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1hm4

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{{STRUCTURE_1hm4| PDB=1hm4 | SCENE= }}
{{STRUCTURE_1hm4| PDB=1hm4 | SCENE= }}
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'''N219L PENTALENENE SYNTHASE'''
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===N219L PENTALENENE SYNTHASE===
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==Overview==
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Incubation of farnesyl diphosphate (1) with the W308F or W308F/H309F mutants of pentalenene synthase, an enzyme from Streptomyces UC5319, yielded pentalenene (2), accompanied by varying proportions of (+)-germacrene A (7) with relatively minor changes in k(cat) and k(cat)/K(m). By contrast, single H309 mutants gave rise to both (+)-germacrene A (7) and protoilludene (8) in addition to pentalenene (2). Mutation to glutamate of each of the three aspartate residues in the Mg(2+)-binding aspartate-rich domain, (80)DDLFD, resulted in reduction in the k(cat)/K(m) for farnesyl diphosphate and formation of varying proportions of pentalenene and (+)-germacrene A (7). Formation of (+)-germacrene A (7) by the various pentalenene synthase mutants is the result of a derailment of the natural anti-Markovnikov cyclization reaction, and not simply the consequence of trapping of a normally cryptic, carbocationic intermediate. Both the N219A and N219L mutants of pentalenene synthase were completely inactive, while the corresponding N219D mutant had a k(cat)/K(m) which was 3300-fold lower than that of the wild-type synthase, and produced a mixture of pentalenene (2) (91%) and the aberrant cyclization product beta-caryophyllene (9) (9%). Finally, the F77Y mutant had a k(cat)/K(m) which was reduced by 20-fold compared to that of the wild-type synthase.
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(as it appears on PubMed at http://www.pubmed.gov), where 12083921 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12083921}}
==About this Structure==
==About this Structure==
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[[Category: Sesquiterpene synthase]]
[[Category: Sesquiterpene synthase]]
[[Category: Terpene]]
[[Category: Terpene]]
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Revision as of 05:23, 1 July 2008

Image:1hm4.png

Template:STRUCTURE 1hm4

N219L PENTALENENE SYNTHASE

Template:ABSTRACT PUBMED 12083921

About this Structure

1HM4 is a Single protein structure of sequence from Streptomyces sp.. Full crystallographic information is available from OCA.

Reference

Pentalenene synthase. Analysis of active site residues by site-directed mutagenesis., Seemann M, Zhai G, de Kraker JW, Paschall CM, Christianson DW, Cane DE, J Am Chem Soc. 2002 Jul 3;124(26):7681-9. PMID:12083921

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