Development of a new transformant selection system for Penicillium chrysogenum: isolation and characterization of the P. chrysogenum acetyl-coenzyme A synthetase gene (facA) and its use as a homologous selection marker

1993 ◽  
Vol 38 (4) ◽  
pp. 514-519 ◽  
Author(s):  
Robin J. Gouka ◽  
Wim van Hartingsveldt ◽  
Roel A. L. Bovenberg ◽  
Cora M. J. van Zeijl ◽  
Cees A. M. J. J. van den Hondel ◽  
...  
Keyword(s):  
Penicillium Chrysogenum ◽  
Coenzyme A ◽  
Selection Marker ◽  
Selection System ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Isolation And Characterization

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 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

Characterization of mutants of the yeastYarrowia lipolytica defective in acetyl-coenzyme a synthetase

Yeast ◽  
1992 ◽  
Vol 8 (3) ◽  
pp. 193-203 ◽  
Author(s):  
Marian Kujau ◽  
Herbert Weber ◽  
Gerold Barth
Keyword(s):  
Coenzyme A ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme
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