This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Anderson, D H Articles by Rodwell, V W Search for Related Content PubMed PubMed Citation Articles by Anderson, D H Articles by Rodwell, V W

research-article

Nucleotide sequence and expression in Escherichia coli of the 3-hydroxy-3-methylglutaryl coenzyme A lyase gene of Pseudomonas mevalonii.

Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907.

ABSTRACT

The mva operon of Pseudomonas mevalonii encodes two enzymes that can convert internalized mevalonate into acetoacetate and acetyl-coenzyme A (CoA). The promoter-proximal gene of this operon is mvaA, the structural gene for 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase (EC 1.1.1.88). The cloning, characterization, and expression of mvaA has been reported (M. J. Beach and V. W. Rodwell, J. Bacteriol. 171:2994-3001, 1989). We report here the nucleotide sequence of another gene of this operon, mvaB, its expression in Escherichia coli, and its identification as the structural gene for HMG-CoA lyase (EC 4.1.3.4). P. mevalonii HMG-CoA lyase is a cytosolic protein with 301 amino acid residues and a molecular weight of 31,600. This represents the first reported sequence of an HMG-CoA lyase from any source.

This article has been cited by other articles:

• Forster-Fromme, K., Hoschle, B., Mack, C., Bott, M., Armbruster, W., Jendrossek, D. (2006). Identification of Genes and Proteins Necessary for Catabolism of Acyclic Terpenes and Leucine/Isovalerate in Pseudomonas aeruginosa.. Appl. Environ. Microbiol. 72: 4819-4828 [Abstract] [Full Text]  
• Gophna, U., Thompson, J. R., Boucher, Y., Doolittle, W. F. (2006). Complex Histories of Genes Encoding 3-Hydroxy-3-methylglutaryl-CoenzymeA Reductase. Mol Biol Evol 23: 168-178 [Abstract] [Full Text]  
• Zhang, Y.-X., Denoya, C. D., Skinner, D. D., Fedechko, R. W., McArthur, H. A. I., Morgenstern, M. R., Davies, R. A., Lobo, S., Reynolds, K. A., Hutchinson, C. R. (1999). Genes encoding acyl-CoA dehydrogenase (AcdH) homologues from Streptomyces coelicolor and Streptomyces avermitilis provide insights into the metabolism of small branched-chain fatty acids and macrolide antibiotic production. Microbiology 145: 2323-2334 [Abstract] [Full Text]  
• Gasson, M. J., Kitamura, Y., McLauchlan, W. R., Narbad, A., Parr, A. J., Parsons, E. L. H., Payne, J., Rhodes, M. J. C., Walton, N. J. (1998). Metabolism of Ferulic Acid to Vanillin. A BACTERIAL GENE OF THE ENOYL-SCoA HYDRATASE/ISOMERASE SUPERFAMILY ENCODES AN ENZYME FOR THE HYDRATION AND CLEAVAGE OF A HYDROXYCINNAMIC ACID SCoA THIOESTER. J. Biol. Chem. 273: 4163-4170 [Abstract] [Full Text]  
• Roberts, J. R., Mitchell, G. A., Miziorko, H. M. (1996). Modeling of a Mutation Responsible for Human 3-Hydroxy-3-methylglutaryl-CoA Lyase Deficiency Implicates Histidine 233as an Active Site Residue. J. Biol. Chem. 271: 24604-24609 [Abstract] [Full Text]  
• Roberts, J. R., Narasimhan, C., Miziorko, H. M. (1995). Evaluation of Cysteine 266 of Human 3-Hydroxy-3-methylglutaryl-CoA Lyase as a Catalytic Residue. J. Biol. Chem. 270: 17311-17316 [Abstract] [Full Text]