Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.8.1.14 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
Search for more literature for 1.8.1.14

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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
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

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Bacillus anthracis
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

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

Turnover Number [1/s]

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

Cofactor

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

kcat/KM [mM/s]

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