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2 results on '"(Chloroplast)"'

1. Ribose-5-phosphate isomerase and ribulose-5-phosphate kinase show apparent specificity for a specific ribulose 5-phosphate species

Author

Louise E. Anderson

Subjects
Aldose-Ketose Isomerases, Biophysics, Ribulose-5-phosphate kinase, Isomerase, Ribose-5-phosphate isomerase, Photosynthesis, Biochemistry, Substrate Specificity, chemistry.chemical_compound, Ribulosephosphates, Ribulose 5-phosphate, Structural Biology, Metabolite channeling, Genetics, Molecular Biology, Pentosephosphates, Kinase, Chemistry, Ribulose, Phosphotransferases, Cell Biology, Molecular biology, Chloroplast, Phosphotransferases (Alcohol Group Acceptor), (Chloroplast), Carbohydrate Epimerases
Abstract

Ribose-5-phosphate isomerase and ribulose-5-phosphate kinase appear to show specificity for a particular ribulose 5-phosphate species. The effect of this specificity will be channeling of ribulose 5-phosphate from the isomerase to the kinase during photosynthesis.

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2. Catalytic and noncatalytic nucleotide binding sites of chloroplast F1 ATPase. Photoaffinity labeling and peptide sequencing

Author

Jun-Mei Zhou, Chad G. Miller, Zhixiong Xue, and Paul D. Boyer

Subjects
Chloroplasts, Photochemistry, ATPase, Biophysics, Biochemistry, Peptide Mapping, Adenosine Triphosphate, Structural Biology, Peptide sequence, Genetics, Moiety, 2-Azido-ATP, Nucleotide, Binding site, Tyrosine, Molecular Biology, chemistry.chemical_classification, Binding Sites, biology, Photoaffinity labeling, Chemistry, Adenine Nucleotides, Site labeling, Affinity Labels, Cell Biology, Peptide Fragments, Adenosine Diphosphate, Proton-Translocating ATPases, Enzyme, biology.protein, F1 ATPase, (Chloroplast)
Abstract

Exposure of chloroplast F1 ATPase to 2-azido-ATP results in the noncovalent tight binding of 2-azido-ATP or 2-azido-ADP to noncatalytic or to catalytic sites. Subsequent photolysis results in covalent labeling of adjacent tryptic peptides of the β-subunit. Binding at noncatalytic sites results in labeling of tyrosine 385 by an ATP or an ADP moiety. Binding at catalytic sites results in labeling of tyrosine 362 by only an ADP moiety. Similar labeling patterns are observed for the heat-activated or the membrane-bound enzymes.

Published
1987

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