A new family of carbon-nitrogen hydrolases.
Using computer methods for database search and multiple alignment, statistically significant sequence similarities were identified between several nitrilases with distinct substrate specificity, cyanide hydratases, aliphatic amidases, beta-alanine synthase, and a few other proteins with unknown molecular function. All these proteins appear to be involved in the reduction of organic nitrogen compounds and ammonia production. Sequence conservation over the entire length, as well as the similarity in the reactions catalyzed by the known enzymes in this family, points to a common catalytic mechanism. The new family of enzymes is characterized by several conserved motifs, one of which contains an invariant cysteine that is part of the catalytic site in nitrilases. Another highly conserved motif includes an invariant glutamic acid that might also be involved in catalysis.
Bork
P
P
European Molecular Biology Laboratory, Heidelberg, Germany.
Koonin
E V
EV
D000581:Amidohydrolases / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence; D000619:Aminohydrolases / Q000737:chemistry / Q000378:metabolism; D000641:Ammonia / Q000494:pharmacology; D016208:Databases, Factual; D006836:Hydro-Lyases / Q000737:chemistry / Q000378:metabolism; D006867:Hydrolases / Q000737:chemistry* / Q000378:metabolism; D016247:Information Storage and Retrieval; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D016415:Sequence Alignment; D017385:Sequence Homology
D000641:Ammonia; D006867:Hydrolases; D000581:Amidohydrolases; C021590:beta-ureidopropionase; D000619:Aminohydrolases; C021867:nitrilase; D006836:Hydro-Lyases; C076848:cyanide hydratase