ERG7/YHR072W Literature Guide Help

Other names published for ERG7: lanosterol synthase ERG7, YHR072W

ERG7 - Function/Process (29)

ReferenceOther Genes Addressed
Oliaro-Bosso S, et al.  (2011) Characterization of the channel constriction allowing the access of the substrate to the active site of yeast oxidosqualene cyclase. PLoS One 6(7):e22134
Wu TK, et al.  (2010) Alteration of the Substrate's Prefolded Conformation and Cyclization Stereochemistry of Oxidosqualene-Lanosterol Cyclase of Saccharomyces cerevisiae by Substitution at Phenylalanine 699. Org Lett 12(3):500-3
Teske B, et al.  (2008) Genetic analyses involving interactions between the ergosterol biosynthetic enzymes, lanosterol synthase (Erg7p) and 3-ketoreductase (Erg27p), in the yeast Saccharomyces cerevisiae. Biochim Biophys Acta 1781(8):359-66
Wu TK, et al.  (2008) Importance of Saccharomyces cerevisiae Oxidosqualene-Lanosterol Cyclase Tyrosine 707 Residue for Chair-Boat Bicyclic Ring Formation and Deprotonation Reactions. Org Lett 10(21):4959-62
Wu TK, et al.  (2008) Protein plasticity: a single amino acid substitution in the Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase generates protosta-13(17),24-dien-3beta-ol, a rearrangement product. Org Lett 10(12):2529-32
Wu TK, et al.  (2006) Phenylalanine 445 within Oxidosqualene-Lanosterol Cyclase from Saccharomyces cerevisiae Influences C-Ring Cyclization and Deprotonation Reactions. Org Lett 8(21):4691-4
Wu TK, et al.  (2006) Site-Saturated Mutagenesis of Histidine 234 of Saccharomyces cerevisiae Oxidosqualene-Lanosterol Cyclase Demonstrates Dual Functions in Cyclization and Rearrangement Reactions. J Am Chem Soc 128(19):6414-9
Wu TK, et al.  (2006) Tryptophan 232 within oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae influences rearrangement and deprotonation but not cyclization reactions. Org Lett 8(7):1319-22
Altmann K and Westermann B  (2005) Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae. Mol Biol Cell 16(11):5410-7
Germann M, et al.  (2005) Characterizing sterol defect suppressors uncovers a novel transcriptional signaling pathway regulating zymosterol biosynthesis. J Biol Chem 280(43):35904-13
Oliaro-Bosso S, et al.  (2005) Access of the Substrate to the Active Site of Yeast Oxidosqualene Cyclase: An Inhibition and Site-Directed Mutagenesis Approach. Chembiochem 6(12):2221-2228
Ott RG, et al.  (2005) Flux of sterol intermediates in a yeast strain deleted of the lanosterol C-14 demethylase Erg11p. Biochim Biophys Acta 1735(2):111-8
Wu TK, et al.  (2005) Histidine residue at position 234 of oxidosqualene-lanosterol cyclase from saccharomyces cerevisiae simultaneously influences cyclization, rearrangement, and deprotonation reactions. Chembiochem 6(7):1177-81
Oliaro-Bosso S, et al.  (2004) Umbelliferone aminoalkyl derivatives as inhibitors of oxidosqualene cyclases from Saccharomyces cerevisiae, Trypanosoma cruzi, and Pneumocystis carinii. Lipids 39(10):1007-12
Mo C, et al.  (2003) In yeast sterol biosynthesis the 3-keto reductase protein (Erg27p) is required for oxidosqualene cyclase (Erg7p) activity. Biochim Biophys Acta 1633(1):68-74
Milla P, et al.  (2002) Yeast oxidosqualene cyclase (Erg7p) is a major component of lipid particles. J Biol Chem 277(4):2406-12
Segura MJ, et al.  (2002) Directed evolution experiments reveal mutations at cycloartenol synthase residue His477 that dramatically alter catalysis. Org Lett 4(25):4459-62
Athenstaedt K, et al.  (1999) Identification and characterization of major lipid particle proteins of the yeast Saccharomyces cerevisiae. J Bacteriol 181(20):6441-8
Corey EJ, et al.  (1996) Molecular cloning of a Schizosaccharomyces pombe cDNA encoding lanosterol synthase and investigation of conserved tryptophan residues. Biochem Biophys Res Commun 219(2):327-31
Venkatramesh M, et al.  (1996) Mechanism and structural requirements for transformation of substrates by the (S)-adenosyl-L-methionine:delta 24(25)-sterol methyl transferase from Saccharomyces cerevisiae. Biochim Biophys Acta 1299(3):313-24
Venkatramesh M and Nes WD  (1995) Novel sterol transformations promoted by Saccharomyces cerevisiae strain GL7: evidence for 9 beta, 19-cyclopropyl to 9(11)-isomerization and for 14-demethylation to 8(14)-sterols. Arch Biochem Biophys 324(1):189-99
Balliano G, et al.  (1994) Inhibition of sterol biosynthesis in Saccharomyces cerevisiae and Candida albicans by 22,23-epoxy-2-aza-2,3-dihydrosqualene and the corresponding N-oxide. Antimicrob Agents Chemother 38(9):1904-8
Nes WD, et al.  (1993) The structural requirements of sterols for membrane function in Saccharomyces cerevisiae. Arch Biochem Biophys 300(2):724-33
Balliano G, et al.  (1992) Characterization and partial purification of squalene-2,3-oxide cyclase from Saccharomyces cerevisiae. Arch Biochem Biophys 293(1):122-9
Ceruti M, et al.  (1992) 2,3-Epoxy-10-aza-10,11-dihydrosqualene, a high-energy intermediate analogue inhibitor of 2,3-oxidosqualene cyclase. J Med Chem 35(16):3050-8
Lewis TL, et al.  (1988) Pleiotropic mutations in Saccharomyces cerevisiae affecting sterol uptake and metabolism. Yeast 4(2):93-106
Nes WR and Dhanuka IC  (1988) Inhibition of sterol synthesis by delta 5-sterols in a sterol auxotroph of yeast defective in oxidosqualene cyclase and cytochrome P-450. J Biol Chem 263(24):11844-50
Karst F and Lacroute F  (1977) Ertosterol biosynthesis in Saccharomyces cerevisiae: mutants deficient in the early steps of the pathway. Mol Gen Genet 154(3):269-77
Katsuki H and Bloch K  (1967) Studies on the biosynthesis of ergosterol in yeast. Formation of methylated intermediates. J Biol Chem 242(2):222-7