منابع مشابه
Isolation and Distribution of Phosphoglycolate Phosphatase.
A phosphatase specific for P-glycolate5 was purified from extracts of tobacco leaves until no other phosphatase activity could be demonstrated in the preparation (10). Other plants have now been examined for the presence of this phosphatase. A new isolation procedure for the enzyme was developed because the (NH4) 2SO4 fractionation procedure, which was used with tobacco leaf extracts, inactivat...
متن کاملIdentification of the photorespiratory 2-phosphoglycolate phosphatase, PGLP1, in Arabidopsis.
The chloroplastidal enzyme 2-phosphoglycolate phosphatase (PGLP), PGLP1, catalyzes the first reaction of the photorespiratory C(2) cycle, a major pathway of plant primary metabolism. Thirteen potential PGLP genes are annotated in the Arabidopsis (Arabidopsis thaliana) genome; however, none of these genes has been functionally characterized, and the gene encoding the photorespiratory PGLP is not...
متن کاملProperties of Phosphoglycolate Phosphatase from Chlamydomonas reinhardtii and Anacystis nidulans.
The levels of activity of 2-phosphoglycolate phosphatase in the green algae, Chlamydomonas reinhardtii and Chlorella vulgaris, were in the range of 37 to 60 micromoles per milligram chlorophyll per hour and in the blue-green algae, Anacystis nidulans and Anabaena variabilis were 204 to 310 micromoles per milligram chlorophyll per hour. The activity in each species was similar regardless of whet...
متن کاملThe phosphoglycolate phosphatase gene and the mutation in the phosphoglycolate phosphatase-deficient mutant (<i>pgp1-1</i>) of <i>Chlamydomonas reinhardtii</i>
The sequences of the phosphoglycolate phosphatase (PGPase) gene Pgp1 and the 5′-upstream region from Chlamydomonas reinhardtii wildtype 2137 and the pgp1-1 mutant N142 that lacks the activity of PGPase (PGP1) were determined. The comparison revealed the alteration of a G to A at position 98 relative to the start codon. This destroyed the “GT” splice donor site at the beginning of the first intr...
متن کاملIdentification of TP53-induced glycolysis and apoptosis regulator (TIGAR) as the phosphoglycolate-independent 2,3-bisphosphoglycerate phosphatase.
The p53-induced protein TIGAR [TP53 (tumour protein 53)-induced glycolysis and apoptosis regulator] is considered to be a F26BPase (fructose-2,6-bisphosphatase) with an important role in cancer cell metabolism. The reported catalytic efficiency of TIGAR as an F26BPase is several orders of magnitude lower than that of the F26BPase component of liver or muscle PFK2 (phosphofructokinase 2), sugges...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1978
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)62322-7