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Literature summary extracted from

  • Wallen, J.R.; Paige, C.; Mallett, T.C.; Karplus, P.A.; Claiborne, A.
    Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of dual NAD(P)H specificity (2008), Biochemistry, 47, 5182-5193.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.1.14 expressed in Escherichia coli B834(DE3) cells Bacillus anthracis
1.8.1.14 expression in Escherichia coli, wild-type and mutant enzymes C42S, and Y367F, Y425F, and Y367/Y425F Bacillus anthracis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.1.14 crystal structure at 2.30 A resolution. The structures of the NADH and NADPH complexes at ca. 2.3 A resolution reveal that a loop consisting of residues Glu180-Thr187 becomes ordered and changes conformation on NAD(P)H binding Bacillus anthracis
1.8.1.14 sitting drop vapor diffusion method, using 16-26% 2-methyl-2,4-pentanediol, 0.2 M magnesium acetate, and 0.1 M sodium cacodylate, pH 6.5, at 15°C Bacillus anthracis

Protein Variants

EC Number Protein Variants Comment Organism
1.8.1.14 Y367/Y425F inactive mutant enzyme Bacillus anthracis
1.8.1.14 Y367F kcat for NADH is 3.9fold lower than wild-type value, kcat for NADPH is 5.6fold lower than wild-type value Bacillus anthracis
1.8.1.14 Y367F the mutant is 18% as active as wild type enzyme Bacillus anthracis
1.8.1.14 Y367F/Y425F inactive Bacillus anthracis
1.8.1.14 Y425F kcat for NADH is 30fold lower than wild-type value, kcat for NADPH is 93fold lower than wild-type value Bacillus anthracis
1.8.1.14 Y425F the mutant is 1% as active as wild type enzyme Bacillus anthracis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.1.14 0.001
-
NADH 25°C, wild-type enzyme Bacillus anthracis
1.8.1.14 0.002
-
NADH wild type enzyme, at 25°C Bacillus anthracis
1.8.1.14 0.002
-
CoA-disulfide 25°C, wild-type enzyme. Cosubstrate: NADH Bacillus anthracis
1.8.1.14 0.003
-
NADPH 25°C, wild-type enzyme Bacillus anthracis
1.8.1.14 0.006
-
NADPH wild type enzyme, at 25°C Bacillus anthracis
1.8.1.14 0.006
-
CoA-disulfide 25°C, wild-type enzyme, cosubstrate: NADPH Bacillus anthracis

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.14 Bacillus anthracis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.14
-
Bacillus anthracis
1.8.1.14 Q-Sepharose column chromatography and Ni-NTA column chromatography Bacillus anthracis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.14 CoA disulfide + NADH
-
Bacillus anthracis CoA + NAD+
-
?
1.8.1.14 CoA disulfide + NADPH
-
Bacillus anthracis CoA + NADP+
-
?
1.8.1.14 CoA-disulfide + NADH + H+ Bacillus anthracis CoADR can use either pyridine nucleotide equally well Bacillus anthracis CoA + NAD+
-
?
1.8.1.14 CoA-disulfide + NADPH + H+ Bacillus anthracis CoADR can use either pyridine nucleotide equally well Bacillus anthracis CoA + NADP+
-
?

Synonyms

EC Number Synonyms Comment Organism
1.8.1.14 BACoADR
-
Bacillus anthracis
1.8.1.14 CoADR
-
Bacillus anthracis
1.8.1.14 coenzyme A-disulfide reductase
-
Bacillus anthracis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.1.14 0.3
-
CoA-disulfide 25°C, mutant enzyme Y25F. Cosubstrate: NADH Bacillus anthracis
1.8.1.14 0.3
-
NADPH mutant enzyme Y425F, at 25°C Bacillus anthracis
1.8.1.14 0.9
-
NADH 25°C, mutant enzyme Y25F Bacillus anthracis
1.8.1.14 0.9
-
NADH mutant enzyme Y425F, at 25°C Bacillus anthracis
1.8.1.14 2 8 NADPH 25°C, wild-type enzyme Bacillus anthracis
1.8.1.14 2 8 NADPH wild type enzyme, at 25°C Bacillus anthracis
1.8.1.14 5
-
CoA-disulfide 25°C, mutant enzyme Y367F. Cosubstrate: NADH Bacillus anthracis
1.8.1.14 5
-
NADPH mutant enzyme Y367F, at 25°C Bacillus anthracis
1.8.1.14 7
-
NADH 25°C, mutant enzyme Y367F Bacillus anthracis
1.8.1.14 7
-
NADH mutant enzyme Y367F, at 25°C Bacillus anthracis
1.8.1.14 27
-
NADH 25°C, wild-type enzyme Bacillus anthracis
1.8.1.14 27
-
NADH wild type enzyme, at 25°C Bacillus anthracis

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.14 FAD
-
Bacillus anthracis
1.8.1.14 NADH
-
Bacillus anthracis
1.8.1.14 NADH CoADR exhibits dual specificity with respect to the NAD(P)H substrate Bacillus anthracis
1.8.1.14 NADPH
-
Bacillus anthracis
1.8.1.14 NADPH CoADR exhibits dual specificity with respect to the NAD(P)H substrate Bacillus anthracis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.8.1.14 0.00027
-
NADH wild type enzyme, at 25°C Bacillus anthracis
1.8.1.14 0.0093
-
NADPH wild type enzyme, at 25°C Bacillus anthracis