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- **********************************************************
- * Hydroxymethylglutaryl-coenzyme A reductases signatures *
- **********************************************************
-
- Hydroxymethylglutaryl-coenzyme A reductase (EC 1.1.1.34) (HMG-CoA reductase)
- [1,2] catalyzes the NADP-dependent synthesis of mevalonate from 3-hydroxy-3-
- methylglutaryl-CoA. In vertebrates, HMG-CoA reductase is the rate-limiting
- enzyme in the biosynthesis of cholesterol. In plants, mevalonate is the
- precursor of all isoprenoids compounds
-
- HMG-CoA reductase is a membrane bound enzyme. Structurally it consists of 3
- domains: a N-terminal region that contains a variable number of transmembrane
- segments (7 in mammals, insects, and fungi; 2 in plants), a linker region, and
- a C-terminal catalytic domain of approximately 400 amino acid residues.
-
- Some bacteria, such as Pseudomonas mevalonii, can use mevalonate as the sole
- carbon source. These bacteria use a NAD-dependent HMG-CoA reductase (EC 1.1.1.
- 88) to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA [3]. The
- Pseudomonas enzyme is structurally related to the catalytic domain of NADP-
- dependent HMG-CoA reductases.
-
- We have selected two conserved regions as signature patterns for HMG-CoA
- reductases. The first one is located in the center of the catalytic domain,
- while the second one is a glycine-rich region located in the C-terminal
- section of that domain
-
- -Consensus pattern: [RKH]-x(6)-D-x-M-G-x-N-x-[LIVM]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: Alcaligenes eutrophus plasmid pJP4
- 2,4-dichlorophenol hydroxylase (tfdB) and phage T4 protein GP27.
-
- -Consensus pattern: [LIVM]-G-x-[LIVM]-G-G-[AG]-T
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: Streptococcus pneumoniae amiC.
- -Last update: December 1992 / Text revised.
-
- [ 1] Caelles C., Ferrer A., Balcells L., Hegardt F.G., Boronat A.
- Plant Mol. Biol. 13:627-638(1989).
- [ 2] Basson M.E., Thorsness M., Finer-Moore J., Stroud R.M., Rine J.
- Mol. Cell. Biol. 8:3797-3808(1988).
- [ 3] Beach M.J., Rodwell V.W.
- J. Bacteriol. 171:2994-3001(1989).
-