Identifiers | |||||||||
---|---|---|---|---|---|---|---|---|---|
Symbol | Lysophospholipase-like protein 1 | ||||||||
Pfam | PF02230 | ||||||||
InterPro | IPR029058 | ||||||||
CATH | 3u0v | ||||||||
SCOP2 | 3u0v / SCOPe / SUPFAM | ||||||||
|
Lysophospholipase-like 1 is a protein in humans that is encoded by the LYPLAL1 gene. [1] The protein is a α/β-hydrolase of uncharacterized metabolic function. Genome-wide association studies in humans have linked the gene to fat distribution [2] and waist-to-hip ratio. [3] The protein's enzymatic function is unclear. LYPLAL1 was reported to act as a triglyceride lipase in adipose tissue [4] and another study suggested that the protein may play a role in the depalmitoylation of calcium-activated potassium channels. [5] However, LYPLAL1 does not depalmitoylate the oncogene Ras [6] and a structural and enzymatic study concluded that LYPLAL1 is generally unable to act as a lipase and is instead an esterase that prefers short-chain substrates, such as acetyl groups. [7] Structural comparisons have suggested that LYPLAL1 might be a protein deacetylase, but this has not been experimentally tested. [8]
Sequence conservation and structural homology suggest a close relationship of LYPLAL1 proteins to acyl-protein thioesterases, and, therefore, it has been suggested that LYPLAL1 might be the third human acyl-protein thioesterase. [9] However, the major structural difference between both protein families has been established in the hydrophobic substrate binding tunnel, which has been identified in human acyl-protein thioesterases 1 [10] and 2, [11] as well as in Zea mays acyl-protein thioesterase 2. [12] In LYPLAL1, this tunnel is closed due to a different loop conformation, changing the enzyme's substrate specificity to short acyl chains. [7]
Identifiers | |||||||||
---|---|---|---|---|---|---|---|---|---|
Symbol | Lysophospholipase-like protein 1 | ||||||||
Pfam | PF02230 | ||||||||
InterPro | IPR029058 | ||||||||
CATH | 3u0v | ||||||||
SCOP2 | 3u0v / SCOPe / SUPFAM | ||||||||
|
Lysophospholipase-like 1 is a protein in humans that is encoded by the LYPLAL1 gene. [1] The protein is a α/β-hydrolase of uncharacterized metabolic function. Genome-wide association studies in humans have linked the gene to fat distribution [2] and waist-to-hip ratio. [3] The protein's enzymatic function is unclear. LYPLAL1 was reported to act as a triglyceride lipase in adipose tissue [4] and another study suggested that the protein may play a role in the depalmitoylation of calcium-activated potassium channels. [5] However, LYPLAL1 does not depalmitoylate the oncogene Ras [6] and a structural and enzymatic study concluded that LYPLAL1 is generally unable to act as a lipase and is instead an esterase that prefers short-chain substrates, such as acetyl groups. [7] Structural comparisons have suggested that LYPLAL1 might be a protein deacetylase, but this has not been experimentally tested. [8]
Sequence conservation and structural homology suggest a close relationship of LYPLAL1 proteins to acyl-protein thioesterases, and, therefore, it has been suggested that LYPLAL1 might be the third human acyl-protein thioesterase. [9] However, the major structural difference between both protein families has been established in the hydrophobic substrate binding tunnel, which has been identified in human acyl-protein thioesterases 1 [10] and 2, [11] as well as in Zea mays acyl-protein thioesterase 2. [12] In LYPLAL1, this tunnel is closed due to a different loop conformation, changing the enzyme's substrate specificity to short acyl chains. [7]