scholarly journals ACETYL-COA CLEAVAGE AND SYNTHESIS IN METHANOGENS; CHARACTERIZATION OF SUBOMPONENT INTERACTIONS IN THE ACETYL-COA DECARBONYLASE/SYNTHASE MULTIENZYME COMPLEX

2013 ◽  
Author(s):  
DAVID A. GRAHAM
Keyword(s):  
Multienzyme Complex ◽  
Acetyl Coa

scholarly journals Isolation and characterization of the acetyl-CoA synthetase from Penicillium chrysogenum. Involvement of this enzyme in the biosynthesis of penicillins.

1992 ◽  
Vol 267 (8) ◽  
pp. 5474-5481
Author(s):  
H Martínez-Blanco ◽  
A Reglero ◽  
M Fernández-Valverde ◽  
M.A. Ferrero ◽  
M.A. Moreno ◽  
...  
Keyword(s):  
Penicillium Chrysogenum ◽  
Acetyl Coa ◽  
Isolation And Characterization

Characterization of the Acyl Substrate Binding Pocket of Acetyl-CoA Synthetase†

Biochemistry ◽  
2006 ◽  
Vol 45 (38) ◽  
pp. 11482-11490 ◽  
Author(s):  
Cheryl Ingram-Smith ◽  
Barrett I. Woods ◽  
Kerry S. Smith
Keyword(s):  
Substrate Binding ◽  
Binding Pocket ◽  
Substrate Binding Pocket ◽  
Acetyl Coa

Characterization of cross-resistance patterns in acetyl-CoA carboxylase inhibitor resistant wild oat (Avena fatua)

Weed Science ◽  
1997 ◽  
Vol 45 (6) ◽  
pp. 750-755 ◽  
Author(s):  
Luc Bourgeois ◽  
Norm C. Kenkel ◽  
Ian N. Morrison
Keyword(s):  
Cluster Analysis ◽  
Principal Component ◽  
Petri Dish ◽  
Cross Resistance ◽  
Wild Oat ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Pairwise Correlation ◽  
Resistance Patterns

The purpose of this study was to determine cross-resistance patterns among wild oat lines resistant to acetyl-CoA carboxylase (ACCase) inhibitors and to determine which, if any, cross-resistant type was more common than another. Discriminatory concentrations of two aryloxyphenoxy-propionates (APP) and three cyclohexanediones (CHD) were determined using a petri-dish bioassay. These concentrations were then applied to 82 resistant wild oat lines identified in previous studies. In addition, two resistant standards (UM1 and UM33) and a susceptible standard (UM5) were included in the experiments. Coleoptile lengths expressed as percentages of untreated controls were used to assess the level of resistance to each herbicide. Large variations were observed among wild oat lines and herbicides. However, cluster analysis summarized the relationship between the five herbicides (variables) and the wild oat lines into three main cross-resistance types. Type A included wild oat lines with high resistance to APP herbicides and no or low resistance to CHD herbicides. Types B and C included those with low to moderate resistant and high levels of resistance to all five herbicides, respectively. Type C was the most common cross-resistance type. Relationships among herbicides were determined using pairwise correlation and principal component analysis (PCA). All correlations were high between APP herbicides and between CHD herbicides but not between APP and CHD herbicides. The first two axes of the PCA accounted for 88.4% of the total variance, with the first axis correlated to the CHD herbicides and the second axis correlated to the APP herbicides. In the PCA, wild oat lines were segregated into the three types identified in the cluster analysis. Although CHD and APP herbicides bind at the same region on the ACCase, resistant wild oat lines respond differently to them.

scholarly journals A Pathway for Degradation of Uracil to Acetyl Coenzyme A in Bacillus megaterium

2020 ◽  
Vol 86 (7) ◽  
Author(s):  
Di Zhu ◽  
Yifeng Wei ◽  
Jinyu Yin ◽  
Dazhi Liu ◽  
Ee Lui Ang ◽  
...  
Keyword(s):  
Energy Source ◽  
Bacillus Megaterium ◽  
Coenzyme A ◽  
Catabolic Pathway ◽  
Acetyl Coa ◽  
Acetyl Coenzyme A ◽  
Content Type ◽  
Biochemical Pathways ◽  
Acetyl Coenzyme

ABSTRACT Bacteria utilize diverse biochemical pathways for the degradation of the pyrimidine ring. The function of the pathways studied to date has been the release of nitrogen for assimilation. The most widespread of these pathways is the reductive pyrimidine catabolic pathway, which converts uracil into ammonia, carbon dioxide, and β-alanine. Here, we report the characterization of a β-alanine:pyruvate aminotransferase (PydD2) and an NAD+-dependent malonic semialdehyde dehydrogenase (MSDH) from a reductive pyrimidine catabolism gene cluster in Bacillus megaterium. Together, these enzymes convert β-alanine into acetyl coenzyme A (acetyl-CoA), a key intermediate in carbon and energy metabolism. We demonstrate the growth of B. megaterium in defined medium with uracil as its sole carbon and energy source. Homologs of PydD2 and MSDH are found in association with reductive pyrimidine pathway genes in many Gram-positive bacteria in the order Bacillales. Our study provides a basis for further investigations of the utilization of pyrimidines as a carbon and energy source by bacteria. IMPORTANCE Pyrimidine has wide occurrence in natural environments, where bacteria use it as a nitrogen and carbon source for growth. Detailed biochemical pathways have been investigated with focus mainly on nitrogen assimilation in the past decades. Here, we report the discovery and characterization of two important enzymes, PydD2 and MSDH, which constitute an extension for the reductive pyrimidine catabolic pathway. These two enzymes, prevalent in Bacillales based on our bioinformatics studies, allow stepwise conversion of β-alanine, a previous “end product” of the reductive pyrimidine degradation pathway, to acetyl-CoA as carbon and energy source.

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