Lipase lid morph

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For an introduction to the structure and function of lipase, please see the article [[Lipase]]. This ''Lipase lid morph'' article is a supplement to the main article on [[Lipase]].
For an introduction to the structure and function of lipase, please see the article [[Lipase]]. This ''Lipase lid morph'' article is a supplement to the main article on [[Lipase]].
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''Candida rugosa'' lipase (triacylglycerol hydrolase) has been observed in two conformations, with the "lid" closed ([[1trh]]) or open ([[1lpm]])<ref name='2states1994'>PMID: 8142901</ref>. When open, substrate can access the catalytic triad, Ser209, Glu341, and His449<ref name='2states1994'>
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''Candida rugosa'' lipase (triacylglycerol hydrolase) has been observed in two conformations, with the "lid" closed ([[1trh]]) or open ([[1lpm]])<ref name='2states1994'>PMID: 8142901</ref>. When open, substrate can access the catalytic triad, Ser209, Glu341, and His449<ref name='2states1994' />
==See Also==
==See Also==

Revision as of 10:22, 14 May 2012

Candida rugosa lipase (1trh, 1lpm).

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For an introduction to the structure and function of lipase, please see the article Lipase. This Lipase lid morph article is a supplement to the main article on Lipase.

Candida rugosa lipase (triacylglycerol hydrolase) has been observed in two conformations, with the "lid" closed (1trh) or open (1lpm)[1]. When open, substrate can access the catalytic triad, Ser209, Glu341, and His449[1]

See Also

Notes and References

  1. ↑ 1.0 1.1 Grochulski P, Li Y, Schrag JD, Cygler M. Two conformational states of Candida rugosa lipase. Protein Sci. 1994 Jan;3(1):82-91. PMID:8142901

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Eric Martz, Karsten Theis

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