Human Cytoplasmic 3-Hydroxy-3-methylglutaryl Coenzyme A Synthase: Expression, Purification, and Characterization of Recombinant Wild-Type and Cys129 Mutant Enzymes

1994 ◽  
Vol 312 (1) ◽  
pp. 1-13 ◽  
Author(s):  
L.L. Rokosz ◽  
D.A. Boulton ◽  
E.A. Butkiewicz ◽  
G. Sanyal ◽  
M.A. Cueto ◽  
...  
Keyword(s):  
Coenzyme A ◽  
Wild Type ◽  
Purification And Characterization

scholarly journals Purification and Characterization of Wild-type and Mutant “Classical” Nitroreductases ofSalmonella typhimurium

1998 ◽  
Vol 273 (37) ◽  
pp. 23922-23928 ◽  
Author(s):  
Masahiko Watanabe ◽  
Tatsuya Nishino ◽  
Koji Takio ◽  
Toshio Sofuni ◽  
Takehiko Nohmi
Keyword(s):  
Wild Type ◽  
Purification And Characterization

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 Purification and characterization of a novel enoyl coenzyme A reductase from Streptomyces collinus.

1992 ◽  
Vol 174 (12) ◽  
pp. 3850-3854 ◽  
Author(s):  
K A Reynolds ◽  
P Wang ◽  
K M Fox ◽  
M K Speedie ◽  
Y Lam ◽  
...  
Keyword(s):  
Coenzyme A ◽  
Purification And Characterization ◽  
Streptomyces Collinus ◽  
Coenzyme A Reductase

scholarly journals Purification and characterization of acyl coenzyme A: alcohol acyltransferase of Neurospora sp.

1989 ◽  
Vol 53 (6) ◽  
pp. 1551-1556 ◽  
Author(s):  
Hiromasa YAMAUCHI ◽  
Tetsuo HASUO ◽  
Teruo AMACHI ◽  
Osamu AKITA ◽  
Shodo HARA ◽  
...  
Keyword(s):  
Coenzyme A ◽  
Purification And Characterization ◽  
Alcohol Acyltransferase ◽  
Acyl Coenzyme A
Sign in / Sign up

Export Citation Format

Share Document