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

BRENDA support

Literature summary for 1.6.1.2 extracted from

  • Bizouarn, T.; Grimley, R.; Diggle, C.; Thomas, C.M.; Jackson, J.B.
    Mutations at tyrosine-235 in the mobile loop region of domain I protein of transhydrogenase from Rhodospirillum rubrum strongly inhibit hydride transfer (1997), Biochim. Biophys. Acta, 1320, 265-274.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of domain I Y235N and Y235F mutants in Escherichia coli Rhodospirillum rubrum

Protein Variants

Protein Variants Comment Organism
Y235F mutant domain I/wild-type domain III mixtures catalyse acetylpyridine adenine dinucleotide reduction with similar rates as wild-type domain I/wild-type domain III mixtures Rhodospirillum rubrum
Y235N mutant domain I/wild-type domain III mixtures catalyse acetylpyridine adenine dinucleotide reduction with similar rates as wild-type domain I/wild-type domain III mixtures Rhodospirillum rubrum

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Rhodospirillum rubrum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Rhodospirillum rubrum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADPH + oxidized 3-acetylpyridine adenine dinucleotide enzyme also catalyzes a rapid, so called cyclic reaction, i.e. the reduction of acetylpyridine adenine dinucleotide in the presence of either NADP+ or NADPH: the NADPH/NADP+ remain permanently bound to domain III and are alternately oxidized by acetylpyridine adenine dinucleotide and then reduced by NADH in domain I Bos taurus NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
?
NADPH + oxidized 3-acetylpyridine adenine dinucleotide enzyme also catalyzes a rapid, so called cyclic reaction, i.e. the reduction of acetylpyridine adenine dinucleotide in the presence of either NADP+ or NADPH: the NADPH/NADP+ remain permanently bound to domain III and are alternately oxidized by acetylpyridine adenine dinucleotide and then reduced by NADH in domain I Rhodospirillum rubrum NADP+ + reduced 3-acetylpyridine adenine dinucleotide
-
?

Subunits

Subunits Comment Organism
? domain I contains the binding site for NAD+ and NADH, domain III for NADP+ and NADPH Rhodospirillum rubrum
? domain I exists as a seperate polypeptide that can be removed from everted membrane vesicle i.e. chromatophores Rhodospirillum rubrum

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Bos taurus
NAD+
-
Rhodospirillum rubrum
NADH
-
Bos taurus
NADH
-
Rhodospirillum rubrum
NADP+
-
Bos taurus
NADP+
-
Rhodospirillum rubrum
NADPH
-
Bos taurus
NADPH
-
Rhodospirillum rubrum