1LPP

ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE

Summary for 1LPP

• Entry DOI: 10.2210/pdb1lpp/pdb
• Descriptor: LIPASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: hydrolase
• Biological source: Candida rugosa (ascomycetes)
• Total number of polymer chains: 1
• Total formula weight: 59927.40

Authors

Grochulski, P.G.,Cygler, M.C. (deposition date: 1995-01-17, release date: 1995-04-20, Last modification date: 2024-10-23)

Primary citation

Grochulski, P.,Bouthillier, F.,Kazlauskas, R.J.,Serreqi, A.N.,Schrag, J.D.,Ziomek, E.,Cygler, M.
Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase.
Biochemistry, 33:3494-3500, 1994

PubMed Abstract: The structures of Candida rugosa lipase-inhibitor complexes demonstrate that the scissile fatty acyl chain is bound in a narrow, hydrophobic tunnel which is unique among lipases studied to date. Modeling of triglyceride binding suggests that the bound lipid must adopt a "tuning fork" conformation. The complexes, analogs of tetrahedral intermediates of the acylation and deacylation steps of the reaction pathway, localize the components of the oxyanion hole and define the stereochemistry of ester hydrolysis. Comparison with other lipases suggests that the positioning of the scissile fatty acyl chain and ester bond and the stereochemistry of hydrolysis are the same in all lipases which share the alpha/beta-hydrolase fold.

PubMed: 8142346
DOI: 10.1021/bi00178a005

Experimental method

X-RAY DIFFRACTION (2.18 Å)