Pyrrolidonyl peptidase. An enzyme for selective removal of pyrrolidonecarboxylic acid residues from polypeptides.
Pyrrolidonyl peptidase. An enzyme for selective removal of pyrrolidonecarboxylic acid residues from polypeptides.
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吡咯烷酰肽酶。
DOI:
10.1021/bi00842a005
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发表时间:
1968
期刊:
影响因子:
2.9
通讯作者:
R. Armentrout
中科院分区:
文献类型:
--
作者:
R. Doolittle;R. Armentrout
A1. large number of naturallyoccurring peptides and proteins are thought to have pyrrolidonecarboxylic acid (pyroglutamic acid) 1 as their amino-terminal residue (Table I), a situation presumedto arise from the cyclization of terminal glutaminyl (I) or glutamyl (III) residues. In this regard, an enzyme has been found which will cyclize terminal glutamine residues on peptides (Messer and Ottesen, 1964). Pyrrolidonyl peptides (II) also can arise artifactually during the isolation of peptides after proteolysis, glutamineterminating peptides being especially liable to cyclize (Sanger and Thompson, 1953; Smyth et al., 1962). The absence of an «-amino group in these peptides and proteins has been a major handicap in thechar-acterization of many of these materials, since aminoterminal analyses, including stepwise degradation methods (Edman and Begg, 1967), cannot be carried out.Our original aim was to look for an enzyme which would open pyrrolidone rings, the hope being that such an enzyme would render terminal amino groups accessible in PCA-terminating peptides. To this end we isolated a microorganism from the soil which will grow on free PCA as the sole source of carbon and nitrogen. At the time we were unaware that Maruyama and Nomura (1956) had previously isolated a similar