determined in a 1 mL reaction mixture containing 1.5 mM PMS, 40 μM DCPIP, purified enzyme and varying steroid substrate concentrations in 50 mM Tris-HCl buffer; reaction rates were read as DCPIP absorbance at 600 nm on a multi-detection microplate reader at 30 C, and Km and Vmax were obtained by fitting the Michaelis-Menten equation. Export row conditions: pH 8; 303.15 K.

normalized_value_unit_evidence: ReKstD columns of Table 2 row Progesterone: kcat 25.4 /s = 25.4 s^(-1); Km 20.2 μM = 0.0202 mM (1 uM = 0.001 mM); kcat/Km primary cell 1.3 × 10^6 /s/M = 1300 s^-1 mM^-1 (1 /s/M = 0.001 s^-1 mM^-1). In the text extraction of the publisher PDF the multiplication sign renders as ×, the micro sign as μ, the plus-minus as ±, and superscript exponents are flattened onto the mantissa, so the printed cell `1.3 × 106` is the paper's 1.3 x 10^6 /s/M = 1300.0 s^-1 mM^-1 (1 /s/M = 0.001 s^-1 mM^-1).

raw_value_unit_evidence: Table 2 Kinetic parameters of the purified MsKstD1 and ReKstD | column group header row of Table 2: Substrate MsKstD1 ReKstD | metric header row: Km (μM) kcat (/s) kcat/Km (/s/M) Km (μM) kcat (/s) kcat/Km (/s/M) (first metric triplet = MsKstD1, second metric triplet = ReKstD) | row: Progesterone 66.7 ± 8.8 127.8 ± 12.1 1.9 × 106 20.2 ± 2.0 25.4 ± 2.5 1.3 × 106 | ReKstD cells read: K m = 20.2 μM; k cat = 25.4 /s; k cat / K m = 1.3 x 10^6 /s/M

row_label: ReKstD | Progesterone


column_label: Table label: Table 2 Kinetic parameters of the purified MsKstD1 and ReKstD. Row: Testosterone. Enzyme column group: ReKstD. Columns read: K m (μM) cell 22.6, k cat (/s) cell 25.8, k cat / K m (/s/M) cell 1.1 x 10^6. metric: kcat; raw value: 25.8; raw unit: s^-1; normalized value: 25.8 s^(-1); metric: Km; raw value: 22.6; raw unit: uM; normalized value: 0.0226 mM; metric: kcat/Km; raw value: 1.1 × 10^6; raw unit: /s/M; normalized value: 1100 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified recombinant ReKstD (KstD cloned from Rhodococcus erythropolis WY1406, expressed in E. coli). Kinetic constants were determined in a 1 mL reaction mixture containing 1.5 mM PMS, 40 μM DCPIP, purified enzyme and varying steroid substrate concentrations in 50 mM Tris-HCl buffer; reaction rates were read as DCPIP absorbance at 600 nm on a multi-detection microplate reader at 30 C, and Km and Vmax were obtained by fitting the Michaelis-Menten equation. Export row conditions: pH 8; 303.15 K.

normalized_value_unit_evidence: ReKstD columns of Table 2 row Testosterone: kcat 25.8 /s = 25.8 s^(-1); Km 22.6 μM = 0.0226 mM (1 uM = 0.001 mM); kcat/Km primary cell 1.1 × 10^6 /s/M = 1100 s^-1 mM^-1 (1 /s/M = 0.001 s^-1 mM^-1). In the text extraction of the publisher PDF the multiplication sign renders as ×, the micro sign as μ, the plus-minus as ±, and superscript exponents are flattened onto the mantissa, so the printed cell `1.1 × 106` is the paper's 1.1 x 10^6 /s/M = 1100.0 s^-1 mM^-1 (1 /s/M = 0.001 s^-1 mM^-1).

raw_value_unit_evidence: Table 2 Kinetic parameters of the purified MsKstD1 and ReKstD | column group header row of Table 2: Substrate MsKstD1 ReKstD | metric header row: Km (μM) kcat (/s) kcat/Km (/s/M) Km (μM) kcat (/s) kcat/Km (/s/M) (first metric triplet = MsKstD1, second metric triplet = ReKstD) | row: Testosterone 70.7 ± 9.2 77.5 ± 5.6 1.1 × 106 22.6 ± 2.3 25.8 ± 2.1 1.1 × 106 | ReKstD cells read: K m = 22.6 μM; k cat = 25.8 /s; k cat / K m = 1.1 x 10^6 /s/M

row_label: ReKstD | Testosterone


enzyme_display_name: UniProt P72222

organism: Pseudomonas putida

substrate_name: Quinoline

enzyme: UniProt P72222

substrate: Quinoline


enzyme_display_name: acyl-CoA oxidase

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA

enzyme: acyl-CoA oxidase


organism: Mycobacterium tuberculosis


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

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=30°C, pH=7.4


enzyme_display_name: UniProt A9XWD7

enzyme: UniProt A9XWD7


organism: Sulfolobus acidocaldarius

substrate_name: oxidized 2,6-dichlorophenolindophenol

substrate: oxidized 2,6-dichlorophenolindophenol


substrate_name: caldariellaquinone

substrate: caldariellaquinone


substrate_name: ferrocyanide

substrate: ferrocyanide


substrate_name: succinate

substrate: succinate


enzyme_display_name: quinoline 2-oxidoreductase

proof_lines:
25°C, wild-type
wild-type

enzyme: quinoline 2-oxidoreductase


proof_lines: with 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyl-2H-tetrazolium chloride as cosubstrate


organism: Paracoccus denitrificans

substrate_name: naphthoquinol

substrate: naphthoquinol


substrate_name: Quinoxaline

substrate: Quinoxaline


organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)


enzyme_display_name: quinaldate 4-oxidoreductase

organism: Serratia marcescens

enzyme: quinaldate 4-oxidoreductase


substrate_name: Quinaldate

proof_lines: with 2-(4-iodophenyl)-3-nitrophenyl-5-phenyltetrazolium chloride as cosubstrate

substrate: Quinaldate


organism: Pseudomonas sp.


organism: Rubrivivax gelatinosus


proof_lines: recombinant wild-type enzyme, pH 8.0, 28°C


substrate_name: all-trans-neurosporene

substrate: all-trans-neurosporene


organism: Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: glutaryl-CoA dehydrogenase (acceptor)

organism: Desulfococcus multivorans

substrate_name: glutaryl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V366Y/A80E with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; 303.15 K; cofactor CoA

proof_lines: pH 7.8, 30°C, mutants V366Y and A80E/V366Y

enzyme: glutaryl-CoA dehydrogenase (acceptor)

substrate: glutaryl-CoA


enzyme_display_name: Glutaryl-CoA dehydrogenase

enzyme: Glutaryl-CoA dehydrogenase


enzyme_display_name: Urocanate reductase

organism: Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1)

proof_lines: KM for urocanate is inferior to 10 uM and kcat is 360 sec(-1) (at pH 7.0).

enzyme: Urocanate reductase


enzyme_display_name: urocanate reductase

organism: Shewanella oneidensis

substrate_name: Urocanate

proof_lines: recombinant two-domain construct UrdA, pH 7.0, 22°C

proof_lines: Km less than 0.01 mM, at pH 7.0 and 25°C

source_databases_merged: brenda skid

enzyme: urocanate reductase

substrate: Urocanate


proof_lines: recombinant wild-type UrdA, pH 7.0, 22°C


enzyme_display_name: 2-methylacyl-CoA dehydrogenase

organism: Rattus norvegicus

substrate_name: 2-Methylbutanoyl-CoA; FAD

assay_conditions_summary: cofactor FAD

enzyme: 2-methylacyl-CoA dehydrogenase

substrate: 2-Methylbutanoyl-CoA; FAD


organism: Solanum tuberosum

column_label: The required Vmax, kcat, and Km all have exact primary table cells for the 2MBCD preferred substrate; ETF is assay context, not a separate substrate row in Table I.

raw_value_unit_evidence: Table I row 2MBCD / 2-Methylbutyryl-CoA: Km 1.0 uM; Vmax 0.59 umol/min; kcat per tetramer 1.77 s^-1.

row_label: 2MBCD; 2-Methylbutyryl-CoA

table_label: Table I: Kinetic parameters of IVD and 2MBCD with preferred substrates


enzyme_display_name: 1-hydroxycarotenoid 3,4-desaturase

organism: Rhodobacter sphaeroides

substrate_name: Acceptor; 1-Hydroxyneurosporene

column_label: Figure 4 plots HND activity versus hydroxyneurosporene concentration; enzyme kinetic prose states the Km for hydroxyneurosporene was calculated to be 13.4 microM.

raw_value_unit_evidence: Figure 4 and enzyme kinetic prose report Km 13.4 microM for hydroxyneurosporene.

row_label: 1-hydroxyneurosporene as the Km-varied substrate for HND

table_label: Figure 4: Double-reciprocal plot of HND activity versus hydroxyneurosporene concentration; enzyme kinetic prose

enzyme: 1-hydroxycarotenoid 3,4-desaturase

substrate: Acceptor; 1-Hydroxyneurosporene


organism: Rhodobacter capsulatus

substrate_name: Phytoene

substrate: Phytoene


substrate_name: zeta-Carotene

substrate: zeta-Carotene


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A80E/V366Y with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; cofactor CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V366Y with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V88S to reconstruct the assayed variant sequence.


organism: Agrobacterium sp.

proof_lines: with quinoline-4-carboxylate as cosubstrate


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


enzyme_display_name: phytoene desaturase (lycopene-forming)

proof_lines: pH 8, 28°C, mutant enzyme L208F (complementation of CrtI in pPEU (DH5a/pACCrtEBEU/pPEUCrtIRg))

enzyme: phytoene desaturase (lycopene-forming)


proof_lines: pH 8, 28°C, mutant enzyme L208P (complementation of CrtI in pUC8 (DH5a/pACCrtEBEU/pUCCrtIRg))


proof_lines: pH 8, 28°C, mutant enzyme (complementation of CrtI in pUC8 (DH5a/pACCrtEBEU/pUCCrtIRg))


enzyme_display_name: Transferred entry: 1.3.8.5

assay_conditions_summary: pH 8; 305.15 K; cofactor CoA

column_label: Required kcat_over_km is metric-labeled in the primary table as Catalytic efficiency 1.79 uM^-1*s^-1; this disagrees with exported kcat_over_km 1770 s^-1*mM^-1.

normalized_value_unit_evidence: kcat 1.77 s^-1 and Km 0.001 mM match; paper catalytic efficiency normalizes to 1790 s^-1*mM^-1, not target 1770 s^-1*mM^-1.

raw_value_unit_evidence: Table I row 2MBCD / 2-Methylbutyryl-CoA: Km 1.0 uM; kcat per tetramer 1.77 s^-1; Catalytic efficiency 1.79 uM^-1*s^-1.

enzyme: Transferred entry: 1.3.8.5


substrate_name: FAD

substrate: FAD


enzyme_display_name: 3-hydroxybenzoyl-CoA reductase

organism: Thauera aromatica

substrate_name: ATP; H2O; 3-Hydroxybenzoyl-CoA; Reduced acceptor

assay_conditions_summary: cofactor ATP

enzyme: 3-hydroxybenzoyl-CoA reductase


enzyme_display_name: UniProt A3SI50

organism: Roseovarius nubinhibens

assay_conditions_summary: pH 9; 313.15 K; cofactor FAD

column_label: Table 5. Km values of wild type DmdC and its mutants to different substrates; row Wild type DmdC / To MMPA-CoA; column Km to MMPA-CoA (mM); raw cell 1.4 +/- 0.2 mM; normalized Km 1.4 mM

normalized_value_unit_evidence: Km=1.4 mM

raw_value_unit_evidence: Wild type DmdC / To MMPA-CoA: Km to MMPA-CoA (mM)=1.4 +/- 0.2 mM

row_label: Wild type DmdC / To MMPA-CoA

enzyme: UniProt A3SI50


column_label: Table 5. Km values of wild type DmdC and its mutants to different substrates; row Wild type DmdC / To FAD; column Km to FAD (uM); raw cell 6.3 +/- 0.5 uM; normalized Km 0.0063 mM

raw_value_unit_evidence: Wild type DmdC / To FAD: Km to FAD (uM)=6.3 +/- 0.5 uM

row_label: Wild type DmdC / To FAD


enzyme_display_name: Hydroxyneurosporene desaturase

organism: Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.)

substrate_name: hydroxyneurosporene (at pH 30 degrees Celsius and pH 8)

column_label: Figure 4 and the enzyme kinetic prose report Km = 13.4 uM for hydroxyneurosporene/1-hydroxyneurosporene.

raw_value_unit_evidence: Figure 4 labels Km=13.4 uM; enzyme kinetic prose states the Km was calculated to be 13.4 uM.

enzyme: Hydroxyneurosporene desaturase


proof_lines:
pH 7.8, 30°C
Raw SKiD Env: Temp=30°C, pH=7.8

source_databases_merged: brenda skid uniprot


enzyme_display_name: Benzoyl-CoA reductase subunit C

substrate_name: benzoyl-CoA

enzyme: Benzoyl-CoA reductase subunit C

substrate: benzoyl-CoA


substrate_name: ATP

substrate: ATP


enzyme_display_name: Benzoyl-CoA reductase subunit D

enzyme: Benzoyl-CoA reductase subunit D


enzyme_display_name: Benzoyl-CoA reductase subunit B

enzyme: Benzoyl-CoA reductase subunit B


enzyme_display_name: Benzoyl-CoA reductase subunit A

enzyme: Benzoyl-CoA reductase subunit A


assay_conditions_summary: pH 7; 295.15 K; cofactor FAD


enzyme_display_name: succinate dehydrogenase

organism: Sulfolobus sp.

enzyme: succinate dehydrogenase


substrate_name: caldariellaquinone

substrate: caldariellaquinone


substrate_name: oxidized 2,6-dichlorophenolindophenol

substrate: oxidized 2,6-dichlorophenolindophenol


substrate_name: succinate

substrate: succinate


organism: Ruegeria pomeroyi

substrate_name: valeryl-CoA

proof_lines: pH and temperature not specified in the publication

substrate: valeryl-CoA


substrate_name: caprylyl-CoA

substrate: caprylyl-CoA


substrate_name: caproyl-CoA

substrate: caproyl-CoA


substrate_name: heptanoyl-CoA

substrate: heptanoyl-CoA


substrate_name: butyryl-CoA

substrate: butyryl-CoA


substrate_name: isobutyryl-CoA

substrate: isobutyryl-CoA


enzyme_display_name: medium-chain acyl-CoA dehydrogenase

organism: Sus scrofa

substrate_name: meldola's blue

proof_lines: medium chain acyl-CoA dehydrogenase from kidney, terminal acceptor iodonitrotetrazolium

enzyme: medium-chain acyl-CoA dehydrogenase

substrate: meldola's blue


substrate_name: phenazine ethosulfate

proof_lines: medium chain acyl-CoA dehydrogenase from kidney, terminal acceptor 2,6-dichlorphenol-indophenol

substrate: phenazine ethosulfate


substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


substrate_name: ferricenium hexafluorophosphate

proof_lines: medium chain acyl-CoA dehydrogenase from kidney

substrate: ferricenium hexafluorophosphate


substrate_name: indolepropionyl-CoA

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: between pH 8.0 and pH 10.0 at a ionic strength between 11 mM and 50 mM, lower values at acidic pH and with higher ionic strength

substrate: indolepropionyl-CoA


substrate_name: butanoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: butanoyl-CoA


substrate_name: decanoyl-CoA

substrate: decanoyl-CoA


substrate_name: hexanoyl-CoA

substrate: hexanoyl-CoA


enzyme_display_name: 3-oxosteroid 1-dehydrogenase

organism: Mycolicibacterium smegmatis

enzyme: 3-oxosteroid 1-dehydrogenase


substrate_name: cortisone

substrate: cortisone


substrate_name: testosterone

substrate: testosterone


substrate_name: cortexolone

substrate: cortexolone


substrate_name: progesterone

substrate: progesterone


enzyme_display_name: dihydroorotate dehydrogenase (quinone)

organism: Toxoplasma gondii

substrate_name: (S)-dihydroorotate

proof_lines:
mutant N302S, pH 8.0, 22°C
mutant enzyme N302S, at pH 8.0 and 25°C

enzyme: dihydroorotate dehydrogenase (quinone)

substrate: (S)-dihydroorotate


substrate_name: decylubiquinone

proof_lines:
mutant enzyme N302S, at pH 8.0 and 25°C
mutant N302S, pH 8.0, 22°C

substrate: decylubiquinone


proof_lines:
wild-type, pH 8.0, 22°C
wild type enzyme, at pH 8.0 and 25°C


proof_lines:
wild type enzyme, at pH 8.0 and 25°C
wild-type, pH 8.0, 22°C


substrate_name: ATP

substrate: ATP


enzyme_display_name: coproporphyrinogen III oxidase (coproporphyrin-forming)

organism: Bacillus subtilis

substrate_name: protoporphyrinogen IX

proof_lines:
at pH 8.7 and 37°C
at pH 7.2 and 30°C

substrate: protoporphyrinogen IX


substrate_name: mesoporphyrinogen IX

enzyme: coproporphyrinogen III oxidase (coproporphyrin-forming)

substrate: mesoporphyrinogen IX


substrate_name: Coproporphyrinogen III

substrate: Coproporphyrinogen III


organism: Ascaris suum


substrate_name: fumarate

proof_lines:
complex II from adult nematode
complex II from larvae

substrate: fumarate


substrate_name: succinate

proof_lines:
complex II from larvae
complex II from adult nematode

substrate: succinate


organism: Rhodococcus erythropolis


proof_lines: apparent value, in 50 mM Tris (pH 7.4), at 30°C


organism: Bos taurus

substrate_name: electron transferring flavoprotein

substrate: electron transferring flavoprotein


substrate_name: hexadecanoyl-CoA

substrate: hexadecanoyl-CoA


enzyme_display_name: long-chain acyl-CoA dehydrogenase

substrate_name: palmitoyl-CoA

proof_lines: in the presence of fatty acid free bovine serum albumin

enzyme: long-chain acyl-CoA dehydrogenase

substrate: palmitoyl-CoA


organism: Escherichia coli


substrate_name: S-dihydroorotate

substrate: S-dihydroorotate


substrate_name: L-malate

substrate: L-malate


substrate_name: D-malate

substrate: D-malate


assay_conditions_summary: pH 7.4; 298.15 K; cofactor FAD

proof_lines: based on FAD content, dependency on assay temperature

proof_lines: succinate oxidation, determined at 0.01 mM ubiquinone-2


enzyme_display_name: coproporphyrinogen dehydrogenase

organism: Vibrio vulnificus

enzyme: coproporphyrinogen dehydrogenase


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


substrate_name: oxidized phenazine ethosulfate

proof_lines: fumarate reductase, succinate oxidation reaction

substrate: oxidized phenazine ethosulfate


substrate_name: Unknown

substrate: Unknown


organism: Homo sapiens

proof_lines: acyl-CoA dehydrogenase activity skin fibroblasts, lab data of a 6-year old male patient with VLCAD deficiency during rhabdomyolysis


substrate_name: decanoyl-CoA

substrate: decanoyl-CoA


substrate_name: octanoyl-CoA

substrate: octanoyl-CoA


organism: Mycobacterium tuberculosis


substrate_name: progesterone

substrate: progesterone


organism: Plasmodium falciparum

substrate_name: L-Dihydroorotate; Ubiquinone

substrate: L-Dihydroorotate; Ubiquinone


substrate_name: L-dihydroorotate

substrate: L-dihydroorotate


proof_lines:
pH 8.0, 22°C, wild-type
wild-type enzyme


organism: Rubrivivax gelatinosus


organism: Rattus norvegicus


substrate_name: isobutyryl-CoA

substrate: isobutyryl-CoA


proof_lines:
isobutyryl-CoA as substrate
(S)-2-methylbutyryl-CoA as substrate


enzyme_display_name: short-chain acyl-CoA dehydrogenase

substrate_name: pentanoyl-CoA

enzyme: short-chain acyl-CoA dehydrogenase

substrate: pentanoyl-CoA


proof_lines:
C-2 proton/deuteron exchange
with phenazine methosulfate


proof_lines: enzyme-catalyzed C-2 proton-deuteron exchange reaction


organism: Mus musculus

column_label: Table I row 2,4-Decadienoyl-CoA; column Km (uM) = 6.

raw_value_unit_evidence: 6 uM

table_label: Table I, Kinetic parameters of recombinant mouse Delta2,Delta4-dienoyl-CoA reductase


column_label: Table I row 2,4-Hexadienoyl-CoA; column Km (uM) = 108. Methods identify the prepared substrate as Delta2-trans,Delta4-trans-hexadienoyl-CoA.


column_label: Table I row 2,4,7,10,13,16,19-Docosaheptanenoyl-CoA; column Km (uM) = 155; footnote 1-b adds 0.06% Triton X-100.


enzyme_display_name: fumarate reductase (cytochrome)

organism: Shewanella putrefaciens

substrate_name: succinate

proof_lines: with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.4, temperature not specified in the publication

enzyme: fumarate reductase (cytochrome)

substrate: succinate


substrate_name: fumarate

proof_lines: with reduced methyl viologen as cosubstrate, at pH 7.4, temperature not specified in the publication

substrate: fumarate


proof_lines: at pH 7.4, temperature not specified in the publication


enzyme_display_name: acyl-CoA oxidase

organism: Yarrowia lipolytica

substrate_name: hexadecanedioyl-CoA

assay_conditions_summary: 303.15 K; cofactor CoA

enzyme: acyl-CoA oxidase

substrate: hexadecanedioyl-CoA


substrate_name: tetradecanoyl-CoA

substrate: tetradecanoyl-CoA


substrate_name: dodecanoyl-CoA

substrate: dodecanoyl-CoA


substrate_name: coenzyme Q7

substrate: coenzyme Q7


substrate_name: methyl-S-dihydroorotate

substrate: methyl-S-dihydroorotate


enzyme_display_name: isovaleryl-CoA dehydrogenase

organism: Arabidopsis thaliana

substrate_name: isovaleryl-CoA

enzyme: isovaleryl-CoA dehydrogenase

substrate: isovaleryl-CoA


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


proof_lines:
fumarate reduction, pH 7.8, 30°C
30°C, pH 7.8


organism: Geobacter metallireducens

assay_conditions_summary: pH 6.8; 303.15 K; cofactor CoA


substrate_name: ubiquinone

substrate: ubiquinone


enzyme_display_name: glutaryl-CoA dehydrogenase (ETF)

enzyme: glutaryl-CoA dehydrogenase (ETF)


substrate_name: ferrocenium hexafluorophosphate

substrate: ferrocenium hexafluorophosphate


substrate_name: palmitoleoyl-CoA

substrate: palmitoleoyl-CoA


substrate_name: linoleoyl-CoA

substrate: linoleoyl-CoA


substrate_name: octanoyl-CoA

assay_conditions_summary: pH 7.6; 298.15 K; cofactor CoA

substrate: octanoyl-CoA


enzyme_display_name: protoporphyrinogen IX dehydrogenase (quinone)

substrate_name: menadione

substrate: menadione


substrate_name: protoporphyrinogen IX

enzyme: protoporphyrinogen IX dehydrogenase (quinone)

substrate: protoporphyrinogen IX


substrate_name: glutaryl-CoA

assay_conditions_summary: 298.15 K; cofactor CoA

substrate: glutaryl-CoA


substrate_name: glutaconyl-CoA

assay_conditions_summary: pH 7.6; 298.15 K; buffer 50 mM potassium phosphate; cofactor CoA

proof_lines: mutant enzyme E370D, at 25°C in 50 mM potassium phosphate buffer, pH 7.6

substrate: glutaconyl-CoA


proof_lines: recombinant mutant R227P with ETF, pH 7.8, temperature not specified in the publication


assay_conditions_summary: pH 7.8; 298.15 K; cofactor CoA

proof_lines: recombinant wild-type enzyme with ETF, pH 7.8, temperature not specified in the publication

proof_lines: recombinant wild-type enzyme, pH 7.6, 25°C, electron acceptor is electron transfer flavoprotein


organism: Acidianus ambivalens

substrate_name: fumarate

proof_lines: pH 6.5, 70°C, detergent treated membranes from aerobic growth

proof_lines: pH 6.5, 70°C, determined for activity in membranes from aerobic growth

proof_lines: pH 6.5, 70°C, detergent treated membranes from anaerobic growth

substrate: fumarate


substrate_name: succinate

substrate: succinate


enzyme_display_name: dihydroorotate dehydrogenase (fumarate)

organism: Lactobacillus delbrueckii subsp. bulgaricus

substrate_name: S-dihydroorotate

proof_lines:
with oxygen
with ferricyanide as electron acceptor

enzyme: dihydroorotate dehydrogenase (fumarate)

substrate: S-dihydroorotate


organism: Mycolicibacterium neoaurum


substrate_name: progesterone

substrate: progesterone


assay_conditions_summary: pH 8; 303.15 K; cofactor CoA


substrate_name: electron transfer protein

proof_lines:
pH 8.0, 30°C, calculated per monomer
pH 8.0, 30°C

substrate: electron transfer protein


enzyme_display_name: (S)-8-oxocitronellyl enol synthase

organism: Nepeta racemosa

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

enzyme: (S)-8-oxocitronellyl enol synthase


substrate_name: NADPH

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

substrate: NADPH


organism: Oryctolagus sp.

proof_lines: succinate with papyriferic acid 0.04 mM, pH 7.4, 25°C


substrate_name: Unknown

substrate: Unknown


substrate_name: hexanoyl-CoA

substrate: hexanoyl-CoA


substrate_name: dodecanoyl-CoA

substrate: dodecanoyl-CoA


substrate_name: decanoyl-CoA

substrate: decanoyl-CoA


substrate_name: dihydroorotate

substrate: dihydroorotate


substrate_name: coenzyme Q6

substrate: coenzyme Q6


organism: Pseudomonas fluorescens


substrate_name: Glutarylpantetheine

substrate: Glutarylpantetheine


organism: Pseudomonas sp.


assay_conditions_summary: pH 7.4; 298.15 K; cofactor CoA


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH


assay_conditions_summary: pH 7

proof_lines: and 0.50, preparation from liver, pH 7, temperature not specified in the publication

proof_lines: and 0.0024, preparation from liver, pH 7, temperature not specified in the publication

proof_lines: and 0.0014, preparation from liver, pH 7, temperature not specified in the publication


enzyme_display_name: succinate dehydrogenase (ubiquinone)

substrate_name: Succinate; Acceptor

enzyme: succinate dehydrogenase (ubiquinone)

substrate: Succinate; Acceptor


substrate_name: octanoyl-CoA

substrate: octanoyl-CoA


assay_conditions_summary: pH 7.6; buffer 50 mM potassium phosphate; cofactor CoA

proof_lines: wild type enzyme, in 50 mM potassium phosphate buffer, pH 7.6


assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA


proof_lines:
pH 7.4, 30°C, wild-type enzyme
wild type enzyme, at pH 7.4 and 30°C


substrate_name: Palmitoyl-CoA; O2

proof_lines:
low concentration
high concentration

substrate: Palmitoyl-CoA; O2


substrate_name: palmitoyl-CoA

proof_lines:
kidney enzyme
liver enzyme

substrate: palmitoyl-CoA


enzyme_display_name: chlorophyllide a reductase

organism: Rhodobacter capsulatus

substrate_name: 8-vinyl chlorophyllide a

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

proof_lines: pH 8.0, 22°C, recombinant BchYZ heterodimer

enzyme: chlorophyllide a reductase

substrate: 8-vinyl chlorophyllide a


organism: Rhodococcus erythropolis

proof_lines: apparent value, in 50 mM Tris (pH 7.4), at 30°C


organism: Saccharomyces cerevisiae

substrate_name: L-dihydroorotate

proof_lines: in 50mM Tris/HCl, 150 mM KCl, 0.1% (v/v) Triton X-100, pH 8, at 30°C

substrate: L-dihydroorotate


substrate_name: S-dihydroorotate

proof_lines:
with O2
with fumarate, pH 7.5
with ferricyanide

substrate: S-dihydroorotate


substrate_name: dihydrooxonate

substrate: dihydrooxonate


enzyme_display_name: protoporphyrinogen oxidase

smiles: O=O

enzyme: protoporphyrinogen oxidase


enzyme_display_name: medium-chain acyl-CoA dehydrogenase

organism: Homo sapiens

substrate_name: recombinant electron transferring flavoprotein

enzyme: medium-chain acyl-CoA dehydrogenase


substrate: recombinant electron transferring flavoprotein


organism: Staphylococcus aureus

substrate_name: protoporphyrinogen IX

substrate: protoporphyrinogen IX


substrate_name: Coproporphyrinogen III

substrate: Coproporphyrinogen III


organism: Sus scrofa

proof_lines: 25°C, with ferricenium as acceptor, pig enzyme reconstituted with 2'-deoxy-FAD

proof_lines: phenazine methosulfate as electron carrier

proof_lines: phenazine methosulfate and 2,6-dichlorophenolindophenol as electron acceptors


proof_lines: 25°C, with ferricenium as acceptor, recombinant wild-type enzyme


substrate_name: butyryl-CoA

proof_lines:
electron transfer protein as acceptor
phenazine methyl sulfate as acceptor

substrate: butyryl-CoA


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: succinate dehydrogenase

substrate_name: 2,6-dichlorophenol indophenol

enzyme: succinate dehydrogenase

substrate: 2,6-dichlorophenol indophenol


proof_lines: 22°C, Sdh3p/Sdh4p double mutant strain H106A/C78A


organism: Trypanosoma cruzi

substrate_name: (S)-dihydroorotate

proof_lines: assay based on isothermal titration calorimetry, pH 8.0, 25°C

substrate: (S)-dihydroorotate


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


organism: Yarrowia lipolytica

substrate_name: decanoyl-CoA

substrate: decanoyl-CoA


substrate_name: hexanoyl-CoA

substrate: hexanoyl-CoA


organism: Arabidopsis thaliana

proof_lines: pH and temperature not specified in the publication


organism: Acinetobacter sp.

substrate_name: lauroyl-CoA

assay_conditions_summary: pH 8.5; cofactor CoA

substrate: lauroyl-CoA


organism: Amaranthus tuberculatus

proof_lines: about, pH 7.4, temperature not specified in the publication


organism: Bacillus subtilis

proof_lines: inhibitor of the activity of mutant and wild-type enzyme


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


organism: Bos taurus


enzyme_display_name: coproporphyrinogen oxidase

substrate_name: Coproporphyrinogen-III

proof_lines:
presence of phospholipids
crude extract
purified enzyme

enzyme: coproporphyrinogen oxidase

substrate: Coproporphyrinogen-III


substrate_name: glutaryl-CoA

substrate: glutaryl-CoA


substrate_name: Harderoporphyrinogen

substrate: Harderoporphyrinogen


substrate_name: fumarate

proof_lines: fumarate reduction, Km of fumarate does not depend on concentration of quinol

substrate: fumarate


substrate_name: Acceptor; Succinate

proof_lines:
25°C, pH 7.5
succinate oxidation
fumarate reduction

substrate: Acceptor; Succinate


substrate_name: electron-transfer flavoprotein

substrate: electron-transfer flavoprotein


enzyme_display_name: dihydroorotate dehydrogenase (quinone)

organism: Escherichia coli

substrate_name: S-dihydroorotate

proof_lines: ubiquinone0 and 2,6-dichlorophenolindophenol mix

proof_lines: 2,6-dichlorophenolindophenol sole electron acceptor

enzyme: dihydroorotate dehydrogenase (quinone)

substrate: S-dihydroorotate


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


substrate_name: menaquinone

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

substrate: menaquinone


proof_lines:
isolated complex
membrane preparation
value below


substrate_name: dihydroorotate

substrate: dihydroorotate


proof_lines: mutant Y318L, 22°C, pH 7.0, presence of 0.1% TritonX-100


organism: Glycine max


organism: Halobacterium salinarum

substrate_name: succinate

proof_lines:
membrane bound enzyme
soluble enzyme

substrate: succinate


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


substrate_name: butyryl-CoA

substrate: butyryl-CoA


substrate_name: Mesoporphyrinogen-IX

substrate: Mesoporphyrinogen-IX


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: palmitoyl-CoA

proof_lines: recombinant enzyme from Spodoptera frugiperda cells

substrate: palmitoyl-CoA


organism: Chromatium sp.


substrate_name: protoporphyrinogen-IX

substrate: protoporphyrinogen-IX


substrate_name: glutaconyl-CoA

substrate: glutaconyl-CoA


proof_lines:
below 0.2/min, R59W mutant enzyme
recombinant mutant R59W, pH 8.2


enzyme_display_name: hydrogen peroxide-dependent heme synthase

organism: Listeria monocytogenes


organism: Mus musculus

substrate_name: progesterone

substrate: progesterone


organism: Mycobacterium tuberculosis

substrate_name: Unknown

proof_lines: pH 6.8, temperature not specified in the publication

substrate: Unknown


enzyme_display_name: 3-oxosteroid 1-dehydrogenase

organism: Mycolicibacterium neoaurum

proof_lines:
pH 7.0, 30°C
recombinant enzyme, pH 8.0, 40°C

enzyme: 3-oxosteroid 1-dehydrogenase


organism: Mycolicibacterium smegmatis


enzyme_display_name: anaerobic carbon monoxide dehydrogenase

organism: Neomoorella thermoacetica

substrate_name: Ferredoxin

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

proof_lines: inhibition of CO/acetyl-CoA exchange reaction

proof_lines: assay at pH 5.5, Ki depends on pH and temperature

enzyme: anaerobic carbon monoxide dehydrogenase

substrate: Ferredoxin


proof_lines:
pH 7. 26°C
at pH 7.0 and 26°C
pH 7, 26°C


organism: Nicotiana tabacum

proof_lines: pH and temperature not specified in the publication

proof_lines: at pH 7.4, temperature not specified in the publication


enzyme_display_name: short-chain acyl-CoA dehydrogenase

organism: Oryctolagus cuniculus

assay_conditions_summary: cofactor CoA

proof_lines: partially purified enzyme, enzyme mixture

enzyme: short-chain acyl-CoA dehydrogenase


enzyme_display_name: aldehyde oxidase

substrate_name: benzaldehyde

proof_lines: pH 7.8, determined according to Eadie-Hofstee

proof_lines: pH 7.8, determined according to Lineweaver-Burk

enzyme: aldehyde oxidase

substrate: benzaldehyde


proof_lines: 2,6-dichlorophenol-indophenol as electron acceptor in D2O

proof_lines: 2,6-dichlorophenol-indophenol as electron acceptor in H2O


assay_conditions_summary: pH 9

proof_lines:
pH 9, p-aminobenzamidine oxidation
pH 9, benzaldehyde oxidation
pH 7, p-aminobenzamidine oxidation


substrate_name: tropylium tetrafluoroborate

substrate: tropylium tetrafluoroborate


proof_lines:
ferricyanide as electron acceptor
competitive inhibitor
noncompetitive inhibitor


organism: Paracoccus denitrificans

proof_lines: for both membrane fragments and mitochondrial enzyme


organism: Plasmodium falciparum

substrate_name: Coproporphyrinogen III

proof_lines:
pH 7.5, 37°C, recombinant enzyme
pH 7.5, 37°C, native enzyme

substrate: Coproporphyrinogen III


proof_lines: 2,6-dichlorophenol indophenol as electron acceptor


enzyme_display_name: isovaleryl-CoA dehydrogenase

organism: Pseudomonas aeruginosa

substrate_name: isovaleryl-CoA

substrate: isovaleryl-CoA


enzyme_display_name: prephenate dehydrogenase

substrate_name: Prephenate; NAD+

assay_conditions_summary: cofactor NAD+

enzyme: prephenate dehydrogenase

substrate: Prephenate; NAD+


substrate_name: prephenate

substrate: prephenate


substrate_name: methyl viologen

substrate: methyl viologen


enzyme_display_name: acyl-CoA oxidase

organism: Phascolarctos cinereus

enzyme: acyl-CoA oxidase


organism: Rattus norvegicus

substrate_name: octanoyl-CoA

substrate: octanoyl-CoA


substrate_name: hexanoyl-CoA

assay_conditions_summary: pH 7.4; 303.15 K; buffer 50 mM phosphate; cofactor CoA

proof_lines: in 50 mM phosphate buffer, pH 7.4, at 30°C

substrate: hexanoyl-CoA


organism: Pseudomonas sp.

substrate_name: NAD+

substrate: NAD+


substrate_name: succinate

proof_lines: succinate with papyriferic acid 0.08 mM, pH 7.4, 25°C

substrate: succinate


substrate_name: S-dihydroorotate

proof_lines:
recombinant enzyme
expressed in SF21 insect cells
expressed in Escherichia coli

substrate: S-dihydroorotate


enzyme_display_name: 7-dehydrocholesterol reductase

substrate_name: NADPH

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

enzyme: 7-dehydrocholesterol reductase

substrate: NADPH


substrate_name: dihydrotestosterone

proof_lines: 37°C, pH not specified in the publication

substrate: dihydrotestosterone


enzyme_display_name: long-chain acyl-CoA dehydrogenase

substrate_name: omega-phenyldecanoyl-CoA

enzyme: long-chain acyl-CoA dehydrogenase

substrate: omega-phenyldecanoyl-CoA


substrate_name: Vanillin

proof_lines: pH 7.4, 37°C, enzyme isolated from animals fed with a selenium-deficient diet

substrate: Vanillin


substrate_name: dihydroorotate

substrate: dihydroorotate


substrate_name: 15-ketoprostaglandin F2alpha

substrate: 15-ketoprostaglandin F2alpha


substrate_name: electron transferring flavoprotein

substrate: electron transferring flavoprotein


substrate_name: decylubiquinone

proof_lines:
expressed in SF21 insect cells
expressed in Escherichia coli

substrate: decylubiquinone


substrate_name: butyryl-CoA

substrate: butyryl-CoA


organism: Rattus sp.

substrate_name: all-trans retinal

substrate: all-trans retinal


organism: Rhodococcus opacus

substrate_name: FAD

assay_conditions_summary: cofactor FAD

substrate: FAD


substrate_name: N-methylnicotinamide

proof_lines: female rat liver enzyme after reduction with DTT

substrate: N-methylnicotinamide


organism: Saccharomyces cerevisiae


enzyme_display_name: DELTA14-sterol reductase

enzyme: DELTA14-sterol reductase


enzyme_display_name: DELTA24(241)-sterol reductase

enzyme: DELTA24(241)-sterol reductase


enzyme_display_name: protoporphyrinogen oxidase

substrate_name: protoporphyrinogen-IX

substrate: protoporphyrinogen-IX


enzyme_display_name: enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)

organism: Staphylococcus aureus

substrate_name: Crotonyl-N-acetyl-cysteamine

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

substrate: Crotonyl-N-acetyl-cysteamine


organism: Rhodococcus rhodochrous


enzyme_display_name: precorrin-2 dehydrogenase

substrate_name: NAD+

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

enzyme: precorrin-2 dehydrogenase

substrate: NAD+


substrate_name: crotonyl-[acyl-carrier protein]

assay_conditions_summary: pH 7.8; 298.15 K; buffer 100 mM Na2HPO4

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

proof_lines: wild type enzyme, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)

enzyme: enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)

substrate: crotonyl-[acyl-carrier protein]


enzyme_display_name: succinate dehydrogenase

organism: Sus scrofa

substrate_name: Unknown

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

substrate: Unknown


enzyme_display_name: medium-chain acyl-CoA dehydrogenase

substrate_name: crotonyl-CoA

proof_lines: hydratase activity, value depending on pH

proof_lines: hydratase reaction, value depending on pH

proof_lines: uncompetitive vs. electron transferring flavoprotein

substrate: crotonyl-CoA


enzyme_display_name: coproporphyrinogen oxidase

substrate_name: Coproporphyrinogen-III

proof_lines: same value for aerobic and anaerobic oxidation

substrate: Coproporphyrinogen-III


enzyme_display_name: dihydropyrimidine dehydrogenase (NADP+)

substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

enzyme: dihydropyrimidine dehydrogenase (NADP+)

substrate: NADP+


substrate_name: octanoyl-pantetheine

enzyme: medium-chain acyl-CoA dehydrogenase

substrate: octanoyl-pantetheine


enzyme_display_name: dihydroorotate dehydrogenase (fumarate)

organism: Trypanosoma cruzi

substrate_name: orotate

proof_lines: inhibition of DHOD2 at 25°C, in the presence of 1 mM fumarate

enzyme: dihydroorotate dehydrogenase (fumarate)

substrate: orotate


substrate_name: fumarate

proof_lines:
37°C, pH 7.0
DHOD1 at 37°C
DHOD2 at 37°C

substrate: fumarate


enzyme_display_name: oxalate oxidase

organism: Triticum aestivum

substrate_name: oxalate

enzyme: oxalate oxidase

substrate: oxalate


enzyme_display_name: fumarate reductase (NADH)

assay_conditions_summary: cofactor NADH

proof_lines: pH and temperature not specified in the publication

enzyme: fumarate reductase (NADH)


organism: Xanthomonas campestris

substrate_name: prephenate

substrate: prephenate


enzyme_display_name: trans-2-enoyl-CoA reductase (NAD+)

organism: Treponema denticola

substrate_name: crotonoyl-CoA

assay_conditions_summary: pH 6.2; 303.15 K; buffer pH 6; cofactor NADH

proof_lines: in potassium phosphate buffer pH 6.2, at 30°C

enzyme: trans-2-enoyl-CoA reductase (NAD+)

substrate: crotonoyl-CoA


organism: Xenopus laevis

substrate_name: testosterone

substrate: testosterone


assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH

proof_lines: pH 6.5, 30°C, versus trans-2-octenoyl N-acetylcysteamine


organism: Zea mays

substrate_name: dodecanoyl-CoA

substrate: dodecanoyl-CoA


enzyme_display_name: 2-alkenal reductase [NAD(P)+]

organism: Arabidopsis thaliana

substrate_name: crotonaldehyde

smiles: CC=CC=O

enzyme: 2-alkenal reductase [NAD(P)+]

substrate: crotonaldehyde


smiles: CCC(=O)C=CC


smiles: CCC(=O)C=C


substrate_name: NADPH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: NADH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

substrate: NADH


enzyme_display_name: protochlorophyllide reductase

substrate_name: protochlorophyllide

enzyme: protochlorophyllide reductase

substrate: protochlorophyllide


assay_conditions_summary: cofactor NADPH


organism: Bacillus subtilis

column_label: Primary-paper page 3 states the apparent Km value of bsFabI for NADH was 7 uM.

raw_value_unit_evidence: bsFabI apparent Km for NADH 7 uM

row_label: bsFabI NADH Km sentence

table_label: Characterization of the Reductases prose and Figure 2 cofactor utilization


assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: Page 3 Characterization prose, YgaA/FabL NADPH segment, Km 16 uM; Figure 2 gives the fixed 100 uM 8:1-NAC condition.

normalized_value_unit_evidence: NADPH Km=0.016 mM.

raw_value_unit_evidence: Page 3 states YgaA has a Km of 16 uM for NADPH.

row_label: YgaA/FabL, NADPH

table_label: Characterization of the Reductases, page 3; Figure 2 assay context


organism: Escherichia coli


organism: Homo sapiens

assay_conditions_summary: pH 6; 296.15 K; cofactor CoA

proof_lines:
pH 6.0, 23°C
presence of 0.1% albumin, pH 7.4, 30°C


assay_conditions_summary: pH 6; 296.15 K; cofactor NADPH


enzyme_display_name: dihydroorotate dehydrogenase (NAD+)

substrate_name: S-dihydroorotate

enzyme: dihydroorotate dehydrogenase (NAD+)

substrate: S-dihydroorotate


organism: Bos taurus


organism: Canis sp.

substrate_name: D-xylose

substrate: D-xylose


organism: Geobacillus stearothermophilus

substrate_name: pyruvate

substrate: pyruvate


assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA

proof_lines:
presence of 0.1% albumin, pH 7.4, 30°C
pH 6.0, 23°C


assay_conditions_summary: pH 7.4; cofactor CoA

column_label: Results prose gives the docosaheptaenoyl-CoA Km under absence-of-albumin conditions; Fig. 2C is the matching substrate panel.

raw_value_unit_evidence: Results prose reports docosaheptaenoyl-CoA Km = 102 uM.

row_label: 2,4,7,10,13,16,19-docosaheptaenoyl-CoA; Fig. 2C; Km prose

table_label: PMID 11514237 results prose plus Fig. 2 kinetic analysis


substrate_name: thymine

substrate: thymine


organism: Nicotiana tabacum


organism: Corynebacterium glutamicum

assay_conditions_summary: pH 7.7; cofactor NAD+

column_label: Primary paper Table 2 reports WT ODH Km (mM) = 0.13; table footnote says kinetic parameters were derived as described under Materials and Methods.

raw_value_unit_evidence: Km raw_value=0.13 raw_unit=mM

row_label: WT row

table_label: Table 2: Summary of effects of AceF mutant proteins on ODH and PDH activities


organism: Haemophilus influenzae

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: prephenate dehydrogenase

enzyme: prephenate dehydrogenase


substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


enzyme_display_name: aldehyde oxidase

organism: Macaca fascicularis

substrate_name: zebularine

enzyme: aldehyde oxidase

substrate: zebularine


proof_lines:
iosenzyme 2
iosenzyme 1


enzyme_display_name: formylmethanofuran dehydrogenase

organism: Methanothermobacter thermautotrophicus

substrate_name: N-formylmethanofuran

enzyme: formylmethanofuran dehydrogenase

substrate: N-formylmethanofuran


enzyme_display_name: anaerobic carbon monoxide dehydrogenase

organism: Methanosarcina barkeri

substrate_name: CO

smiles: [Co]

enzyme: anaerobic carbon monoxide dehydrogenase

substrate: CO


organism: Physcomitrium patens


organism: Methanothermobacter wolfeii

substrate_name: N-Furfurylformamide

proof_lines:
molybdenum enzyme
tungsten-substituted molybdenum enzyme
non-substituted molybdenum enzyme

substrate: N-Furfurylformamide


organism: Mus musculus

proof_lines:
female, pH 7.5, 37°C
male, pH 7.5, 37°C


organism: Pseudomonas aeruginosa

substrate_name: crotonyl-[acyl-carrier protein]

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication

substrate: crotonyl-[acyl-carrier protein]


organism: Rattus norvegicus

proof_lines: pH 7.4, 37°C, enzyme from Wistar-Imamichi strain, ratio Vmax/Km 1.98 microl per min and mg

proof_lines: pH 7.4, 37°C, enzyme from Jcl:Wistar strain, ratio Vmax/Km 1.00 microl per min and mg

proof_lines: pH 7.4, 37°C, enzyme from Crj:Wistar strain, ratio Vmax/Km 1.46 microl per min and mg


assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADPH

proof_lines:
iosenzyme 2
iosenzyme 1
versus progesterone


proof_lines:
pH 7.6, 30°C, presence of 0.3 M KCl
recombinant enzyme


proof_lines:
male, pH 7.5, 37°C
female, pH 7.5, 37°C


organism: Plasmodium falciparum

substrate_name: NAD+; Phosphate; D-Glyceraldehyde 3-phosphate

assay_conditions_summary: cofactor NAD+


substrate_name: NAD+; D-Glyceraldehyde 3-phosphate; Phosphate


organism: Saccharomyces cerevisiae

substrate: NAD+; Phosphate; D-Glyceraldehyde 3-phosphate


organism: Zea mays


enzyme_display_name: pyruvate oxidase

organism: Lactobacillus plantarum

substrate_name: Pyruvate; Phosphate; O2

enzyme: pyruvate oxidase

substrate: Pyruvate; Phosphate; O2


enzyme_display_name: trans-2-enoyl-CoA reductase (NADPH)

substrate_name: H+; Crotonoyl-CoA; NADPH

assay_conditions_summary: cofactor CoA

enzyme: trans-2-enoyl-CoA reductase (NADPH)

substrate: H+; Crotonoyl-CoA; NADPH


organism: Enterococcus faecalis

substrate_name: O2; L-Dihydroorotate

substrate: O2; L-Dihydroorotate


organism: Escherichia coli

substrate_name: Acceptor; L-Dihydroorotate

substrate: Acceptor; L-Dihydroorotate


organism: Mycobacterium bovis

substrate_name: H2O; Succinate semialdehyde; NADP+

assay_conditions_summary: cofactor NADP+

substrate: H2O; Succinate semialdehyde; NADP+


enzyme_display_name: dihydrolipoyl dehydrogenase

organism: Sus scrofa

substrate_name: 2-Oxoglutarate; NAD+; Coenzyme A

enzyme: dihydrolipoyl dehydrogenase

substrate: 2-Oxoglutarate; NAD+; Coenzyme A


organism: Columba sp.

substrate_name: NAD+; Coenzyme A; 2-Oxoglutarate

substrate: NAD+; Coenzyme A; 2-Oxoglutarate


organism: Lactococcus lactis


enzyme_display_name: aldehyde ferredoxin oxidoreductase

organism: Caldicellulosiruptor bescii

substrate_name: glyceraldehyde 3-phosphate

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

enzyme: aldehyde ferredoxin oxidoreductase

substrate: glyceraldehyde 3-phosphate


organism: Streptomyces collinus

substrate_name: NADP+

assay_conditions_summary: pH 7.4; cofactor NADP+

substrate: NADP+


substrate_name: D-xylose

substrate: D-xylose


organism: Mycobacterium smegmatis

substrate_name: Pyruvate; Coenzyme A; NAD+

substrate: Pyruvate; Coenzyme A; NAD+


organism: Oncorhynchus mykiss


organism: Mycobacterium tuberculosis


substrate_name: NADP+; 2-Oxoglutarate; Coenzyme A

substrate: NADP+; 2-Oxoglutarate; Coenzyme A


enzyme_display_name: fumarate reductase (menaquinone)

substrate_name: Fumarate; Reduced acceptor

enzyme: fumarate reductase (menaquinone)

substrate: Fumarate; Reduced acceptor


enzyme_display_name: alanine dehydrogenase

organism: Streptomyces phaeochromogenes

substrate_name: NAD+

assay_conditions_summary: pH 10

enzyme: alanine dehydrogenase

substrate: NAD+


substrate_name: NADH

substrate: NADH


organism: Thermus caldophilus

substrate_name: pyruvate

substrate: pyruvate


substrate_name: L-Ala

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

assay_conditions_summary: pH 8

substrate: L-Ala


enzyme_display_name: UniProt P9WQB1

substrate_name: L-serine

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

enzyme: UniProt P9WQB1

substrate: L-serine


enzyme_display_name: UniProt O52942

organism: Phormidium lapideum

enzyme: UniProt O52942


enzyme_display_name: glutamate dehydrogenase

organism: Streptomyces fradiae

enzyme: glutamate dehydrogenase


organism: Achlya sp. (in: Oomycetes)


organism: Neurospora crassa


substrate_name: L-glutamate

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

substrate: L-glutamate


organism: Psychrobacter sp.

smiles: N


enzyme_display_name: UniProt Q43314

organism: Arabidopsis thaliana

enzyme: UniProt Q43314


enzyme_display_name: UniProt P00366

organism: Bos taurus

enzyme: UniProt P00366


enzyme_display_name: UniProt P39633

organism: Bacillus subtilis

enzyme: UniProt P39633


enzyme_display_name: UniProt P24295

organism: [Clostridium] symbiosum

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

enzyme: UniProt P24295


enzyme_display_name: UniProt P00370

organism: Escherichia coli

enzyme: UniProt P00370


enzyme_display_name: UniProt B6V7E4

organism: Aspergillus niger

enzyme: UniProt B6V7E4


substrate_name: NADPH

substrate: NADPH


enzyme_display_name: UniProt Q8ILF7

organism: Plasmodium falciparum

enzyme: UniProt Q8ILF7


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

organism: Chlamydomonas reinhardtii

assay_conditions_summary: cofactor NADH

proof_lines: isozyme 2, amination activity, cofactor NADH

proof_lines: isozyme 1, amination activity, cofactor NADH

proof_lines: isozyme 1, amination activity, cofactor NADPH

enzyme: glutamate dehydrogenase [NAD(P)+]


organism: Janthinobacterium lividum

assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+


organism: Lemna minor


assay_conditions_summary: cofactor NADPH


proof_lines:
cosubstrate NADPH
cosubstrate NADH


substrate_name: glutamate

substrate: glutamate


proof_lines:
cosubstrates NADPH + 2-oxoglutarate
cosubstrates NADH + 2-oxoglutarate


enzyme_display_name: UniProt A0A0U4QBJ6

organism: Corynebacterium glutamicum

assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+

enzyme: UniProt A0A0U4QBJ6


assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH


assay_conditions_summary: pH 7; 303.15 K; cofactor NADH


enzyme_display_name: glutamate dehydrogenase (NADP(+))

enzyme: glutamate dehydrogenase (NADP(+))


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


organism: Azospirillum brasilense

assay_conditions_summary: pH 10; cofactor NADP+

proof_lines:
cofactor NAD+, value below 200.0
cofactor NADP+
NADP+-dependent activity


proof_lines:
cofactor NADH
NADPH-dependent activity
NADH-dependent activity


proof_lines: biphasic Lineweaver-Burk plot suggests 2 Km values


substrate_name: Unknown

proof_lines:
at pH 10.0
at pH 8.5

substrate: Unknown


organism: Cereibacter sphaeroides

assay_conditions_summary: pH 7.2; cofactor NADH

proof_lines:
50 mM Tris-HCl, pH 7.2
500 mM Tris-HCl, pH 8.2
500 mM Tris-HCl, pH 7.2


assay_conditions_summary: pH 7.2; cofactor NAD+

proof_lines:
50 mM Tris-HCl, pH 7.2
500 mM Tris-HCl, pH 9.4
500 mM Tris-HCl, pH 7.2


assay_conditions_summary: pH 7.2; cofactor NADPH

proof_lines:
50 mM Tris-HCl, pH 7.2
500 mM Tris-HCl, pH 7.2
500 mM Tris-HCl, pH 8.2


proof_lines:
500 mM Tris-HCl, pH 8.2
500 mM Tris-HCl, pH 7.2
50 mM Tris-HCl, pH 7.2


column_label: Table 2; Glu-degradation reaction; NADP+ row; columns kcat (s^-1), Km (uM), kcat/Km (s^-1 uM^-1).

normalized_value_unit_evidence: Km 93 uM=0.093 mM; kcat/Km 0.087 s^-1 uM^-1=87 s^-1 mM^-1; exported 87.09677419354838 is the kcat/Km ratio from 8.1/0.093 within Table 2 rounding.

row_label: NADP+

table_label: PMID 28486765 Table 2: Kinetic parameters of CgGDH for both forward and reverse reactions


column_label: Table 2; Glu-production reaction; NADPH row; columns kcat (s^-1), Km (uM), kcat/Km (s^-1 uM^-1); footnote on parenthesized kcat.

normalized_value_unit_evidence: Km 16 uM=0.016 mM; kcat/Km 130 s^-1 uM^-1=130000 s^-1 mM^-1; exported 137500.0 is the kcat/Km ratio from 2200/0.016 within Table 2 rounding.

raw_value_unit_evidence: Table 2 row NADPH reports kcat=(2200 +/- 41) s^-1; Km=16 +/- 1.4 uM; kcat/Km=130 s^-1 uM^-1. Table 2 footnote says parenthesized kcat values were lower due to substrate unsaturation and were not taken into account.

row_label: NADPH


column_label: Table 2; Glu-production reaction; alpha-KG row; columns kcat (s^-1), Km (uM), kcat/Km (s^-1 uM^-1); footnote on parenthesized kcat.

normalized_value_unit_evidence: Km 890 uM=0.89 mM; kcat/Km 2.8 s^-1 uM^-1=2800 s^-1 mM^-1; exported 2808.9887640449438 is the kcat/Km ratio from 2500/0.89 within Table 2 rounding.

raw_value_unit_evidence: Table 2 row alpha-KG reports kcat=(2500 +/- 76) s^-1; Km=890 +/- 78 uM; kcat/Km=2.8 s^-1 uM^-1. Table 2 footnote says parenthesized kcat values were lower due to substrate unsaturation and were not taken into account.

row_label: alpha-KG


column_label: Table 3; Enzyme CgGDH; Coenzyme NADH row; columns kcat (s^-1), Km (uM), kcat/Km (s^-1 uM^-1).

normalized_value_unit_evidence: Km 160 uM=0.16 mM; kcat/Km 0.0088 s^-1 uM^-1=8.8 s^-1 mM^-1; exported 8.75 is the kcat/Km ratio from 1.4/0.16 within Table 3 rounding.

raw_value_unit_evidence: Table 3 row CgGDH/NADH reports kcat=1.4 +/- 0.37 s^-1; Km=160 +/- 53 uM; kcat/Km=0.0088 s^-1 uM^-1.

row_label: CgGDH NADH

table_label: PMID 28486765 Table 3: Coenzyme specificities of CgGDH and mutants


column_label: Table 2; Glu-production reaction; NH4+ row; columns kcat (s^-1), Km (uM), kcat/Km (s^-1 uM^-1).

normalized_value_unit_evidence: Km 33000 uM=33.0 mM; kcat/Km 0.10 s^-1 uM^-1=100 s^-1 mM^-1; exported 103.03030303030303 is the kcat/Km ratio from 3400/33.0 within Table 2 rounding.


column_label: Table 2; Glu-degradation reaction; Glu row; columns kcat (s^-1), Km (uM), kcat/Km (s^-1 uM^-1).

row_label: Glu


organism: Mycobacterium smegmatis

substrate_name: H+; NH3; 2-Oxoglutarate; NADH

substrate: H+; NH3; 2-Oxoglutarate; NADH


organism: Homo sapiens

substrate_name: H+; 2-Oxoglutarate; NH3; NADH

substrate: H+; 2-Oxoglutarate; NH3; NADH


substrate_name: 2-Oxoglutarate; NADH; H+; NH3

substrate: 2-Oxoglutarate; NADH; H+; NH3


organism: Bacillus licheniformis

protein_accession_database: NCBI Protein

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

column_label: Table 3, NADPH row: Kcat 11.11 min^-1; Km 0.111 mmol/L; Kcat/Km 100.09 min^-1 mM^-1.

normalized_value_unit_evidence: Kcat normalized_value=0.18516666666666667 normalized_unit=s^-1; Km normalized_value=0.111 normalized_unit=mM; Kcat/Km normalized_value=1.6681666666666666 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: NADPH row: Kcat raw_value=11.11 raw_unit=min^-1; Km raw_value=0.111 raw_unit=mmol/L; Kcat/Km raw_value=100.09 raw_unit=min^-1*mM^-1.

table_label: Table 3, PDF page 6


column_label: Table 3, L-glutamate row: Kcat 3.70 min^-1; Km 23.296 mmol/L; Kcat/Km 0.159 min^-1 mM^-1.

normalized_value_unit_evidence: Kcat normalized_value=0.06166666666666667 normalized_unit=s^-1; Km normalized_value=23.296 normalized_unit=mM; Kcat/Km normalized_value=0.00265 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: L-glutamate row: Kcat raw_value=3.70 raw_unit=min^-1; Km raw_value=23.296 raw_unit=mmol/L; Kcat/Km raw_value=0.159 raw_unit=min^-1*mM^-1.

row_label: L-glutamate


column_label: Table 3, 2-Oxoglutarate row: Kcat 9.09 min^-1; Km 4.727 mmol/L; Kcat/Km 1.923 min^-1 mM^-1.

normalized_value_unit_evidence: Kcat normalized_value=0.1515 normalized_unit=s^-1; Km normalized_value=4.727 normalized_unit=mM; Kcat/Km normalized_value=0.03205 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: 2-Oxoglutarate row: Kcat raw_value=9.09 raw_unit=min^-1; Km raw_value=4.727 raw_unit=mmol/L; Kcat/Km raw_value=1.923 raw_unit=min^-1*mM^-1.


sequence_source: uniparc

sequence_variant_note: Resolved canonical sequence from uniparc and applied mutation signature K136A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniparc and applied mutation signature S265A to reconstruct the assayed variant sequence.


organism: Sphagnum fallax


assay_conditions_summary: cofactor NAD+


proof_lines:
cofactor NADH
cofactor NADPH


organism: Thielaviopsis paradoxa

assay_conditions_summary: pH 8.5; 333.15 K; cofactor NADH


assay_conditions_summary: pH 9.5; 333.15 K; cofactor NAD+


substrate_name: L-alanine

substrate: L-alanine


organism: Bacteroides fragilis

proof_lines: reductive amination, low-activity form of the enzyme

proof_lines: reductive amination, high-activity form of the enzyme


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

proof_lines: oxidative deamination, low-activity form of the enzyme

proof_lines: oxidative deamination, high-activity form of the enzyme

substrate: NADP+


proof_lines: isozyme 1, amination activity, cofactor NADH

proof_lines: isozyme 3, amination activity, cofactor NADH

proof_lines: isozyme 2, amination activity, cofactor NADH


proof_lines:
isozyme 1, deamination activity
isozyme 2, deamination activity
isozyme 3, deamination activity


proof_lines: isozyme 1, amination activity, cofactor NADPH

proof_lines: isozyme 3, amination activity, cofactor NADPH

proof_lines: isozyme 2, amination activity, cofactor NADPH


proof_lines:
isozyme 1, deamination activity
isozyme 3, deamination activity
isozyme 2, deamination activity


enzyme_display_name: glutamate dehydrogenase (NADP+)

organism: Acropora formosa

enzyme: glutamate dehydrogenase (NADP+)


proof_lines: oxidative deamination, biphasic kinetics


organism: Thermus thermophilus

assay_conditions_summary: pH 8; 310.15 K; buffer and 2 mM EDTA, pH 8, at 37°C; cofactor NADH

proof_lines: recombinant enzyme complex TtGDH-APRTh, pH and temperature not specified in the publication

proof_lines: recombinant enzyme complex TtGDH-APRTh, with AMP, pH and temperature not specified in the publication

proof_lines: recombinant enzyme complex TtGDH-APRTh, with L-leucine, pH and temperature not specified in the publication


assay_conditions_summary: pH 8; 310.15 K; buffer and 2 mM EDTA, pH 8, at 37°C


proof_lines: recombinant enzyme complex TtGDH-APRTh, low Glu concentration, pH and temperature not specified in the publication

proof_lines: recombinant enzyme complex TtGDH-APRTh, low Glu concentration, with AMP, pH and temperature not specified in the publication

proof_lines: recombinant enzyme complex TtGDH-APRTh, high Glu concentration, pH and temperature not specified in the publication


assay_conditions_summary: pH 8; 310.15 K; buffer and 2 mM EDTA, pH 8, at 37°C; cofactor NAD+


organism: Bacillus japonicum

assay_conditions_summary: cofactor NADH


organism: Aeropyrum pernix

assay_conditions_summary: pH 8.3; 323.15 K; cofactor NADPH


assay_conditions_summary: pH 8.3; 323.15 K; cofactor NADP+


organism: Blastocladiella emersonii


organism: Metabacillus fastidiosus


assay_conditions_summary: cofactor NADPH


organism: Pyrococcus furiosus

assay_conditions_summary: pH 7.6; 333.15 K; cofactor NADPH


assay_conditions_summary: pH 7.6; 333.15 K; cofactor NADP+


assay_conditions_summary: pH 7.6; 323.15 K; cofactor NADPH


organism: Alicyclobacillus acidocaldarius


organism: Priestia megaterium


organism: Thermococcus waiotapuensis


assay_conditions_summary: pH 8; 353.15 K; cofactor NADP+


assay_conditions_summary: pH 8; 353.15 K; cofactor NADPH


organism: Thermophilic bacillus


organism: Thermococcus sp.

assay_conditions_summary: 353.15 K; cofactor NADP+


assay_conditions_summary: 353.15 K; cofactor NADPH


organism: Corallomycetella repens


proof_lines:
reductive amination, biphasic kinetics
biphasic kinetics
reductive amination


organism: Haloferax mediterranei

assay_conditions_summary: pH 8.5; 298.15 K; cofactor NADP+

proof_lines:
reductive amination at 25°C
pH 8.5, 40°C


assay_conditions_summary: pH 8.5; 313.15 K; cofactor NADP+

proof_lines:
pH 8.5, 40°C
reductive amination at 25°C


assay_conditions_summary: 298.15 K; cofactor NADP+


organism: Geotrichum candidum

assay_conditions_summary: pH 4; 303.15 K; cofactor NADP+

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


organism: Pyrococcus sp.


organism: Salinibacter ruber

assay_conditions_summary: pH 8; cofactor NADH


assay_conditions_summary: pH 8; cofactor NADPH


assay_conditions_summary: pH 8


organism: Limosilactobacillus fermentum

assay_conditions_summary: cofactor NADP+


organism: Archaeoglobus fulgidus

assay_conditions_summary: 333.15 K; cofactor NADPH


assay_conditions_summary: 333.15 K; cofactor NADP+


organism: Proteus inconstans

assay_conditions_summary: cofactor NADPH


proof_lines:
oxidative deamination
reductive amination


organism: Bacteroides ovatus


organism: Phocaeicola vulgatus


organism: Parabacteroides distasonis


organism: uncultured bacterium

assay_conditions_summary: pH 8; 343.15 K; cofactor NADP+


assay_conditions_summary: pH 8; 343.15 K; cofactor NAD+


organism: Thermococcus litoralis


organism: Rattus norvegicus

proof_lines: animals treated with alkalized extract from the tuber of Corydalis ternata


assay_conditions_summary: cofactor NADH


organism: Pyrobaculum islandicum


organism: Aeropyrum pernix K1

assay_conditions_summary: 323.15 K; cofactor NADPH

proof_lines:
reductive amination at 50°C
reductive amination
reductive amination at 70°C


proof_lines:
oxidative deamination at 50°C
oxidative deamination


assay_conditions_summary: 353.15 K; cofactor NADP+

proof_lines: recombinant enzyme, oxidative deamination


organism: Urocitellus richardsonii

proof_lines:
euthermic animal, assay at 37°C
hibernating animal, assay at 5°C
hibernating animal, assay at 37°C


proof_lines:
hibernating animal, assay at 5°C
assay at 5°C
euthermic animal, assay at 5°C


proof_lines:
assay at 5°C
euthermic animal, assay at 37°C
hibernating animal, assay at 5°C


organism: Thunnus thynnus


organism: Entodinium caudatum

assay_conditions_summary: cofactor NAD+


organism: Bacillus licheniformis


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH


organism: Aspergillus ochraceus


organism: Bifidobacterium bifidum


organism: Dictyostelium discoideum


enzyme_display_name: L-amino-acid dehydrogenase

organism: Bacillus subtilis

proof_lines:
(+ L-isoleucine)
(+ L-valine)

enzyme: L-amino-acid dehydrogenase


substrate_name: L-isoleucine

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

substrate: L-isoleucine


substrate_name: L-valine

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

substrate: L-valine


organism: Plasmodium falciparum


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


organism: Kluyveromyces lactis

proof_lines: S0.5 value, Hill coefficient 4, pH 5.8, 30°C


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

proof_lines: S0.5 value, Hill coefficient 1.8, pH 7.5, 30°C


proof_lines: S0.5 value, Hill coefficient 2.7, pH 7.5, 30°C


organism: Janthinobacterium lividum

proof_lines: pH 6.5, 25°C, recombinant enzyme, in presence of 10 mM L-aspartate


proof_lines: as NH4+, pH 6.5, 25°C, recombinant enzyme, in absence of L-aspartate


organism: Thermus thermophilus


assay_conditions_summary: pH 9.5; 298.15 K; cofactor NAD+

proof_lines: in the presence of 20 mM L-glutamate, in 100 mM glycine/NaOH (pH 9.5), at 25°C


proof_lines: in the presence of 5 mM NAD+, in 100 mM glycine/NaOH (pH 9.5), at 25°C