Tripeptidyl peptidase - Revision history

Michal Harel at 07:21, 17 May 2022

Michal Harel — Tue, 17 May 2022 07:21:07 GMT

←Older revision		Revision as of 07:21, 17 May 2022
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	== 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<ref>PMID:29378960</ref>.<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 />

Alexander Berchansky — Thu, 26 Sep 2019 14:04:32 GMT

←Older revision		Revision as of 14:04, 26 September 2019
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	== Structural highlights ==		== Structural highlights ==
-	TPP-I catalytic triad is the typical <scene name='43/433127/Cv/3'>Ser-Glu-Asp</scene> and the active site contains an <scene name='43/433127/Cv/4'>octahedrally coordinated Ca+2 ion</scene><ref>PMID:19038966</ref>.	+	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>

Michal Harel — Thu, 27 Sep 2018 17:15:56 GMT

←Older revision		Revision as of 17:15, 27 September 2018
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	== Function ==		== Function ==
	[[Tripeptidyl peptidase]] (TPP) is an enzyme which cleaves N-terminal tripeptides from polypeptides.<br />		[[Tripeptidyl peptidase]] (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.

Michal Harel — Thu, 27 Sep 2018 17:13:04 GMT

←Older revision		Revision as of 17:13, 27 September 2018
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-	<StructureSection load='' size='~~450~~' 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'>	+	<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 ==

Joel L. Sussman — Tue, 07 Nov 2017 11:26:23 GMT

←Older revision		Revision as of 11:26, 7 November 2017
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-	<StructureSection load='~~3ee6~~' size='450' 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'>	+	<StructureSection load='' size='450' 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 ==

Alexander Berchansky — Tue, 07 Nov 2017 10:20:23 GMT

←Older revision		Revision as of 10:20, 7 November 2017
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-	<StructureSection load='3ee6' size='450' 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/2'>	+	<StructureSection load='3ee6' size='450' 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 ==

Alexander Berchansky — Thu, 06 Apr 2017 12:55:21 GMT

←Older revision		Revision as of 12:55, 6 April 2017
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	== Structural highlights ==		== Structural highlights ==
-	TPP-I catalytic triad is the typical <scene name='43/433127/Cv/3'>Ser-Glu-Asp</scene> and the active site contains an octahedrally coordinated Ca+2 ion<ref>PMID:19038966</ref>.	+	TPP-I catalytic triad is the typical <scene name='43/433127/Cv/3'>Ser-Glu-Asp</scene> and the active site contains an <scene name='43/433127/Cv/4'>octahedrally coordinated Ca+2 ion</scene><ref>PMID:19038966</ref>.

	</StructureSection>		</StructureSection>

Alexander Berchansky — Thu, 06 Apr 2017 12:45:03 GMT

←Older revision		Revision as of 12:45, 6 April 2017
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	== Structural highlights ==		== Structural highlights ==
-	TPP-I catalytic triad is the typical Ser-Glu-Asp and the active site contains an octahedrally coordinated Ca+2 ion<ref>PMID:19038966</ref>.	+	TPP-I catalytic triad is the typical <scene name='43/433127/Cv/3'>Ser-Glu-Asp</scene> and the active site contains an octahedrally coordinated Ca+2 ion<ref>PMID:19038966</ref>.

	</StructureSection>		</StructureSection>

Alexander Berchansky — Thu, 06 Apr 2017 12:38:24 GMT

←Older revision		Revision as of 12:38, 6 April 2017
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-	<StructureSection load='3ee6' size='450' side='right' caption='Glycosylated tripeptidyl peptidase I dimer complex with sulfate, Zn+2 (grey), Ca+2 (green) and Cl- (green) ions, [[3ee6]]' scene=''>	+	<StructureSection load='3ee6' size='450' 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/2'>

	== Function ==		== Function ==

Alexander Berchansky — Thu, 06 Apr 2017 12:35:39 GMT

←Older revision		Revision as of 12:35, 6 April 2017
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-	<StructureSection load='3ee6' size='~~340~~' side='right' caption='Glycosylated tripeptidyl peptidase I dimer complex with sulfate, Zn+2 (grey), Ca+2 (green) and Cl- (green) ions, [[3ee6]]' scene=''>	+	<StructureSection load='3ee6' size='450' side='right' caption='Glycosylated tripeptidyl peptidase I dimer complex with sulfate, Zn+2 (grey), Ca+2 (green) and Cl- (green) ions, [[3ee6]]' scene=''>

	== Function ==		== Function ==