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Title: Serine-15 is the regulatory seryl-phosphorylation site in C sub 4 -leaf phosphoenolpyruvate carboxylase (PEPCase) from maize

Conference · · Plant Physiology, Supplement; (USA)
OSTI ID:5851128
;  [1]
  1. Univ. of Nebraska, Lincoln (USA)

The {sup 32}P-labeled regulatory site phosphopeptide was purified from a tryptic digest of in vitro phosphorylated/activated dark-form PEPCase by metal ion affinity and reversed-phase chromatography and subjected to automated Edman degradation analysis. The amino acid sequence of this phosphoseryl peptide is His-His-Ser(P)-Ile-Asp-Ala-Gln-Leu-Arg. This nonapeptide, which corresponds exactly to residues 13-21 in the deduced primary sequence of the maize leaf carboxylase, is far removed from a recently identified active-site cysteine (Cys-553) in the C-terminal region of the primary structure. Comparative analysis of the deduced N-terminal sequences of C{sub 3}, C{sub 4}, and CAM leaf PEPCases suggests that the motif of Lys/Arg-X-X-Ser is an important structural requirement of the C{sub 4}- and CAM-leaf protein-serine kinases.

OSTI ID:
5851128
Report Number(s):
CONF-9007196-; CODEN: PPYSA
Journal Information:
Plant Physiology, Supplement; (USA), Vol. 93:1; Conference: Annual meeting of the American Society of Plant Physiologists, Indianapolis, IN (USA), 29 Jul - 2 Aug 1990; ISSN 0079-2241
Country of Publication:
United States
Language:
English