Nitrilase enzymes catalyse the hydrolysis of nitriles to carboxylic acids and ammonia, without the formation of "free" amide intermediates. Nitrilases are involved in natural product biosynthesis and post translational modifications in plants, animals, fungi and certain prokaryotes. Nitrilases can also be used as catalysts in preparative organic chemistry. Among others, nitrilases have been used for the resolution of racemic mixtures. Nitrilase should not be confused with nitrile hydratase which hydrolyses nitriles to amides. Nitrile hydratases are almost invariably co-expressed with an amidase, which converts the amide to the carboxylic acid. Consequently, it can sometimes be difficult to distinguish nitrilase activity from nitrile hydratase plus amidase activity.
Paenarthrobacter ureafaciens KI72, popularly known as nylon-eating bacteria, is a strain of Paenarthrobacter ureafaciens that can digest certain by-products of nylon 6 manufacture. It uses a set of enzymes to digest nylon, popularly known as nylonase.
CRT is the gene cluster responsible for the biosynthesis of carotenoids. Those genes are found in eubacteria, in algae and are cryptic in Streptomyces griseus.
Bradyrhizobium is a genus of Gram-negative soil bacteria, many of which fix nitrogen. Nitrogen fixation is an important part of the nitrogen cycle. Plants cannot use atmospheric nitrogen (N2); they must use nitrogen compounds such as nitrates.
dCMP deaminase is an enzyme which converts deoxycytidylic acid to deoxyuridylic acid.
In enzymology, an opine dehydrogenase (EC 1.5.1.28) is an enzyme that catalyzes the chemical reaction
In enzymology, a cyanoalanine nitrilase (EC 3.5.5.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a cyanuric acid amidohydrolase (EC 3.5.2.15) is an enzyme that catalyzes the chemical reaction
Bradyrhizobium elkanii is a species of legume-root nodulating, microsymbiotic nitrogen-fixing bacterium originally identified as DNA homology group II strains of B. japonicum . In 1988, it was discovered that only DNA homology group II strains caused a destructive bleaching of leaves, termed scientifically "microsymbiont-induced foliar chlorosis", which was widespread in soybean production fields of the southern United States . Whole cell fatty acid content together with antibiotic resistance profiles were major phenotypic differences that helped establish DNA homology group II strains as a new species, Bradyrhizobium elkanii .
3-Carboxy-cis,cis-muconic acid is a metabolite of the catechin degradation by Bradyrhizobium japonicum.
NAAA (gene) may refer to:
5-nitrosalicylate dioxygenase (EC 1.13.11.64, naaB (gene)) is an enzyme with systematic name 5-nitrosalicylate:oxygen 1,2-oxidoreductase (decyclizing). This enzyme catalyses the following chemical reaction
The enzyme 2-oxo-3-(5-oxofuran-2-ylidene)propanoate lactonase (EC 3.1.1.91, naaC (gene); systematic name 2-oxo-3-(5-oxofuran-2-ylidene)propanoate lactonohydrolase) catalyses the reaction
3-Fumarylpyruvate hydrolase (EC 3.7.1.20, nagK (gene), naaD (gene)) is an enzyme with systematic name 3-fumarylpyruvate hydrolyase. This enzyme catalyses the following chemical reaction
Bradyrhizobium canariense is a species of legume-root nodulating, endosymbiont nitrogen-fixing bacterium. It is acid-tolerant and nodulates endemic genistoid legumes from the Canary Islands. The type strain is BTA-1T.
Bradyrhizobium yuanmingense is a species of legume-root nodulating, endosymbiont nitrogen-fixing bacterium, associated with Lespedeza and Vigna species. Its type strain is CCBAU 10071(T).
Bradyrhizobium diazoefficiens is a species of bacteria from the genus of Bradyrhizobium.
Bradyrhizobium jicamae is a Gram-negative, strictly aerobic bacteria from the genus Bradyrhizobium.
Bradyrhizobium pachyrhizi is a bacterium from the genus of Bradyrhizobium which was isolated from nodules of Pachyrhizus erosus in Guanacaste in Costa Rica.
3-Fumarylpyruvic acid, or 3-fumarylpyruvate, is a dicarboxylic acid formed from the isomerisation of 3-maleylpyruvate by maleylpyruvate isomerase. It is converted into fumarate and pyruvate by 3-fumarylpyruvate hydrolase.
