Source:http://linkedlifedata.com/resource/pubmed/id/16668168
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
2010-6-29
|
| pubmed:abstractText |
Reversible seryl-phosphorylation contributes to the light/dark regulation of C(4)-leaf phosphoenolpyruvate carboxylase (PEPC) activity in vivo. The specific regulatory residue that, upon in vitro phosphorylation by a maize-leaf protein-serine kinase(s), leads to an increase in catalytic activity and a decrease in malate-sensitivity of the target enzyme has been recently identified as Ser-15 in (32)P-phosphorylated/activated dark-form maize PEPC (J-A Jiao, R Chollet [1990] Arch Biochem Biophys 283: 300-305). In order to ascertain whether this N-terminal seryl residue is, indeed, the in vivo regulatory phosphorylation site, [(32)P]phosphopeptides were isolated and purified from in vivo(32)P-labeled maize and sorghum leaf PEPC and subjected to automated Edman degradation analysis. The results show that purified light-form maize PEPC contains 14-fold more (32)P-radioactivity than the corresponding dark-form enzyme on an equal protein basis and, more notably, only a single N-terminal serine residue (Ser-15 in maize PEPC and its structural homolog, Ser-8, in the sorghum enzyme) was found to be (32)P-phosphorylated in the light or dark. These in vivo observations, combined with the results from our previous in vitro phosphorylation studies (J-A Jiao, R Chollet [1989] Arch Biochem Biophys 269: 526-535; [1990] Arch Biochem Biophys 283: 300-305), demonstrate that an N-terminal seryl residue in C(4) PEPC is, indeed, the regulatory site that undergoes light/dark changes in phosphorylation-status and, thus, plays a major, if not cardinal role in the light-induced changes in catalytic and regulatory properties of this cytoplasmic C(4)-photosynthesis enzyme in vivo.
|
| pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16668168-11607171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16668168-16664046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16668168-16665065,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16668168-16668131,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16668168-2148159,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16668168-2148863,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16668168-2268676,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16668168-2308851,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16668168-2493217,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16668168-3139092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16668168-3355158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16668168-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16668168-942051
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0032-0889
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
96
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
297-301
|
| pubmed:dateRevised |
2010-9-15
|
| pubmed:year |
1991
|
| pubmed:articleTitle |
In vivo regulatory phosphorylation site in c(4)-leaf phosphoenolpyruvate carboxylase from maize and sorghum.
|
| pubmed:affiliation |
Department of Biochemistry, University of Nebraska-Lincoln, East Campus, Lincoln, Nebraska 68583-0718.
|
| pubmed:publicationType |
Journal Article
|