Chain elongation in the isoprenoid biosynthetic pathway

Current Opinion in Chemical Biology

Volumn 1, Issue 4, 1997, Pages 570-578

  Kellogg, Brenda A ^a   Poulter, C Dale ^a  

^a UNIVERSITY OF UTAH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FARNESYL TRANS TRANSFERASE; GERANYLTRANSFERASE; ISOPRENOID PHOSPHATE; TRANSFERASE;

BINDING SITE; BIOSYNTHESIS; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; DIMERIZATION; ENZYMOLOGY; GENETICS; METABOLISM; PHYLOGENY; PROTEIN PROCESSING; PROTEIN SECONDARY STRUCTURE; REVIEW; SACCHAROMYCES CEREVISIAE;

ALKYL AND ARYL TRANSFERASES; BINDING SITES; CATALYSIS; DIMERIZATION; FARNESYLTRANSTRANSFERASE; GERANYLTRANSTRANSFERASE; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MOLECULAR STRUCTURE; PHYLOGENY; POLYISOPRENYL PHOSPHATES; PROTEIN ISOPRENYLATION; PROTEIN STRUCTURE, SECONDARY; SACCHAROMYCES CEREVISIAE;

EID: 0031311293     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(97)80054-3     Document Type: Article

References (32)

1. Spurgeon SL, Porter JW: Conversion of Acetyl Coenzyme A to isopentenyl pyrophosphate. In Biosynthesis of Isoprenoid Compounds, vol 1. Edited by Porter JW, Spurgeon SL New York: John Wiley and Sons; 1981:1-93.
2. Rohmer M, Seeman M, Horbach S, Bringer-Meyer S, Sahm H: Glyceraldehyde 3-phosphate and pyruvate as precursors of isoprenic units in an alternative nonmevalonate pathway for terpenoid biosynthesis. J Am Chem Soc 1996, 118:2564-2566. Glyceraldehyde 3-phosphate and pyruvate were shown to be the initial precursors in an alternate non-mevalonate pathway leading to the production of IPP in bacteria.
3. Poulter CD, Satterwhite DM: Mechanism of the prenyl-transfer reaction. Studies with (E) and (Z)-3-trifluoromethyl-2-buten-1-yl pyrophosphate. Biochemistry 1977, 16:5470-5478.
4. Poulter CD, Argyle JC, Mash EA: Farnesyl diphosphate synthetase: mechanistic studies of the 1′-4 coupling reaction with 2-fluorogeranyl pyrophosphate. J Biol Chem 1978, 253:7227-7233.
5. Poulter CD, Wiggins PL, Le AT: Farnesylpyrophosphate synthetase. A stepwise mechanism for the 1′-4 condensation reaction. J Am Chem Soc 1981, 103:3926-3927.
6. Davisson VJ, Neal TR, Poulter CD: Farnesyl diphosphate synthase. Catalysis of an intramolecular prenyl transfer with bisubstrate analogs. J Am Chem Soc 1993, 115:1235-1245.
7. Davisson VJ, Poulter CD: Farnesyl diphosphate synthase. Interplay between substrate topology, stereochemistry and regiochemistry in electrophilic alkylations. J Am Chem Soc 1993, 115:1245-1260.
8. Cornforth JW, Cornforth RH, Doninger C, Popjak G: Studies on the biosynthesis of cholesterol XIX Steric course of hydrogen elimination and of C-C bond formations in squalene biosynthesis. Proc R Soc Lond B Biol Sci 1966, 163:492-514.
9. Chen A, Kroon PA, Poulter CD: Isoprenyl diphosphae syntheses: protein sequence comparisons, a phylogenetic tree and predictions of secondary structure. Protein Sci 1994, 3:600-607.
10. Tarshis LC, Yan M, Poulter CD, Sachetinni JC: Crystal structure of recombinant farnesyl diphosphate synthase at 2.6 Ȧ resolution. Biochemistry 1994, 33:10871-10877.
11. Eberhardt NL, Rilling HC: Prenyltransferase from Saccharomyces cerevisiae. Purification to homogeneity and molecular properties. J Biol Chem 1975, 250:863-866.
12. Dogbo A, Camara B: Purification of isopentenyl pyrophosphate isomerase and geranyl geranyl pyrophosphate synthase from Capsicum chromoplasts by affinity chromatography. Biochim Biophys Acta 1987, 920:140-148.
13. Chen A, Poulter CD: Purification and characterization of farnesyl diphosphate/geranyl geranyl diphosphate synthase, a thermostable bifunctional enzyme from methanobacterium thermoautotrophicum. J Biol Chem 1993, 268:11002-11007.
14. Reed BC, Rilling HC: Substrate binding of avian liver prenyltransferase. Biochemistry 1976, 15:3739-3745.
15. Jiang Y, Proteau P, Poulter D, Ferro-Novick S: BTS1 encodes a geranyl geranyl diphosphate synthase in Saccharomyces cerevisiae. J Biol Chem 1995, 270:21793-21799.
16. Sagami H, Morita Y, Ogura K: Purification and properties of geranylgeranyl-diphosphate synthase from bovine brain. J Biol Chem 1994, 269: 32, 20561-20566.
17. Yoshida I, Koyama T, Ogura K: Dynamic interaction between components of hexaprenyl diphosphate synthase from Micrococcus luteus BP-26. Biochemistry 1987, 26:6840-6845.
18. Fujii H, Koyama T, Ogura K: Essential protein factors for polyprenyl pyrophosphate synthetases. FEBS Lett 1983, 161:257-260.
19. Koike-Takeshita A, Koyama T, Obata S, Ogura K: Molecular cloning and nucleotide sequences of the genes for two essential proteins constituting a novel enzyme system for heptaprenyl diphosphate synthesis. J Biol Chem 1995, 270:18396-18400.
20. Zhang Y, Koyama T, Ogura K: Two cistrons of the gerC operon of Bacillus subtilis encode the two subunits of heptaprenyl diphosphate synthase. J Bacteriol 1997, 179:1417-1419. The two proteins encoded by the gerC locus of Bacillus subtilis were identified as dissociable heterodimers of the HepPPSase involved in the biosynthesis of the sidechain of menaquinone 7 (a mobile electron carrier which contains a prenyl side chain consisting of seven isoprene units).
21. Ashby MN, Edwards PA: Elucidation of the deficiency in two yeast coenzyme Q mutants. Characterization of the structural gene encoding hexaprenyl pyrophosphate synthetase. J Biol Chem 1990, 265:13157-13164.
22. Ohnuma S, Koyama T, Ogura K: Purification of solanesyl diphosphate synthase from Micrococcus luteus. A new class of prenyltransferase. J Biol Chem 1991, 266:23706-23713.
23. 2+ ions with the first conserved DDXXD (single-letter amino acid code, where X is any amino acid) motif and that the phenylalanines mutated at positions 112 and 113 make up the floor of the allylic binding pocket which interacts with the hydrocarbon tail of geranyl diphosphate.
24. Song L, Poulter CD: Yeast farnesyl-diphosphate synthase: site-directed mutagenesis of residues in highly conserved prenyltransferase domains I and II. Proc Natl Acad Sci USA 1994, 91:3044-3048.
25. IPP.
26. Marrero PF, Poulter CD, Edwards PA: Effects of site-directed mutagenesis on the highly conserved aspartate residues in domain II of FPPSase activity. J Biol Chem 1992, 267:21873-21878.
27. Koyama T, Tajima M, Nishino T, Ogura K: Significance of Phe220 and Gln-221 in the catalytic mechanism of farnesyl diphosphate synthase of Bacillus stearothermophilus. Biochem Biophys Res Comm 1995, 212:681-686.
28. Ohnuma S, Nakazawa T, Hemmi H, Hallberg A, Koyama T, Ogura K, Nishino T: Conversion from farnesyl diphosphate synthase to geranylgeranyl diphosphate synthase by random chemical mutagenesis. J Biol Chem 1996, 271:10087-10095. This paper examines the determinants of product chain length specificity in Bacillus stearothermophilus farnesyl diphosphate synthase using a random mutagenesis approach coupled with a clever in vivo screening method. Mutations of three amino acids (Leu59, Tyr81 and Val157) to smaller residues led to the ability of the enzyme to produce geranylgeranyl diphosphate.
29. Ohnuma S, Hirooka K, Ohto C, Nishino T: Conversion from archael geranylgeranyl diphosphate synthase to farnesyl diphosphate synthase. Two amino acids before the first aspartate rich motif solely determine eukaryotic farnesyl diphosphate synthase activity. J Biol Chem 1997, 272:5192-5198. Six mutant geranylgeranyl diphosphate synthases (GGPPSases) were constructed by inserting the regions around the first aspartate-rich motif from human, rat, plant, yeast, and bacterial farnesyl diphosphate synthases (FPP-Sases) into the corresponding region of Sulfolobus acidocaldarius GGPP-Sase. Product specificity analysis in these mutants demonstrated that in eukaryotic FPPSases the two amino acids located four and five residues before the first DDXXD (single-letter amino acid code, where X is any amino acid) motif solely determine product chain length.
30. Ohnuma S, Hirooka K, Hemmi H, Ishida C, Ohto C, Nishino T: Conversion of product specificity of archaebacterial geranylgeranyl diphosphate synthase. Identification of essential amino acid residues for chain length determination of prenyltransferase reaction. J Biol Chem 1996, 271:18831-18837.
31. Baba T, Allen CM: Prenyltransferases from Micrococcus luteus: characterization of undecaprenyl pyrophosphate synthetase. Arch Biochem Biophys 1980, 200:474-484.
32. Adair WL, Cafmeyer N, Keller RK: Solubilization and characterization of the long chain prenyltransferase involved in dolichyl phosphate biosynthesis. J Biol Chem 1984, 259:4441-4445.