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Carboxypeptidase sequence alignment

The sequence alignment between the different carboxypeptidases was the largest... [Pg.86]

Fig. 1 Blocks of multiple sequence alignment of protein sequences of carboxypeptidases from B. taurus, Mus musculus, Rattus norvegicus, Neurospora crassa, Schizosaccharomyces pombe, Drosophila melanogaster, and Homo sapiens along with protein sequence from H. pylori (Uniprot accession code HPAG1 0372 from strain HPAG1). Numbers on the top correspond to amino acid residue number of the carboxypeptidase enzyme from B. taurus. Gray vertical columns indicate conserved residues. Amino acid residues corresponding to Glu-182 and His-306, which coordinate to zinc, are conserved, whereas another Zn-coordinating amino acid residue corresponding to His-179 is substituted by Gin in the Helicobacter sequence. Functionally important residues corresponding to Arg-237 are also conserved... Fig. 1 Blocks of multiple sequence alignment of protein sequences of carboxypeptidases from B. taurus, Mus musculus, Rattus norvegicus, Neurospora crassa, Schizosaccharomyces pombe, Drosophila melanogaster, and Homo sapiens along with protein sequence from H. pylori (Uniprot accession code HPAG1 0372 from strain HPAG1). Numbers on the top correspond to amino acid residue number of the carboxypeptidase enzyme from B. taurus. Gray vertical columns indicate conserved residues. Amino acid residues corresponding to Glu-182 and His-306, which coordinate to zinc, are conserved, whereas another Zn-coordinating amino acid residue corresponding to His-179 is substituted by Gin in the Helicobacter sequence. Functionally important residues corresponding to Arg-237 are also conserved...
The following proteins were chosen for multiple sequence alignment T. califomica acetylcholinesterase, Xanthobacter autotrophicus haloalkane dehalogenase, G. candidum lipase and wheat serine carboxypeptidase. This set was selected because they are all members of the o/fi hydrolase fold family (Ollis et al, 1992). This family of proteins, which is believed to have evolved by... [Pg.658]

Figure 5 Multiple sequence alignment of carboxypeptidases. Similarity of the enzymatically active subunit of human carboxypeptidase N (7) to carboxypeptidase A from bovine (1), rat (3), human mast cell (4), bovine carboxypeptidase B (2), human carboxypeptidase M (5), and bovine carboxypeptidase H (6). Residues identical and conservative changes in at least four proteins are boxed. Arrows indicate active site residues. (From N Refs. 119-123.)... [Pg.87]

Fig. 8 Putative member of carboxypeptidase family from H. pylori HP1075) is aligned with homologous members of bovine carboxypeptidase A. Glu-72, His-169 (Zn binding sites), Arg-145 (carboxylate-binding determinant), and Glu-270 (catalytic residue) are conserved in the H. pylori homologue. However, Zn binding residues corresponding to His-69 are substituted by Gin in the Helicobacter protein sequence... Fig. 8 Putative member of carboxypeptidase family from H. pylori HP1075) is aligned with homologous members of bovine carboxypeptidase A. Glu-72, His-169 (Zn binding sites), Arg-145 (carboxylate-binding determinant), and Glu-270 (catalytic residue) are conserved in the H. pylori homologue. However, Zn binding residues corresponding to His-69 are substituted by Gin in the Helicobacter protein sequence...
Alignment of five completely sequenced members of the pancreatic digestive enzyme carboxypeptidase family1 is shown in Fig. 1, along with hepatopancreatic carboxypeptidase B from crayfish.8 Only the amino acid... [Pg.593]


See other pages where Carboxypeptidase sequence alignment is mentioned: [Pg.159]    [Pg.656]    [Pg.86]    [Pg.154]    [Pg.592]    [Pg.594]    [Pg.83]    [Pg.77]   
See also in sourсe #XX -- [ Pg.593 , Pg.594 ]




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