Tripeptidyl peptidase: Difference between revisions
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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> | ||