Tripeptidyl peptidase
From Proteopedia
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| - | <StructureSection load=' | + | <StructureSection load='' size='350' side='right' caption='Glycosylated tripeptidyl peptidase I dimer complex with sulfate, Zn+2 (grey), Ca+2 (green) and Cl- (green) ions, [[3ee6]]' scene='43/433127/Cv/5'> |
== Function == | == Function == | ||
| - | [[Tripeptidyl peptidase]] (TPP) is an enzyme which cleaves N-terminal tripeptides from polypeptides.<br /> | + | [[Tripeptidyl peptidase]] or '''tripeptidyl aminopeptidase''' (TPP) is an enzyme which cleaves N-terminal tripeptides from polypeptides.<br /> |
| - | * '''TPP-I''' functions in lysosomes.<br /> | + | * '''TPP-I''' functions in lysosomes<ref>PMID:29378960</ref>.<br /> |
* '''TPP-II''' is part of the ubiquitin-proteasome pathway. <br /> | * '''TPP-II''' is part of the ubiquitin-proteasome pathway. <br /> | ||
* '''TPP-IV''' is a serine exopeptidase which cleaves proline dipeptides from the N-terminus of polypeptides. | * '''TPP-IV''' is a serine exopeptidase which cleaves proline dipeptides from the N-terminus of polypeptides. | ||
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== Structural highlights == | == Structural highlights == | ||
| - | TPP-I catalytic triad is the typical <scene name='43/433127/Cv/ | + | TPP-I catalytic triad is the typical <scene name='43/433127/Cv/6'>Ser-Glu-Asp</scene> and the active site contains an <scene name='43/433127/Cv/7'>octahedrally coordinated Ca+2 ion</scene><ref>PMID:19038966</ref>. |
</StructureSection> | </StructureSection> | ||
Current revision
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3D Structures of Tripeptidyl peptidase
Updated on 17-May-2022
References
- ↑ Sole-Domenech S, Rojas AV, Maisuradze GG, Scheraga HA, Lobel P, Maxfield FR. Lysosomal enzyme tripeptidyl peptidase 1 destabilizes fibrillar Abeta by multiple endoproteolytic cleavages within the beta-sheet domain. Proc Natl Acad Sci U S A. 2018 Feb 13;115(7):1493-1498. doi:, 10.1073/pnas.1719808115. Epub 2018 Jan 29. PMID:29378960 doi:http://dx.doi.org/10.1073/pnas.1719808115
- ↑ Wisniewski KE, Kida E, Walus M, Wujek P, Kaczmarski W, Golabek AA. Tripeptidyl-peptidase I in neuronal ceroid lipofuscinoses and other lysosomal storage disorders. Eur J Paediatr Neurol. 2001;5 Suppl A:73-9. PMID:11589013
- ↑ Stepensky P, Rensing-Ehl A, Gather R, Revel-Vilk S, Fischer U, Nabhani S, Beier F, Brummendorf TH, Fuchs S, Zenke S, Firat E, Pessach VM, Borkhardt A, Rakhmanov M, Keller B, Warnatz K, Eibel H, Niedermann G, Elpeleg O, Ehl S. Early-onset Evans syndrome, immunodeficiency, and premature immunosenescence associated with tripeptidyl-peptidase II deficiency. Blood. 2015 Jan 29;125(5):753-61. doi: 10.1182/blood-2014-08-593202. Epub 2014, Nov 20. PMID:25414442 doi:http://dx.doi.org/10.1182/blood-2014-08-593202
- ↑ McKay RM, McKay JP, Suh JM, Avery L, Graff JM. Tripeptidyl peptidase II promotes fat formation in a conserved fashion. EMBO Rep. 2007 Dec;8(12):1183-9. Epub 2007 Oct 12. PMID:17932511 doi:http://dx.doi.org/10.1038/sj.embor.7401086
- ↑ Pal A, Kraetzner R, Gruene T, Grapp M, Schreiber K, Gronborg M, Urlaub H, Becker S, Asif AR, Gartner J, Sheldrick GM, Steinfeld R. Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis. J Biol Chem. 2009 Feb 6;284(6):3976-84. Epub 2008 Nov 26. PMID:19038966 doi:10.1074/jbc.M806947200
