In:
FEBS Letters, Wiley, Vol. 268, No. 2 ( 1990-08), p. 355-359
Abstract:
Five protein serine/threonine phosphatases (PP) have been identified by cloning cDNA from mammalian and Drosophila libraries. These novel enzymes, which have not yet been detected by the techniques of protein chemistry and enzymology, are termed PPV, PP2B w , PPX, PPY and PPZ. The complete amino acid sequences of PPX, PPY and PPZ and an almost complete sequence of PPV are presented. In the catalytic domain PPV and PPX are more similar to PP2A (57–69% identity) than PPI (45–49% identity), while PPY and PPZ are more similar to PP1 (66–68% identity) than PP2A (44% identity). The cDNA for PP2B W encodes a novel Ca 2+ /calmodulin‐dependent protein phosphatase only 62% identical to PP2B in the catalytic domain. Approaches for determining the cellular functions of these protein phosphatases are discussed.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(90)81285-V
Language:
English
Publisher:
Wiley
Publication Date:
1990
detail.hit.zdb_id:
1460391-3
SSG:
12
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