Kinetic characterization of the [3'-32P]coenzyme A/acetyl coenzyme A exchange catalyzed by a three-subunit form of the carbon monoxide dehydrogenase/acetyl-CoA synthase from Clostridium thermoaceticum

Biochemistry ◽  
1989 ◽  
Vol 28 (11) ◽  
pp. 4675-4680 ◽  
Author(s):  
Shawn E. Ramer ◽  
Scott A. Raybuck ◽  
William H. Orme-Johnson ◽  
Christopher T. Walsh
Keyword(s):  
Carbon Monoxide ◽  
Coenzyme A ◽  
Carbon Monoxide Dehydrogenase ◽  
Kinetic Characterization ◽  
Clostridium Thermoaceticum ◽  
Acetyl Coa ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme

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.

scholarly journals Nickel-Dependent Oligomerization of the Alpha Subunit of Acetyl-Coenzyme A Synthase/Carbon Monoxide Dehydrogenase†

Biochemistry ◽  
2007 ◽  
Vol 46 (41) ◽  
pp. 11606-11613 ◽  
Author(s):  
Xiangshi Tan ◽  
Ioannis Kagiampakis ◽  
Ivan V. Surovtsev ◽  
Borries Demeler ◽  
Paul A. Lindahl
Keyword(s):  
Carbon Monoxide ◽  
Coenzyme A ◽  
Carbon Monoxide Dehydrogenase ◽  
Alpha Subunit ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Acetyl Coenzyme A Synthase

Paramagnetic centers and acetyl-coenzyme A/CO exchange activity of carbon monoxide dehydrogenase from Methanothrix soehngenii

1991 ◽  
Vol 195 (2) ◽  
pp. 385-391 ◽  
Author(s):  
Mike S. M. JETTEN ◽  
Wilfred R. HAGEN ◽  
Antonio J. PIERIK ◽  
Alfons J. M. STAMS ◽  
Alexander J. B. ZEHNDER
Keyword(s):  
Carbon Monoxide ◽  
Coenzyme A ◽  
Carbon Monoxide Dehydrogenase ◽  
Paramagnetic Centers ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
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