Involvement of arginine residues in the allosteric activation and inhibition ofSynechocystis PCC 6803 ADPglucose pyrophosphorylase

Alberto A. Iglesias; Genichi Kakefuda; Jack Preiss

doi:10.1007/bf01025217

Involvement of arginine residues in the allosteric activation and inhibition ofSynechocystis PCC 6803 ADPglucose pyrophosphorylase

Journal of Protein Chemistry ◽

10.1007/bf01025217 ◽

1992 ◽

Vol 11 (2) ◽

pp. 119-128 ◽

Cited By ~ 13

Author(s):

Alberto A. Iglesias ◽

Genichi Kakefuda ◽

Jack Preiss

Keyword(s):

Allosteric Activation ◽

Adpglucose Pyrophosphorylase ◽

Arginine Residues ◽

Pcc 6803

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Involvement of arginine residues in the allosteric activation of Escherichia coli ADP-glucose synthetase

Biochemistry ◽

10.1021/bi00537a036 ◽

1982 ◽

Vol 21 (8) ◽

pp. 1929-1934 ◽

Cited By ~ 13

Author(s):

Curtis A. Carlson ◽

Jack Preiss

Keyword(s):

Escherichia Coli ◽

Allosteric Activation ◽

Arginine Residues

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Mechanism of allosteric activation of glycogen phosphorylase probed by the reactivity of essential arginine residues. Identification of an arginine residue involved in the binding of glucose 1-phosphate

Biochemistry ◽

10.1021/bi00511a044 ◽

1981 ◽

Vol 20 (8) ◽

pp. 2354-2360 ◽

Cited By ~ 11

Author(s):

Bernard Vandenbunder ◽

Marc Dreyfus ◽

Olivier Bertrand ◽

May J. Dognin ◽

Lise Sibilli ◽

...

Keyword(s):

Glycogen Phosphorylase ◽

Arginine Residue ◽

Allosteric Activation ◽

Arginine Residues

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Arginine residues in the D2 polypeptide may stabilize bicarbonate binding in photosystem II of Synechocystis sp. PCC 6803

Biochimica et Biophysica Acta (BBA) - Bioenergetics ◽

10.1016/s0005-2728(05)80202-6 ◽

1991 ◽

Vol 1059 (2) ◽

pp. 171-180 ◽

Cited By ~ 34

Author(s):

Jiancheng Cao ◽

W.F.J. Vermaas ◽

Govindjee

Keyword(s):

Photosystem Ii ◽

Arginine Residues ◽

Synechocystis Sp ◽

Pcc 6803

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Contributions of the substrate-binding arginine residues to maleate-induced closure of the active site of Escherichia coli aspartate aminotransferase

European Journal of Biochemistry ◽

10.1046/j.1432-1033.2001.02035.x ◽

2001 ◽

Vol 268 (6) ◽

pp. 1640-1645

Author(s):

Annelise Matharu ◽

Hideyuki Hayashi ◽

Hiroyuki Kagamiyama ◽

Bruno Maras ◽

Robert A. John

Keyword(s):

Escherichia Coli ◽

Active Site ◽

Aspartate Aminotransferase ◽

Substrate Binding ◽

Arginine Residues

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Ga-68 labeling of stable neurotensin(8-13) analogs via carbamoylated arginine residues gives NTS 1 R PET ligands with promising in vitro profile

10.1055/s-0040-1708265 ◽

2020 ◽

Author(s):

L Schindler ◽

J Moosbauer ◽

G Bernhardt ◽

D Hellwig ◽

M Keller

Keyword(s):

Arginine Residues

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A study of the impact of mazie SBE I on the [alpha]-polyglucan produced in Synechocystis sp. strain PCC 6803

10.31274/rtd-180813-17053 ◽

2007 ◽

Author(s):

Shayani Deborah Nesaranjani Pieris

Keyword(s):

The Impact ◽

Synechocystis Sp ◽

Pcc 6803

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Faculty Opinions recommendation of Sugar-induced increases in trehalose 6-phosphate are correlated with redox activation of ADPglucose pyrophosphorylase and higher rates of starch synthesis in Arabidopsis thaliana.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1031821.368953 ◽

2006 ◽

Author(s):

Sjef Smeekens

Keyword(s):

Arabidopsis Thaliana ◽

Starch Synthesis ◽

Adpglucose Pyrophosphorylase ◽

Redox Activation

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Faculty Opinions recommendation of ChlH, the H subunit of the Mg-chelatase, is an anti-sigma factor for SigE in Synechocystis sp. PCC 6803.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1160026.620293 ◽

2009 ◽

Author(s):

Keith Chater

Keyword(s):

Sigma Factor ◽

Mg Chelatase ◽

Synechocystis Sp ◽

Pcc 6803

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Faculty Opinions recommendation of Regulation of clathrin-mediated endocytosis by hierarchical allosteric activation of AP2.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.727137601.793529064 ◽

2017 ◽

Author(s):

Margaret S Robinson

Keyword(s):

Allosteric Activation

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Faculty Opinions recommendation of The cyanobacterial homologue of HCF136/YCF48 is a component of an early photosystem II assembly complex and is important for both the efficient assembly and repair of photosystem II in Synechocystis sp. PCC 6803.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.7466956.7759054 ◽

2011 ◽

Author(s):

Dario Leister

Keyword(s):

Photosystem Ii ◽

Synechocystis Sp ◽

Pcc 6803

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