LYPLAL1
Protein-coding gene in the species Homo sapiens
title: "LYPLAL1" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["genes-on-human-chromosome-1"] description: "Protein-coding gene in the species Homo sapiens" topic_path: "general/genes-on-human-chromosome-1" source: "https://en.wikipedia.org/wiki/LYPLAL1" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0
::summary Protein-coding gene in the species Homo sapiens ::
::data[format=table title="Infobox protein family"]
| Field | Value |
|---|---|
| Symbol | Lysophospholipase-like protein 1 |
| image | Human_LYPLAL1.png |
| caption | Crystal structure of human LYPLAL1, PDB code 3u0v. Alpha helices are in red, beta strands in gold, catalytic site residues in black. |
| Pfam | PF02230 |
| SCOP | 3u0v |
| CATH | 3u0v |
| InterPro | IPR029058 |
| :: |
| Symbol = Lysophospholipase-like protein 1 | Name = | image = Human_LYPLAL1.png | width = | caption = Crystal structure of human LYPLAL1, PDB code 3u0v. Alpha helices are in red, beta strands in gold, catalytic site residues in black. | Pfam = PF02230 | Pfam_clan = | SMART = | PROSITE = | MEROPS = | SCOP =3u0v | CATH =3u0v | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = | InterPro =IPR029058 Lysophospholipase-like 1 is a protein in humans that is encoded by the LYPLAL1 gene. | title = Entrez Gene: Lysophospholipase-like 1 | url = https://www.ncbi.nlm.nih.gov/gene?db=gene&cmd=retrieve&list_uids=127018 | access-date = 2013-02-27
Relationship to acyl-protein thioesterases
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. 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 and 2, as well as in Zea mays acyl-protein thioesterase 2. In LYPLAL1, this tunnel is closed due to a different loop conformation, changing the enzyme's substrate specificity to short acyl chains. ::figure[src="https://upload.wikimedia.org/wikipedia/commons/0/05/LYLPLAL1_tunnel.png" caption="electrostatic charges]] (red = negative, blue = positive, white = hydrophobic. On the right, the tunnel-closing loop is shown."] ::
References
References
- (2011). "Gene by sex interaction for measures of obesity in the framingham heart study". Journal of Obesity.
- (November 2010). "Meta-analysis identifies 13 new loci associated with waist-hip ratio and reveals sexual dimorphism in the genetic basis of fat distribution". Nature Genetics.
- (October 2007). "Adipocyte triglyceride lipase expression in human obesity". American Journal of Physiology. Endocrinology and Metabolism.
- (April 2012). "Distinct acyl protein transferases and thioesterases control surface expression of calcium-activated potassium channels". The Journal of Biological Chemistry.
- (May 2012). "Chemical-biological exploration of the limits of the Ras de- and repalmitoylating machinery". ChemBioChem.
- (January 2012). "Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity despite close relationship to acyl protein thioesterases". Journal of Lipid Research.
- (2018). "Structural and chemical biology of deacetylases for carbohydrates, proteins, small molecules and histones". Communications Biology.
- (January 2009). "Protein acyl thioesterases (Review)". Molecular Membrane Biology.
- (November 2000). "Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A". Structure.
- (December 2016). "Molecular Mechanism for Isoform-Selective Inhibition of Acyl Protein Thioesterases 1 and 2 (APT1 and APT2)". ACS Chemical Biology.
- (December 2017). "A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors". Nature Communications.
::callout[type=info title="Wikipedia Source"] This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page. ::