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Nitrilases superfamily

Brenner, C. (2002) Catalysis in the nitrilase superfamily. Current Opinion in Structural Biology, 12, 775-782. [Pg.193]

The a-chloroacetamide group has features that are beneficial for undirected ABPP. Its small size does not bias binding elements towards a specific class of enzyme, and it possesses reactivity towards a broad variety of nucleophilic amino acid residues. A library of a-chloroacetamide-based probes were synthesized by Cravatt s group. The binding element in these probes was a dipeptide that was varied with small, large, hydrophobic, and charged side chains, and a biotin or rhodamine tag was appended as a reporter tag. Upon screening of eukaryotic proteomes with this library, many enzymes previously unaddressed by directed ABPP probes were uncovered. These included fatty acid synthase, hydro-xypyruvate reductase, malic enzyme, and the nitrilase superfamily [163, 164]. In contrast to the sulfonate esters, a-chloroacetamides react preferentially with cysteine residues in the proteome. [Pg.27]

Nitrilases and amidases belong to the class of hydrolases and nitrile hydratase belongs to the class of lyase. Nitrilases are an important class of nitrilase superfamily that convert nitrile to the corresponding carboxylic acids and ammonia, whereas nitrile hydratase first converts into the corresponding amide and then this amide is transformed by amidase. There are very few reports for the surface modification of PAN and PA for increasing its hydrophilicity using nitrilases, nitrile hydratases, and amidases. [Pg.98]

Branches of Nitrilase Superfamily with Their Substrates... [Pg.365]

Cyanide hydratase and cyanide dihydratase belongs to the nitrilase branch of nitrilase superfamily, using HCN as the only efficient substrate and producing amide and acid products, respectively. Microorganisms appear in fact to have evolved separate metabolic pathways for the hydrolysis of inorganic cyanide. Thus, most nitrilases (as well as nitrile hydratases) till now investigated do not display activity... [Pg.365]

The CO—NH amide bond is relatively energy-rich and can be hydrolyzed to free carboxylic acids and ammonia, by a variety of unrelated or distantly related enzymes, called amidases. Most of amidases are sulfhydryl enzymes like all members of the nitrilase superfamily, while other amidases such as those from Pseudomonas... [Pg.368]

Pace, H.C. and Brenner, C. 2001. The nitrilase superfamily Classification, structure and function. Genome Biology, 2 1-9. [Pg.411]

The similarity of fungal nitrilases to plant nitrilases or to the Nit domain of the NitFHit protein from Caenorhahditis elegans, one of the crystallized members of the nitrilase superfamily, is below 30%, but the sequences flanking the catalytic triad (Glu-Lys-Cys) residues show higher similarities (see Figure 14.3). [Pg.232]

Nitrilases are classified into branch 1 of the nitrilase superfamily, which is comprised of enzymes acting on various nonpeptide CN bonds [15]. All the proteins of this superfamily are characterized by a conserved catalytic triade (glu, lys, cys) and an additional conserved glu residue that seems to participate in the reaction mechanism [2]. Members of class 1 transform the CN bonds in nitriles and cyanides. The enzymes in which these activities were confirmed share in some cases levels of aa sequence identity as low as about 20%. This sequence diversity is reflected in different substrate specificities and different reaction products (carboxylic acids, amides) in various subtypes of these enzymes (aromatic nitrilases, aliphatic nitrilases, arylacetonitrilases, cyanide hydratases, cyanide dihydratases). [Pg.272]

Investigation of the structure-function relationships in nitrilases was largely based on sequence analyses, homology modeling, and mutational studies, as the crystal structures of nitrile-hydrolyzing enzymes have not been available except for an aliphatic nitrilase from Pyrococcus abyssi [13]. Other crystallized members of the nitrilase superfamily (amidases, N-carbamoyl-D-amino acid amidohydrolases, etc. [9]) shared only low levels of identity with experimentally confirmed nitrilases. [Pg.275]

Aliphatic amidase enzymes demonstrate sequence similarity to the nitrilase superfamily thus indicating some form of evolutionary relationship. These amidases contain a Glu-Lys-Cys catalytic triad and exist as homotetrameric or homohexameric sttuctures that function via a ping-pong (bi-bi) reaction mechanism [60, 61]. [Pg.304]


See other pages where Nitrilases superfamily is mentioned: [Pg.357]    [Pg.364]    [Pg.364]    [Pg.364]    [Pg.229]    [Pg.235]    [Pg.657]    [Pg.238]    [Pg.238]    [Pg.250]    [Pg.276]    [Pg.301]    [Pg.331]   
See also in sourсe #XX -- [ Pg.364 ]




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Nitrilases

Superfamily

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