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- W144927104 abstract "This chapter examines the activity, specificity and structural chemistry of aminopeptidase B. Aminopeptidase B is a single-chain protein comprising 650 amino acid residues with a calculated molecular mass of 72,300 Da and a theoretical pi of 5.83. Aminopeptidase B primary structure exhibits an N-terminal putative signal peptide and the consensus Zn2+-binding site. The protein contains at least one disulfide bond and several potential phosphorylation sites. Neither hydrophobic transmembrane domains nor N-glycosylation sites could be predicted from the amino acid sequence. Moreover, aminopeptidase B is not O-glycosylated as demonstrated using endo-α-N-acetylgalactosaminidase. Secondary structure predictions using the Gamier and Robson algorithm indicated that aminopeptidase B might be a β/α protein. In the Ml family, the most closely related protein to aminopeptidase B is LTA4 hydrolase, which exhibits 33% identity and 48% similarity. Aminopeptidase B is present in several rat tissues, in cattle pituitary secretory vesicles and in various cell lines. Observations of seminiferous tubule sections showed that the enzyme is concentrated in the cytoplasm of late spermatids that gives rise to the residual bodies." @default.
- W144927104 created "2016-06-24" @default.
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- W144927104 date "2004-01-01" @default.
- W144927104 modified "2023-09-25" @default.
- W144927104 title "Aminopeptidase B" @default.
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- W144927104 doi "https://doi.org/10.1016/b978-0-12-079611-3.50089-6" @default.
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