Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity despite close relationship to acyl protein thioesterases.
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ABSTRACT:
SUBMITTER: Burger M
PROVIDER: S-EPMC3243480 | biostudies-literature | 2012 Jan
REPOSITORIES: biostudies-literature
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Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity despite close relationship to acyl protein thioesterases.
Bürger Marco M Zimmermann Tobias J TJ Kondoh Yasumitsu Y Stege Patricia P Watanabe Nobumoto N Osada Hiroyuki H Waldmann Herbert H Vetter Ingrid R IR
Journal of lipid research 20111103 1
Sequence homology indicates the existence of three human cytosolic acyl protein thioesterases, including APT1 that is known to depalmitoylate H- and N-Ras. One of them is the lysophospholipase-like 1 (LYPLAL1) protein that on the one hand is predicted to be closely related to APT1 but on the other hand might also function as a potential triacylglycerol lipase involved in obesity. However, its role remained unclear. The 1.7 Å crystal structure of LYPLAL1 reveals a fold very similar to APT1, as ex ...[more]
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