Studies on the substrate binding segments and catalytic action of lanosterol synthase. Affinity labeling with carbocations derived from mechanism-based analogs of 2,3-oxidosqualene and site-directed mutagenesis probes

Journal of the American Chemical Society

Volumn 119, Issue 6, 1997, Pages 1289-1296

  Corey, E J ^a   Cheng, Hengmiao ^a   Baker, C Hunter ^a   Matsuda, Seiichi P T ^a   Li, Ding ^a   Song, Xuelei ^a  

^a HARVARD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

LANOSTEROL SYNTHASE;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MODEL; SACCHAROMYCES CEREVISIAE; SITE DIRECTED MUTAGENESIS;

EID: 0030984243     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja963228o     Document Type: Article

References (20)

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15. 4 reverse phase HPLC and counted for radioactivity. Any radioactive peak was rechromatographed and submitted for sequencing by automated Edman degradation on an Applied Biosystems 494A, 477A (Foster City CA) or Hewlett Packard G1005A (Palo Alto CA) instrument. Tryptic peptide sequences were also determined by microcapillary HPLC/electrospray ionization/tandem mass spectrometry on a Finnigan TSQ7000 triple quadrupole mass spectrometer (San Jose, CA) as described by Hunt et al. (1992). These analyses were performed by Dr. William S. Lane and associates in the Harvard Protein Microchemical Analysis Laboratory. We are grateful to them for expert assistance,
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