Enzymatic formation of multiple triterpenes by mutation of tyrosine 510 of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae.
about
Unusually cyclized triterpenes: occurrence, biosynthesis and chemical synthesis.Synthesis of arborane triterpenols by a bacterial oxidosqualene cyclase.Progress in terpene synthesis strategies through engineering of Saccharomyces cerevisiae.β-Amyrin biosynthesis: catalytic mechanism and substrate recognition.Histidine residue at position 234 of oxidosqualene-lanosterol cyclase from saccharomyces cerevisiae simultaneously influences cyclization, rearrangement, and deprotonation reactions.The triterpene cyclase protein family: a systematic analysis.Protein engineering of oxidosqualene-lanosterol cyclase into triterpene monocyclase.
P2860
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P2860
Enzymatic formation of multiple triterpenes by mutation of tyrosine 510 of the oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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name
Enzymatic formation of multipl ...... from Saccharomyces cerevisiae.
@en
Enzymatic formation of multipl ...... from Saccharomyces cerevisiae.
@nl
type
label
Enzymatic formation of multipl ...... from Saccharomyces cerevisiae.
@en
Enzymatic formation of multipl ...... from Saccharomyces cerevisiae.
@nl
prefLabel
Enzymatic formation of multipl ...... from Saccharomyces cerevisiae.
@en
Enzymatic formation of multipl ...... from Saccharomyces cerevisiae.
@nl
P2860
P356
P1433
P1476
Enzymatic formation of multipl ...... from Saccharomyces cerevisiae.
@en
P2093
Cheng-Hsiang Chang
Tung-Kung Wu
P2860
P304
P356
10.1002/CBIC.200400079
P577
2004-12-01T00:00:00Z