Insights into the Mechanistic Role of the [Fe4S4] Cubane in the A-Cluster {[Fe4S4]-(SR)-[NipNid]} of Acetyl-Coenzyme A Synthase

ChemBioChem ◽  
2011 ◽  
Vol 12 (9) ◽  
pp. 1417-1421 ◽  
Author(s):  
Yi Liu ◽  
Feng Wang ◽  
Pingwei Li ◽  
Xiangshi Tan
Keyword(s):  
Coenzyme A ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Acetyl Coenzyme A Synthase

Structures and Energetics of Models for the Active Site of Acetyl-Coenzyme A Synthase:  Role of Distal and Proximal Metals in Catalysis

2004 ◽  
Vol 126 (11) ◽  
pp. 3410-3411 ◽  
Author(s):  
Charles Edwin Webster ◽  
Marcetta Y. Darensbourg ◽  
Paul A. Lindahl ◽  
Michael B. Hall
Keyword(s):  
Active Site ◽  
Coenzyme A ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Acetyl Coenzyme A Synthase

Probing the role of the bridging C509 between the [Fe4S4] cubane and the [NipNid] centre in the A-cluster of acetyl-coenzyme A synthase

2011 ◽  
Vol 47 (4) ◽  
pp. 1291-1293 ◽  
Author(s):  
Yi Liu ◽  
Xiaofei Zhu ◽  
Feng Wang ◽  
Tianlei Ying ◽  
Pingwei Li ◽  
...  
Keyword(s):  
Coenzyme A ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Acetyl Coenzyme A Synthase

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

Thiolate-Bridged Nickel−Copper Complexes:  A Binuclear Model for the Catalytic Site of Acetyl Coenzyme A Synthase?

2003 ◽  
Vol 125 (15) ◽  
pp. 4422-4423 ◽  
Author(s):  
Rangan Krishnan ◽  
Janis K. Voo ◽  
Charles G. Riordan ◽  
Lev Zahkarov ◽  
Arnold L. Rheingold
Keyword(s):  
Copper Complexes ◽  
Coenzyme A ◽  
Catalytic Site ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Nickel Copper ◽  
Acetyl Coenzyme A Synthase

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 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.

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