Substrate Specificity of Human Carboxypeptidase A6*

Substrate specificity of human metallocarboxypeptidase D: Comparison of the two active carboxypeptidase domains

Metallocarboxypeptidase D (CPD) is a membrane-bound component of the trans-Golgi network that cycles to the cell surface through exocytic and endocytic pathways. Unlike other members of the metallocarboxypeptidase family, CPD is a multicatalytic enzyme with three carboxypeptidase-like domains, although only the first two domains are predicted to be enzymatically active. To investigate the enzym...

The Specificity of Carboxypeptidase

All the information hitherto available with respect to the specificity of carboxypeptidase has been obtained by the use of crude enzyme preparations (1). Consequently, there still remains some uncertainty as to whether the previously reported hydrolyses of various synthetic substrates, attributed to the action of carboxypeptidase, are all due to the same enzyme. Indeed, Abderhalden and Abderhal...

Comparison of Substrate Specificity of Escherichia Coli p-Aminobenzoyl-Glutamate Hydrolase with Pseudomonas Carboxypeptidase G

Reduced folic acid derivatives support biosynthesis of DNA, RNA and amino acids in bacteria as well as in eukaryotes, including humans. While the genes and steps for bacterial folic acid synthesis are known, those associated with folic acid catabolism are not well understood. A folate catabolite found in both humans and bacteria is p-aminobenzoyl-glutamate (PABA-GLU). The enzyme p-aminobenzoyl-...

Human carboxypeptidase A4: Characterization of the substrate specificity and implications for a role in extracellular peptide processing

1 To whom correspondence should be addressed: Institut de Biotecnologia i de Biomedicina & Departament de Bioquimica, Universitat Autonoma de Barcelona, IBB-Campus de la UAB, Bellaterra (Barcelona), 08193, Spain.Tel.: 34-935811231; Fax: 34-935812011; E-mail: [email protected] 2 To whom correspondence should be addressed: Dept. of Molecular Pharmacology, Albert Einstein College of Medicine, 1...

Substrate Specificity of MMPs