Metallocarboxypeptidase G (Porphyromonas gingivalis)  

Yu-Yen Chen, ... Eric C. Reynolds, in Handbook of Proteolytic Enzymes (Third Edition), 2013

Name and History

The first isolated carboxypeptidase from Porphyromonas gingivaliswas reported in 2002 by two independent research groups. Masuda et al. [1] reported the isolation of ‘Arg carboxypeptidase’ (RCP) from strain W381, which was resolved by SDS-PAGE into three major bands of 43, 33 and 32 kDa with identical N-terminal amino acid sequences (YEWNAYPTYEAYISMMEEFQTKYPSLXTXS). Chen et al. [2] purified a 70 kDa soluble enzyme to apparent homogeneity from strain HG66, with the same N-terminal amino acid sequence(YEWNAYPTYEAYISMMEEFQ). This purified enzyme was designated CPG70 to reflect its measured mass 69.8 kDa by MALDI-TOF mass spectrometry (MS) and its precursor protein CPG, short for (metallo)carboxypeptidase G to indicate its production by P. gingivalis, i.e. CPG.

CPG/CPG70 is also known as immunoreactive 92 kDa antigen PG21[3] and has been described in the literature by its various gene locusnames depending on the bacterial strains and the genome databases used. For example, the cpg locus in P. gingivalis strain W83 has been referred to as PG0232 (TIGR/JCVI Locus; now PG_0232) or PG0212 (LANL Gene ID). CPG70 is unrelated to carboxypeptidase G, first reported in 1967 by Levy and Goldman [4], or G1 and G2, all of which were renamed by NC-IUBMB and MEROPS as glutamate carboxypeptidase (Chapter 355).

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