Tripeptidyl peptidase: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel, Joel L. Sussman

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-[[Image:2d5l.png|left|200px|thumb|Crystal Structure of Tripeptidyl peptidase ([[2d5l]])]]
+<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'>
-{{STRUCTURE_3ee6|  PDB=3ee6  | SIZE=400| SCENE= |right|CAPTION=Tripeptidyl peptidase dimer complex with sulfate, Zn+2 (grey), Ca+2 (green) and Cl- (green) ions, [[3ee6]]}}
+== Function ==
+[[Tripeptidyl peptidase]] or '''tripeptidyl aminopeptidase''' (TPP) is an enzyme which cleaves N-terminal tripeptides from polypeptides.<br />
+*  '''TPP-I''' functions in lysosomes<ref>PMID:29378960</ref>.<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.
+== Didease ==
+TPP-I participates in lysosomal turnover of proteins in pathological conditions associated with cell injury and its mutations cause the fatal neurodegenerative childhood neuronal ceroid lipofuscinosis<ref>PMID:11589013</ref>.  TPP-II deficiency is linked to severe autoimmunity<ref>PMID:25414442</ref>.  TPP-II has central and peripheral roles in metabolism and hence in fat formation<ref>PMID:17932511</ref>.
+== Structural highlights ==
+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>
-[[Tripeptidyl peptidase]] (TPP) is an enzyme which cleaves N-terminal tripeptides from polypeptides.  TPP-I functions in lysosomes, TPP-II is part of the ubiquitin-proteasome pathway. The images at the left and at the right correspond to one representative TPP, ''i.e.'' the crystal structure of Pro-Tripeptidyl peptidase-IV from ''Porphyromonas gingivalis'' ([[2d5l]]).
-{{TOC limit|limit=2}}
 == 3D Structures of Tripeptidyl peptidase ==
+Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+{{#tree:id=OrganizedByTopic|openlevels=0|
+*Tripeptidyl peptidase-I
-===TPP-I===
+**[[3ee6]] – TPP-I – human<br />
+**[[3edy]] – hTPP-I precursor residues 20-563<br />
-[[3ee6]] – TPP-I – human<br />
-[[3edy]] – hTPP-I precursor residues 20-563<br />
-===TPP-II===
-[[3lxu]] – TPP-II residues 463-770 – ''Drosophila melanogaster''<br />
-===TPP-IV===
+*Tripeptidyl peptidase-II
-[[2eep]] – PgPro-TPP-IV+inhibitor – ''Porphyromonas gingivalis''<br />
+**[[3lxu]] – TPP-II residues 463-770 – ''Drosophila melanogaster''<br />
-[[2d5l]] - PgPro-TPP-IV<br />
-[[2z3w]] - PgPro-TPP-IV (mutant)<br />
-[[2z3z]], [[2dcm]] - PgPro-TPP-IV (mutant)+inhibitor<br />
+*Tripeptidyl peptidase-IV
+**[[2eep]] – PgPro-TPP-IV+inhibitor – ''Porphyromonas gingivalis''<br />
+**[[2d5l]] - PgPro-TPP-IV<br />
+**[[2z3w]] - PgPro-TPP-IV (mutant)<br />
+**[[2z3z]] - PgPro-TPP-IV (mutant)+inhibitor<br />
+**[[2dcm]] - PgPro-TPP-IV (mutant) + substrate<br />
+}}
+== References ==
+<references/>
 [[Category:Topic Page]]