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Volumn 6, Issue 7, 2005, Pages 1177-1181
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Histidine residue at position 234 of oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae simultaneously influences cyclization, rearrangement, and deprotonation reactions
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Author keywords
Cyclization; Homology modeling; Oxidosqualene cyclase; Rearrangement; Sterols; Terpenoids
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Indexed keywords
LANOSTEROL SYNTHASE;
PROTEIN OXIDOSQUALENE LANOSTEROL CYCLASE;
UNCLASSIFIED DRUG;
AMINO ACID SEQUENCE;
ARTICLE;
CYCLIZATION;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
MUTATIONAL ANALYSIS;
PRIORITY JOURNAL;
PROTEIN ANALYSIS;
PROTEIN FUNCTION;
PROTEIN STRUCTURE;
PROTON TRANSPORT;
REACTION ANALYSIS;
SACCHAROMYCES CEREVISIAE;
STRUCTURE ACTIVITY RELATION;
AMINO ACID SEQUENCE;
CYCLIZATION;
HISTIDINE;
INTRAMOLECULAR TRANSFERASES;
MODELS, MOLECULAR;
MUTAGENESIS, SITE-DIRECTED;
POLYMERASE CHAIN REACTION;
SACCHAROMYCES CEREVISIAE;
SACCHAROMYCES CEREVISIAE PROTEINS;
TRITERPENES;
SACCHAROMYCES CEREVISIAE;
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EID: 22144474720
PISSN: 14394227
EISSN: None
Source Type: Journal
DOI: 10.1002/cbic.200500084 Document Type: Article |
Times cited : (31)
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References (25)
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