How pantothenol intervenes in Coenzyme-A biosynthesis of Mycobacterium tuberculosis

2007 ◽  
Vol 361 (4) ◽  
pp. 903-909 ◽  
Author(s):  
Parimal Kumar ◽  
Manmohan Chhibber ◽  
Avadhesha Surolia
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Coenzyme A ◽  
Coenzyme A Biosynthesis

A detailed biochemical characterization of phosphopantothenate synthetase, a novel enzyme involved in coenzyme A biosynthesis in the Archaea

Extremophiles ◽  
2012 ◽  
Vol 16 (6) ◽  
pp. 819-828 ◽  
Author(s):  
Takuya Ishibashi ◽  
Hiroya Tomita ◽  
Yuusuke Yokooji ◽  
Tatsuya Morikita ◽  
Bunta Watanabe ◽  
...  
Keyword(s):  
Coenzyme A ◽  
Biochemical Characterization ◽  
Coenzyme A Biosynthesis

Some Aspects of the Enzyme Activities Involved in Coenzyme A Biosynthesis in Various Microorganisms

1974 ◽  
Vol 38 (5) ◽  
pp. 1015-1021 ◽  
Author(s):  
Sakayu Shimizu ◽  
Katsuro Kubo ◽  
Hazime Morioka ◽  
Yoshiki Tani ◽  
Koichi Ogata
Keyword(s):  
Enzyme Activities ◽  
Coenzyme A ◽  
Coenzyme A Biosynthesis

scholarly journals Characterization of Benzoyl Coenzyme A Biosynthesis Genes in the Enterocin-Producing Bacterium “Streptomyces maritimus”

2003 ◽  
Vol 185 (2) ◽  
pp. 399-404 ◽  
Author(s):  
Longkuan Xiang ◽  
Bradley S. Moore
Keyword(s):  
Benzoic Acid ◽  
Phenylalanine Ammonia Lyase ◽  
Coenzyme A ◽  
Primary Metabolism ◽  
The Novel ◽  
Wild Type ◽  
Coa Ligase ◽  
Encoding Gene ◽  
Coenzyme A Biosynthesis

ABSTRACT The novel benzoyl coenzyme A (benzoyl-CoA) biosynthesis pathway in “Streptomyces maritimus” was investigated through a series of target-directed mutations. Genes involved in benzoyl-CoA formation were disrupted through single-crossover homologous recombination, and the resulting mutants were analyzed for their ability to biosynthesize the benzoyl-CoA-primed polyketide antibiotic enterocin. Inactivation of the unique phenylalanine ammonia-lyase-encoding gene encP was previously shown to be absolutely required for benzoyl-CoA formation in “S. maritimus”. The fatty acid β-oxidation-related genes encH, -I, and -J, on the other hand, are necessary but not required. In each case, the yield of benzoyl-CoA-primed enterocin dropped below wild-type levels. We attribute the reduced benzoyl-CoA formation in these specific mutants to functional substitution and cross-talk between the products of genes encH, -I, and -J and the enzyme homologues of primary metabolism. Disruption of the benzoate-CoA ligase encN gene did not perturb enterocin production, however, demonstrating that encN is extraneous and that benzoic acid is not a pathway intermediate. EncN rather serves as a substitute pathway for utilizing exogenous benzoic acid. These experiments provide further support that benzoyl-CoA is formed in a novel bacterial pathway that resembles the eukaryotic assembly of benzoyl-CoA from phenylalanine via a β-oxidative path.

scholarly journals Pyrazinoic Acid Inhibits Mycobacterial Coenzyme A Biosynthesis by Binding to Aspartate Decarboxylase PanD

2017 ◽  
Vol 3 (11) ◽  
pp. 807-819 ◽  
Author(s):  
Pooja Gopal ◽  
Wilson Nartey ◽  
Priya Ragunathan ◽  
Jansy Sarathy ◽  
Firat Kaya ◽  
...  
Keyword(s):  
Coenzyme A ◽  
Coenzyme A Biosynthesis ◽  
Pyrazinoic Acid

scholarly journals Biochemical Characterization of Pantoate Kinase, a Novel Enzyme Necessary for Coenzyme A Biosynthesis in the Archaea

2012 ◽  
Vol 194 (19) ◽  
pp. 5434-5443 ◽  
Author(s):  
H. Tomita ◽  
Y. Yokooji ◽  
T. Ishibashi ◽  
T. Imanaka ◽  
H. Atomi
Keyword(s):  
Coenzyme A ◽  
Biochemical Characterization ◽  
Coenzyme A Biosynthesis ◽  
Kinase A

Plant coenzyme A biosynthesis: characterization of two pantothenate kinases from Arabidopsis

2006 ◽  
Vol 61 (4-5) ◽  
pp. 629-642 ◽  
Author(s):  
G. B. Tilton ◽  
W. J. Wedemeyer ◽  
J. Browse ◽  
J. Ohlrogge
Keyword(s):  
Coenzyme A ◽  
Coenzyme A Biosynthesis
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