Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
C1 family peptidase
This family is closely related to the Peptidase_C1 family Pfam:PF00112, containing several prokaryotic and eukaryotic aminopeptidases and bleomycin hydrolases. [1]. 9546396. The unusual active site of Gal6/bleomycin hydrolase can act as a carboxypeptidase, aminopeptidase, and peptide ligase. Zheng W, Johnston SA, Joshua-Tor L;. Cell 1998;93:103-109. [2]. 7925365. Gene cloning and characterization of PepC, a cysteine aminopeptidase from Streptococcus thermophilus, with sequence similarity to the eucaryotic bleomycin hydrolase. Chapot-Chartier MP, Rul F, Nardi M, Gripon JC;. Eur J Biochem 1994;224:497-506. (from Pfam)
C1 family peptidase (also called papain family protein) may be an endopeptidase or an exopeptidase, and catalyzes the hydrolysis of peptide bonds in substrates using a catalytic dyad of Cys and His residues; similar to Homo sapiens bleomycin hydrolase and Lactobacillus aminopeptidases
aminopeptidase C
PepC (aminopeptidase C) is a cysteine aminopeptidase found in the cytosol in lineages that include Lactobacillus lactis, Listeria monocytogenes, and Streptococcus thermophilus. The enzyme hydrolyzes bleomycin A2, as do its eukaryotic counterparts (hence the designation as EC 3.4.22.40), but bleomycin is unlikely to be the physiological substrate.
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on