The 1.75 Å Crystal Structure of Acetyl-CoA Synthetase Bound to Adenosine-5‘-propylphosphate and Coenzyme A†

Biochemistry ◽  
2003 ◽  
Vol 42 (10) ◽  
pp. 2866-2873 ◽  
Author(s):  
Andrew M. Gulick ◽  
Vincent J. Starai ◽  
Alexander R. Horswill ◽  
Kristen M. Homick ◽  
Jorge C. Escalante-Semerena
Keyword(s):  
Crystal Structure ◽  
Coenzyme A ◽  
Acetyl Coa

scholarly journals Crystal Structure of TDP-Fucosamine Acetyltransferase (WecD) from Escherichia coli, an Enzyme Required for Enterobacterial Common Antigen Synthesis

2006 ◽  
Vol 188 (15) ◽  
pp. 5606-5617 ◽  
Author(s):  
Ming-Ni Hung ◽  
Erumbi Rangarajan ◽  
Christine Munger ◽  
Guy Nadeau ◽  
Traian Sulea ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Escherichia Coli ◽  
Coenzyme A ◽  
Structural Data ◽  
Enteric Bacteria ◽  
Common Antigen ◽  
Acetyl Coa ◽  
Enterobacterial Common Antigen ◽  
Thiolate Anion ◽  
Acetyl Transfer

ABSTRACT Enterobacterial common antigen (ECA) is a polysaccharide found on the outer membrane of virtually all gram-negative enteric bacteria and consists of three sugars, N-acetyl-d-glucosamine, N-acetyl-d-mannosaminuronic acid, and 4-acetamido-4,6-dideoxy-d-galactose, organized into trisaccharide repeating units having the sequence →3)-α-d-Fuc4NAc-(1→4)-β-d-ManNAcA-(1→4)-α-d-GlcNAc-(1→. While the precise function of ECA is unknown, it has been linked to the resistance of Shiga-toxin-producing Escherichia coli (STEC) O157:H7 to organic acids and the resistance of Salmonella enterica to bile salts. The final step in the synthesis of 4-acetamido-4,6-dideoxy-d-galactose, the acetyl-coenzyme A (CoA)-dependent acetylation of the 4-amino group, is carried out by TDP-fucosamine acetyltransferase (WecD). We have determined the crystal structure of WecD in apo form at a 1.95-Å resolution and bound to acetyl-CoA at a 1.66-Å resolution. WecD is a dimeric enzyme, with each monomer adopting the GNAT N-acetyltransferase fold, common to a number of enzymes involved in acetylation of histones, aminoglycoside antibiotics, serotonin, and sugars. The crystal structure of WecD, however, represents the first structure of a GNAT family member that acts on nucleotide sugars. Based on this cocrystal structure, we have used flexible docking to generate a WecD-bound model of the acetyl-CoA-TDP-fucosamine tetrahedral intermediate, representing the structure during acetyl transfer. Our structural data show that WecD does not possess a residue that directly functions as a catalytic base, although Tyr208 is well positioned to function as a general acid by protonating the thiolate anion of coenzyme A.

scholarly journals X-ray crystal structure of a malonate-semialdehyde dehydrogenase fromPseudomonassp. strain AAC

2017 ◽  
Vol 73 (1) ◽  
pp. 24-28 ◽  
Author(s):  
Matthew Wilding ◽  
Colin Scott ◽  
Thomas S. Peat ◽  
Janet Newman
Keyword(s):  
Crystal Structure ◽  
Search Model ◽  
Molecular Replacement ◽  
X Rays ◽  
X Ray Diffraction ◽  
Acetyl Coa ◽  
Space Group ◽  
X Ray ◽  
Semialdehyde Dehydrogenase

The NAD-dependent malonate-semialdehyde dehydrogenase KES23460 fromPseudomonassp. strain AAC makes up half of a bicistronic operon responsible for β-alanine catabolism to produce acetyl-CoA. The KES23460 protein has been heterologously expressed, purified and used to generate crystals suitable for X-ray diffraction studies. The crystals belonged to space groupP212121and diffracted X-rays to beyond 3 Å resolution using the microfocus beamline of the Australian Synchrotron. The structure was solved using molecular replacement, with a monomer from PDB entry 4zz7 as the search model.

scholarly journals Genome Sequence of Serratia marcescens MSU97, a Plant-Associated Bacterium That Makes Multiple Antibiotics

2017 ◽  
Vol 5 (9) ◽  
Author(s):  
Miguel A. Matilla ◽  
Zulema Udaondo ◽  
Tino Krell ◽  
George P. C. Salmond
Keyword(s):  
Serratia Marcescens ◽  
Genome Sequence ◽  
Coenzyme A ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Acetyl Coenzyme A ◽  
Content Type ◽  
Acetyl Coenzyme ◽  
Multiple Antibiotics

ABSTRACT Serratia marcescens MSU97 was isolated from the Guayana region of Venezuela due to its ability to suppress plant-pathogenic oomycetes. Here, we report the genome sequence of MSU97, which produces various antibiotics, including the bacterial acetyl-coenzyme A (acetyl-CoA) carboxylase inhibitor andrimid, the chlorinated macrolide oocydin A, and the red linear tripyrrole antibiotic prodigiosin.

Determination of coenzyme A and acetyl CoA in tissue extracts

1969 ◽  
Vol 29 (2) ◽  
pp. 293-299 ◽  
Author(s):  
John B. Allred ◽  
David G. Guy
Keyword(s):  
Coenzyme A ◽  
Acetyl Coa ◽  
Tissue Extracts

scholarly journals Crystal structure of the β-subunit of acetyl-CoA carboxylase inC. glutamicum

2005 ◽  
Vol 61 (a1) ◽  
pp. c189-c189
Author(s):  
R. Natsume ◽  
M. Yamada ◽  
M. Senda ◽  
T. Nakamatsu ◽  
S. Horinouchi ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Β Subunit ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa

scholarly journals The Apparent Malate Synthase Activity of Rhodobacter sphaeroides Is Due to Two Paralogous Enzymes, (3S)-Malyl-Coenzyme A (CoA)/β-Methylmalyl-CoA Lyase and (3S)- Malyl-CoA Thioesterase

2010 ◽  
Vol 192 (5) ◽  
pp. 1249-1258 ◽  
Author(s):  
Tobias J. Erb ◽  
Lena Frerichs-Revermann ◽  
Georg Fuchs ◽  
Birgit E. Alber
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Coenzyme A ◽  
Glyoxylate Cycle ◽  
Condensation Reaction ◽  
Malate Synthase ◽  
Acetyl Coa ◽  
Acetyl Coenzyme A ◽  
Claisen Condensation ◽  
Enzyme Functions ◽  
The Glyoxylate Cycle

ABSTRACT Assimilation of acetyl coenzyme A (acetyl-CoA) is an essential process in many bacteria that proceeds via the glyoxylate cycle or the ethylmalonyl-CoA pathway. In both assimilation strategies, one of the final products is malate that is formed by the condensation of acetyl-CoA with glyoxylate. In the glyoxylate cycle this reaction is catalyzed by malate synthase, whereas in the ethylmalonyl-CoA pathway the reaction is separated into two proteins: malyl-CoA lyase, a well-known enzyme catalyzing the Claisen condensation of acetyl-CoA with glyoxylate and yielding malyl-CoA, and an unidentified malyl-CoA thioesterase that hydrolyzes malyl-CoA into malate and CoA. In this study the roles of Mcl1 and Mcl2, two malyl-CoA lyase homologs in Rhodobacter sphaeroides, were investigated by gene inactivation and biochemical studies. Mcl1 is a true (3S)-malyl-CoA lyase operating in the ethylmalonyl-CoA pathway. Notably, Mcl1 is a promiscuous enzyme and catalyzes not only the condensation of acetyl-CoA and glyoxylate but also the cleavage of β-methylmalyl-CoA into glyoxylate and propionyl-CoA during acetyl-CoA assimilation. In contrast, Mcl2 was shown to be the sought (3S)-malyl-CoA thioesterase in the ethylmalonyl-CoA pathway, which specifically hydrolyzes (3S)-malyl-CoA but does not use β-methylmalyl-CoA or catalyze a lyase or condensation reaction. The identification of Mcl2 as thioesterase extends the enzyme functions of malyl-CoA lyase homologs that have been known only as “Claisen condensation” enzymes so far. Mcl1 and Mcl2 are both related to malate synthase, an enzyme which catalyzes both a Claisen condensation and thioester hydrolysis reaction.

Crystal Structure of Dephospho-Coenzyme A Kinase from Haemophilus influenzae

2001 ◽  
Vol 136 (2) ◽  
pp. 119-125 ◽  
Author(s):  
Galina Obmolova ◽  
Alexey Teplyakov ◽  
Nicklas Bonander ◽  
Edward Eisenstein ◽  
Andrew J Howard ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Haemophilus Influenzae ◽  
Coenzyme A

Transcriptional regulation of acetyl coenzyme A carboxylase gene expression by tumor necrosis factor in 30A-5 preadipocytes

1989 ◽  
Vol 9 (3) ◽  
pp. 974-982
Author(s):  
M E Pape ◽  
K H Kim
Keyword(s):  
Tumor Necrosis Factor ◽  
Rna Polymerase ◽  
Tumor Necrosis ◽  
Transcriptional Control ◽  
Coenzyme A ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Mrna Accumulation ◽  
Acetyl Coenzyme A ◽  
Necrosis Factor

Acetyl coenzyme A (acetyl-CoA) carboxylase activity, amount, and mRNA levels increase during the differentiation of 30A-5 preadipocytes to adipocytes. Tumor necrosis factor (TNF) completely prevents this differentiation, with concomitant inhibition of acetyl-CoA carboxylase mRNA accumulation. To investigate the mechanisms by which TNF prevents acetyl-CoA carboxylase mRNA accumulation, we determined the effect of TNF on the transcription rate of the carboxylase gene and the half-life of carboxylase mRNA. Nuclear runoff transcription assays revealed no differences in the number of RNA polymerase molecules actively engaged in transcription of the acetyl-CoA carboxylase gene in preadipocytes, adipocytes, TNF-treated preadipocytes, or at any time during the course of differentiation. However, changes in adipsin, glycerophosphate dehydrogenase, and actin mRNAs, whose levels are also differentiation dependent, can be accounted for in part by changes in the number of polymerase complexes on their respective genes. To determine whether TNF caused a decrease in the stability of carboxylase RNA transcripts, we measured the rate of decay of prelabeled acetyl-CoA carboxylase mRNA. Control and TNF-treated cells showed no difference between the apparent half-lives of acetyl-CoA carboxylase mRNAs (9 h). However, the rate of acetyl-CoA carboxylase mRNA synthesis in vivo was decreased three- to fourfold in the presence of TNF. These data demonstrate that TNF prevents accumulation of acetyl-CoA carboxylase mRNA during preadipocyte differentiation by decreasing the rate of acetyl-CoA carboxylase gene transcription. However, transcriptional control is not due to a change in the number of RNA polymerase complexes actively engaged in carboxylase transcript elongation which could be measured by a number runoff assay. Instead, transcriptional control may be related to the rate at which RNA polymerase traverses the acetyl-CoA carboxylase gene.

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