New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases
Author:
- 19 October 2011
- journal article
- review article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 151 (1) , 13-25
Abstract
Peptidases or proteinases are now classified into seven families based on the nature of the catalytic residues [MEROPS—the peptidase database (http://merops.sanger.ac.uk/)]. They are aspartic- (first described in 1993), cysteine- (1993), serine- (1993) metallo- (1993), threonine- (1997), glutamic- (2004) and asparagine-peptidase (2010). By using an S-PI (pepstatin Ac) as a probe, a new subfamily of serine peptidase, serine-carboxyl peptidase (sedolisin) was discovered in 2001. In addition, the sixth family of peptidase, glutamic peptidase (eqolisin) was also discovered in 2004. The former peptidase is widely distributed in nature from archea to mammals, including humans. One of these enzymes is related to a human fatal hereditable disease, Batten disease. In contrast, the distribution of the latter peptidases is limited, with most of them found in human or plant pathogenic fungi. One such enzyme was isolated from a fungal infection in an HIV-infected patient. In this review, the background of the findings, and crystal structures, catalytic mechanisms, substrates specificities and distribution of the new peptidase families are described.Keywords
This publication has 68 references indexed in Scilit:
- Clarification of the Mechanism of Acylation Reaction and Origin of Substrate Specificity of the Serine-Carboxyl Peptidase Sedolisin through QM/MM Free Energy SimulationsThe Journal of Physical Chemistry B, 2011
- Studies on the Catalytic Mechanism of a Glutamic PeptidaseJournal of Biological Chemistry, 2010
- pH controls both transcription and post-translational processing of the protease BcACP1 in the phytopathogenic fungus Botrytis cinereaMicrobiology, 2009
- Crystal Structure and Autoactivation Pathway of the Precursor Form of Human Tripeptidyl-peptidase 1, the Enzyme Deficient in Late Infantile Ceroid LipofuscinosisJournal of Biological Chemistry, 2009
- Inhibition of a Secreted Glutamic Peptidase Prevents Growth of the Fungus Talaromyces emersoniiJournal of Biological Chemistry, 2008
- The QM/MM Molecular Dynamics and Free Energy Simulations of the Acylation Reaction Catalyzed by the Serine-Carboxyl Peptidase Kumamolisin-AsBiochemistry, 2007
- Crystal Structure of Scytalidoglutamic Peptidase with its First Potent Inhibitor Provides Insights into Substrate Specificity and CatalysisJournal of Molecular Biology, 2007
- Isolation and properties of extracellular proteinases of Penicillium marneffeiBiological Chemistry, 2006
- Characterization of Endopeptidase Activity of Tripeptidyl Peptidase-I/CLN2 Protein Which Is Deficient in Classical Late Infantile Neuronal Ceroid LipofuscinosisBiochemical and Biophysical Research Communications, 2000
- Purification and properties of an S-PI(pepstatin Ac)-insensitive carboxyl proteinase from a Xanthomonas sp. bacterium.Agricultural and Biological Chemistry, 1987