Coenzyme-linked reactions involving l(+)glutamic dehydrogenase
نویسندگان
چکیده
منابع مشابه
Coenzyme A-linked Aldehyde Dehydrogenase from EschericKa coli
Coenzyme A-linked aldehyde dehydrogenase from Escherichia coIi strain B was purified 170-fold over cell-free extracts, and certain of its properties were investigated. The enzyme is essentially inactive in the absence of sulfhydryl compounds such as dithiothreitol and /3-mercaptoethanol. Addition of a thiol reagent after incubation of the enzyme with substrates results in very slow reactivation...
متن کاملGlutaryl-Coenzyme A dehydrogenase deficiency
Key-words Disease name and synomyms Diagnosis criteria/definition Differential diagnosis Incidence Clinical description Treatment Etiology Diagnostic methods Genetic counseling and prenatal diagnosis Unresolved questions and outlook References
متن کاملThe crotonase superfamily: divergently related enzymes that catalyze different reactions involving acyl coenzyme a thioesters.
Synergistic investigations of the reactions catalyzed by several members of an enzyme superfamily provide a more complete understanding of the relationships between structure and function than is possible from focused studies of a single enzyme alone. The crotonase (or enoyl-CoA hydratase) superfamily is such an example whereby members catalyze a wide range of metabolic reactions but share a co...
متن کاملIdentification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea.
Two putative malate dehydrogenase genes, MJ1425 and MJ0490, from Methanococcus jannaschii and one from Methanothermus fervidus were cloned and overexpressed in Escherichia coli, and their gene products were tested for the ability to catalyze pyridine nucleotide-dependent oxidation and reduction reactions of the following alpha-hydroxy-alpha-keto acid pairs: (S)-sulfolactic acid and sulfopyruvic...
متن کاملPurification and properties of the inducible coenzyme A-linked butyraldehyde dehydrogenase from Clostridium acetobutylicum.
The coenzyme A (CoA)-linked butyraldehyde dehydrogenase (BAD) from Clostridium acetobutylicum was characterized and purified to homogeneity. The enzyme was induced over 200-fold, coincident with a shift from an acidogenic to a solventogenic fermentation, during batch culture growth. The increase in enzyme activity was found to require new protein synthesis since induction was blocked by the add...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1939
ISSN: 0306-3283
DOI: 10.1042/bj0330549