Cloning, sequencing, and overexpression of mvaA, which encodes Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase - PubMed (original) (raw)

Comparative Study

Cloning, sequencing, and overexpression of mvaA, which encodes Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase

M J Beach et al. J Bacteriol. 1989 Jun.

Abstract

We have cloned, determined the primary structure of, and overexpressed in Escherichia coli the gene mvaA, which is the 1,287-base structural gene for the 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase [EC 1.1.1.88] of Pseudomonas mevalonii. The amino acid composition of HMG-CoA reductase agreed with that predicted from the nucleotide sequence of mvaA, and DNA-derived sequences were identical to all experimentally determined peptide sequences. Overexpression of mvaA in E. coli yielded quantities of HMG-CoA reductase over 1,500-fold higher than those present in control cultures. Comparison of the primary structure of the P. mevalonii enzyme with the DNA-derived primary structure for a mammalian HMG-CoA reductase revealed two regions of similarity suggestive of functional relatedness. An open reading frame, ORF1, lies on the 3' side of mvaA, and a potential ribosome-binding site for ORF1 overlaps the termination codon of mvaA.

PubMed Disclaimer

Cited by

An Atomic-Level Perspective of HMG-CoA-Reductase: The Target Enzyme to Treat Hypercholesterolemia.
Gesto DS, Pereira CMS, Cerqueira NMFS, Sousa SF. Gesto DS, et al. Molecules. 2020 Aug 26;25(17):3891. doi: 10.3390/molecules25173891. Molecules. 2020. PMID: 32859023 Free PMC article. Review.
Divergent Isoprenoid Biosynthesis Pathways in Staphylococcus Species Constitute a Drug Target for Treating Infections in Companion Animals.
Misic AM, Cain CL, Morris DO, Rankin SC, Beiting DP. Misic AM, et al. mSphere. 2016 Sep 28;1(5):e00258-16. doi: 10.1128/mSphere.00258-16. eCollection 2016 Sep-Oct. mSphere. 2016. PMID: 27704053 Free PMC article.
A novel role for coenzyme A during hydride transfer in 3-hydroxy-3-methylglutaryl-coenzyme A reductase.
Steussy CN, Critchelow CJ, Schmidt T, Min JK, Wrensford LV, Burgner JW 2nd, Rodwell VW, Stauffacher CV. Steussy CN, et al. Biochemistry. 2013 Aug 6;52(31):5195-205. doi: 10.1021/bi400335g. Epub 2013 Jul 24. Biochemistry. 2013. PMID: 23802607 Free PMC article.
Inhibition of the class II HMG-CoA reductase of Pseudomonas mevalonii.
Hedl M, Rodwell VW. Hedl M, et al. Protein Sci. 2004 Jun;13(6):1693-7. doi: 10.1110/ps.03597504. Protein Sci. 2004. PMID: 15152097 Free PMC article.
Essentiality, expression, and characterization of the class II 3-hydroxy-3-methylglutaryl coenzyme A reductase of Staphylococcus aureus.
Wilding EI, Kim DY, Bryant AP, Gwynn MN, Lunsford RD, McDevitt D, Myers JE Jr, Rosenberg M, Sylvester D, Stauffacher CV, Rodwell VW. Wilding EI, et al. J Bacteriol. 2000 Sep;182(18):5147-52. doi: 10.1128/JB.182.18.5147-5152.2000. J Bacteriol. 2000. PMID: 10960099 Free PMC article.

References

1. J Mol Biol. 1983 Jun 5;166(4):557-80 - PubMed
1. Methods Enzymol. 1983;91:352-9 - PubMed
1. Biochemistry. 1983 Aug 16;22(17):4089-95 - PubMed
1. Methods Enzymol. 1983;100:243-55 - PubMed
1. Experientia. 1983 Nov 15;39(11):1199-213 - PubMed

Cloning, sequencing, and overexpression of mvaA, which encodes Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase - PubMed (original) (raw)