Lipase lid morph: Difference between revisions

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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]].


''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'>
''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 13:22, 14 May 2012

Candida rugosa lipase (1trh, 1lpm).

Drag the structure with the mouse to rotate

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 AlsoSee Also

Notes and ReferencesNotes 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