20 research outputs found
Aminopeptidase C of Aspergillus niger is a Novel Phenylalanine Aminopeptidase
Get PDFA novel enzyme with a specific phenylalanine aminopeptidase activity (ApsC) from Aspergillus niger (CBS 120.49) has been characterized. The derived amino acid sequence is not similar to any previously characterized aminopeptidase sequence but does share similarity with some mammalian acyl-peptide hydrolase sequences. ApsC was found to be most active towards phenylalanine beta-naphthylamide (F-betaNA) and phenylalanine para-nitroanilide (F-betaNA), but it also displayed activity towards other amino acids with aromatic side chains coupled to betaNA; other amino acids with nonaromatic side chains coupled to either pNA or betaNA were not hydrolyzed or were poorly hydrolyzed. ApsC was not able to hydrolyze N-acetylalanine-pNA, a substrate for acyl-peptide hydrolases
Functional and physical interactions of components of the yeast mitochondrial inner-membrane import machinery (MIM)
Get PDFDeterminants for binding of a 40 kDa protein to the leaders of yeast mitochondrial mRNAs
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The polytopic mitochondrial inner membrane proteins MIM17 and MIM23 operate at the same preprotein import site.
Get PDFThe polytopic mitochondrial inner membrane proteins MIM17 and MIM23 operate at the same preprotein import site.
Get PDFMultiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane
Get PDFTargeting and assembly of the oxoglutarate carrier: general principles for biogenesis of carrier proteins of the mitochondrial inner membrane
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