Serine-15 is the regulatory seryl-phosphorylation site in C sub 4 -leaf phosphoenolpyruvate carboxylase (PEPCase) from maize
- 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
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Related Subjects
ENZYMES
BIOCHEMICAL REACTION KINETICS
LEAVES
MAIZE
PHOSPHORUS 32
PHOSPHORUS COMPOUNDS
PHOSPHOTRANSFERASES
TRACER TECHNIQUES
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
CEREALS
DAYS LIVING RADIOISOTOPES
GRAMINEAE
ISOTOPE APPLICATIONS
ISOTOPES
KINETICS
LIGHT NUCLEI
LILIOPSIDA
MAGNOLIOPHYTA
NUCLEI
ODD-ODD NUCLEI
PHOSPHORUS ISOTOPES
PHOSPHORUS-GROUP TRANSFERASES
PLANTS
RADIOISOTOPES
REACTION KINETICS
TRANSFERASES
550201* - Biochemistry- Tracer Techniques