Genes carboxypeptidases

SHIRLEY, A.M., McMICHAEL, C.M., CHAPPLE, C The sng2 mutant of Arabidopsis is defective in the gene encoding the serine carboxypeptidase-like protein sinapoylglucose Choline sinapoyltransferase, Plant J., 2001, 28, 83-94. 

Renaturation of denatured protein is dictated by the primary structure of the protein. The trypsin family of enzymes and carboxypeptidase A are synthesized as proenzymes that are proteolytically activated. The proteolyzed, active enzymes have primary structures different from the gene product and are not active upon renaturation. In addition, zinc is a cofactor required for carboxypeptidase A activity. 

Lehfeldt, C., Shirley, A. M., Meyer, K., Ruegger, M. O., Cusumano, J. C., Viitanen, P. V., Stack, D., and Chappie, C., 2000, Cloning of the SNG1 gene of Arabidopsis reveals a role for a serine carboxypeptidase-1 ike protein as an acyltransferase in secondary metabolism, Plant Cell 12 1295-1306. 

Bacich D. J., Ramadan E., O Keefe D. S., Bukhari N., Wegorzewska I., Ojeifo O., Olszewski R., Wrenn C. C., Bzdega T., Wroblewska B., Heston W. D., and Neale J. H. (2002). Deletion ofthe glutamate carboxypeptidase II gene in mice reveals a second enzyme activity that hydrolyzes N-acetylaspartylglutamate. J. Neurochem. 83 20-29. 

Hamstra, D. A., and Rehemtulla, A. Toward an enzyme/prodrug strategy for cancer gene therapy Endogenous activation of carboxypeptidase A mutants by PACE/furin family of propeptidases. Hum. Gene Ther. 10 235-248, 1999. 

Cloning and Expression of Acid Carboxypeptidase Gene (CPDS)... 

Chiba, Y., Midorikawa, T., and Ichishima, E. (1995). Cloning and expression of the carboxypeptidase gene from Aspergillus saitoi and determination of the catalytic residues by site-directed mutagenesis. Biochem. J., 308, 405-409. 

Agouti Gene and Agouti Protein Melanocortin Receptors Proposed Feedback Loop Fat Gene and Carboxypeptidase E Tubby Gene Summary References Bibliography... 

In 1993, a thermostable aminoacylase from Bacillus stearothermophilus was characterized by Sakanyan et al.l51. The enzyme hydrolyzes N-acyl derivatives of aromatic amino acids preferentially and even has some dipeptidase activity. Its optimal reaction temperature is 70 °C after incubation for 15 min, 90% of the original activity was retained. The authors write that the similarity of the B. stearothermophilus enzyme sequence with that of other enzymes such as aminoacylase I, acetylornithine deacetylase and carboxypeptidase G2 suggests a common origin. The aminoacylase from B. stearothermophilus is well characterized the gene has been completely sequenced1511, cloned into E. coli and overexpressed[51> 671 and studied for catalytic and stability properties16 1 the intrinsic one Zn2+ ion per subunit seems to have a predominantly structural role and activity can be restored to the apo-enzyme by Co2+ and particularly by Cd2+ (3-fold activity ) but not by Zn2+. 

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