The role of adenosine triphosphate citrate lyase in the metabolism of acetyl coenzyme a and function of blood platelets in diabetes mellitus

Metabolism ◽  
2004 ◽  
Vol 53 (1) ◽  
pp. 66-72 ◽  
Author(s):  
Anna Michno ◽  
Anna Skibowska ◽  
Anna Raszeja-Specht ◽  
Justyna Ćwikowska ◽  
Andrzej Szutowicz
Keyword(s):  
Diabetes Mellitus ◽  
Adenosine Triphosphate ◽  
Coenzyme A ◽  
Blood Platelets ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Citrate Lyase ◽  
And Function

scholarly journals An essential role of acetyl coenzyme A in the catalytic cycle of insect arylalkylamine N-acetyltransferase

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Chu-Ya Wu ◽  
I-Chen Hu ◽  
Yi-Chen Yang ◽  
Wei-Cheng Ding ◽  
Chih-Hsuan Lai ◽  
...  
Keyword(s):  
Essential Role ◽  
Coenzyme A ◽  
Catalytic Cycle ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme

scholarly journals Biochemical and Mutational Analyses of AcuA, the Acetyltransferase Enzyme That Controls the Activity of the Acetyl Coenzyme A Synthetase (AcsA) in Bacillus subtilis

2008 ◽  
Vol 190 (14) ◽  
pp. 5132-5136 ◽  
Author(s):  
Jeffrey G. Gardner ◽  
Jorge C. Escalante-Semerena
Keyword(s):  
Bacillus Subtilis ◽  
Coenzyme A ◽  
Effective Means ◽  
Wild Type ◽  
Modification System ◽  
Vitro Assay ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme

ABSTRACT The acuABC genes of Bacillus subtilis comprise a putative posttranslational modification system. The AcuA protein is a member of the Gcn5-related N-acetyltransferase (GNAT) superfamily, the AcuC protein is a class I histone deacetylase, and the role of the AcuB protein is not known. AcuA controls the activity of acetyl coenzyme A synthetase (AcsA; EC 6.2.1.1) in this bacterium by acetylating residue Lys549. Here we report the kinetic analysis of wild-type and variant AcuA proteins. We contrived a genetic scheme for the identification of AcuA residues critical for activity. Changes at residues H177 and G187 completely inactivated AcuA and led to its rapid turnover. Changes at residues R42 and T169 were less severe. In vitro assay conditions were optimized, and an effective means of inactivating the enzyme was found. The basic kinetic parameters of wild-type and variant AcuA proteins were obtained and compared to those of eukaryotic GNATs. Insights into how the isolated mutations may exert their deleterious effect were investigated by using the crystal structure of an AcuA homolog.

scholarly journals Molecular Characterization of a Heteromeric ATP-Citrate Lyase That Generates Cytosolic Acetyl-Coenzyme A in Arabidopsis

2002 ◽  
Vol 130 (2) ◽  
pp. 740-756 ◽  
Author(s):  
Beth L. Fatland ◽  
Jinshan Ke ◽  
Marc D. Anderson ◽  
Wieslawa I. Mentzen ◽  
Li Wei Cui ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Coenzyme A ◽  
Atp Citrate Lyase ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Citrate Lyase

scholarly journals The Role of Pyruvate Dehydrogenase and Acetyl-Coenzyme A Synthetase in Fatty Acid Synthesis in Developing Arabidopsis Seeds

2000 ◽  
Vol 123 (2) ◽  
pp. 497-508 ◽  
Author(s):  
Jinshan Ke ◽  
Robert H. Behal ◽  
Stephanie L. Back ◽  
Basil J. Nikolau ◽  
Eve Syrkin Wurtele ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Pyruvate Dehydrogenase ◽  
Coenzyme A ◽  
Acid Synthesis ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme

Role of acetyl-coenzyme A synthetase in leaves of Arabidopsis thaliana

2002 ◽  
Vol 402 (2) ◽  
pp. 259-267 ◽  
Author(s):  
Robert H Behal ◽  
Ming Lin ◽  
Stephanie Back ◽  
David J Oliver
Keyword(s):  
Arabidopsis Thaliana ◽  
Coenzyme A ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme

Lack of Citrate Lyase — the Key Enzyme of the Reductive Carboxylic Acid Cycle — in Chlorobium thiosulfatophilum and Rhodospirillum rubrum

1972 ◽  
Vol 27 (8) ◽  
pp. 967-973 ◽  
Author(s):  
Norbert Beuscher ◽  
Gerhard Gottschalk
Keyword(s):  
Carboxylic Acid ◽  
Rhodospirillum Rubrum ◽  
Coenzyme A ◽  
Reaction Sequence ◽  
Acetyl Coenzyme A ◽  
Acid Cycle ◽  
Acetyl Coenzyme ◽  
Citrate Lyase ◽  
Chlorobium Thiosulfatophilum ◽  
Key Enzyme

Extracts of Chlorobium thiosulfatophilum and of Rhodospirillum rubrum have been tested for the presence of citrate lyase under various conditions. This enzyme could not be detected. It is, therefore, concluded that a complete reductive carboxylic acid cycle does not occur in these microorganisms.The enzymes required for a-ketoglutarate synthesis from oxaloaetate and acetyl-coenzyme A are present in autotrophically grown cells of C. thiosulfatophilum and R. rubrum. This supports the view that a reaction sequence catalyzing the conversion of α-ketoglutarate into oxaloacetate is unlikely to exist in these bacteria.

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