Aminoacylase - Revision history

Michal Harel at 08:18, 27 May 2019

Michal Harel — Mon, 27 May 2019 08:18:05 GMT

←Older revision		Revision as of 08:18, 27 May 2019
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	</StructureSection>		</StructureSection>
-	==3D structures of D-aminoacylase==

-	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-	{{#tree:id=OrganizedByTopic\|openlevels=0\|
-
-	*D-aminoacylase
-
-	**[[1m7j]], [[1v51]] – AfDAA + Zn – ''Alcaligenes faecalis''<br />
-	**[[1rjq]], [[1rjr]], [[1v4y]] - AfDAA (mutant) + Zn <br />
-	**[[1rjp]] - AfDAA + Zn + Cu<br />
-	**[[1rk5]] - AfDAA (mutant) + Zn + Cu<br />
-	**[[1rk6]] - AfDAA + Zn + Cd<br />
-
-	*L-aminoacylase or aspartoacylase
-
-	**[[1q7l]] – hLAA 1 (mutant) + Zn - human<br />
-	**[[2i3c]], [[2o53]], [[2q51]] – hLAA 2 + Zn <br />
-	**[[2o4h]] – hLAA 2 + Zn + methyl-aspartate<br />
-	**[[4mri]], [[4mxu]], [[4nfr]], [[4tnu]] – hLAA 2 (mutant) + Zn + methyl-aspartate<br />
-	**[[2q4z]], [[2gu2]] – LAA 2 + Zn - rat<br />
-	**[[3nh4]] – mLAA 3 + Zn + Cs – mouse <br />
-	**[[3nh3]] – mLAA 3 (mutant) + Zn <br />
-	**[[3nfz]] – mLAA 3 (mutant) + Zn + acetyl-tyrosine<br />
-	**[[3nh8]] – mLAA 3 (mutant) + Zn + acetyl-cysteine<br />
-	}}
	== References ==		== References ==
	<references/>		<references/>

	[[Category:Topic Page]]		[[Category:Topic Page]]

Michal Harel at 08:16, 27 May 2019

Michal Harel — Mon, 27 May 2019 08:16:58 GMT

←Older revision		Revision as of 08:16, 27 May 2019
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	== Function ==		== Function ==

-	'''D-aminoacylase''' (DAA) hydrolyzes N-acyl neutral D-amino acids. DAA was found in different genera of bacteria: ''Pseudomonas'', ''Streptomyces'' and ''Alcaligenes''. Each genera has a different substrate preference. DAA from ''Alcaligenes faecalis'' (AfDAA) shows preference for D-Met, D-Phe and D-Leu and lesser effectivity for D-Trp, D-Ala and D-val. AfDAA is a zinc-assisted enzyme. <ref name="Ad">PMID:14736882</ref>	+	'''D-aminoacylase''' (DAA) hydrolyzes N-acyl neutral D-amino acids. DAA was found in different genera of bacteria: ''Pseudomonas'', ''Streptomyces'' and ''Alcaligenes''. Each genera has a different substrate preference. DAA from ''Alcaligenes faecalis'' (AfDAA) shows preference for D-Met, D-Phe and D-Leu and lesser effectivity for D-Trp, D-Ala and D-val. AfDAA is a zinc-assisted enzyme. <ref name="Ad">PMID:14736882</ref>'''L-aminoacylase''' (LAA) or '''aspartoacylase''' hydrolyzes N-acyl-L-amino acid to L-amino acid and carboxylate.

		+	== Disease ==
		+
		+	Mutations in LAA1 are characterized by accumulation of N-acetyl amino acids in the urine and cause seizures, delay of psychomotor development and moderate mental retardation<ref>PMID:21414403</ref>
	== Structural highlights ==		== Structural highlights ==

	AfDAA is catalytically activated by Zn<sup>+2</sup> <scene name='57/570615/Cv/5'>bound tightly at the β site</scene> and <scene name='57/570615/Cv/6'>inhibited by the addition of a second weakly bound Zn<sup>+2</sup> at the α site</scene>. <scene name='57/570615/Cv/7'>Two sites together</scene>.<ref name="Ad">PMID:14736882</ref>		AfDAA is catalytically activated by Zn<sup>+2</sup> <scene name='57/570615/Cv/5'>bound tightly at the β site</scene> and <scene name='57/570615/Cv/6'>inhibited by the addition of a second weakly bound Zn<sup>+2</sup> at the α site</scene>. <scene name='57/570615/Cv/7'>Two sites together</scene>.<ref name="Ad">PMID:14736882</ref>
		+
		+	==3D structures of aminoacylase==
		+	[[Aminoacylase 3D structures]]
		+
	</StructureSection>		</StructureSection>
	==3D structures of D-aminoacylase==		==3D structures of D-aminoacylase==

	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}		Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
		+	{{#tree:id=OrganizedByTopic\|openlevels=0\|
		+
		+	*D-aminoacylase
		+
		+	**[[1m7j]], [[1v51]] – AfDAA + Zn – ''Alcaligenes faecalis''<br />
		+	**[[1rjq]], [[1rjr]], [[1v4y]] - AfDAA (mutant) + Zn <br />
		+	**[[1rjp]] - AfDAA + Zn + Cu<br />
		+	**[[1rk5]] - AfDAA (mutant) + Zn + Cu<br />
		+	**[[1rk6]] - AfDAA + Zn + Cd<br />

-	~~[[1m7j]], [[1v51]] – AfDAA + Zn – ''Alcaligenes faecalis''<br />~~	+	*L-aminoacylase or aspartoacylase
-	~~[[1rjq]], [[1rjr]], [[1v4y]]~~ - ~~AfDAA (mutant) + Zn <br />~~	+
-	~~[[1rjp]] - AfDAA + Zn + Cu<br />~~	+
-	~~[[1rk5]] - AfDAA (mutant) + Zn + Cu<br />~~	+
-	~~[[1rk6]] - AfDAA + Zn + Cd<br />~~	+

		+	**[[1q7l]] – hLAA 1 (mutant) + Zn - human<br />
		+	**[[2i3c]], [[2o53]], [[2q51]] – hLAA 2 + Zn <br />
		+	**[[2o4h]] – hLAA 2 + Zn + methyl-aspartate<br />
		+	**[[4mri]], [[4mxu]], [[4nfr]], [[4tnu]] – hLAA 2 (mutant) + Zn + methyl-aspartate<br />
		+	**[[2q4z]], [[2gu2]] – LAA 2 + Zn - rat<br />
		+	**[[3nh4]] – mLAA 3 + Zn + Cs – mouse <br />
		+	**[[3nh3]] – mLAA 3 (mutant) + Zn <br />
		+	**[[3nfz]] – mLAA 3 (mutant) + Zn + acetyl-tyrosine<br />
		+	**[[3nh8]] – mLAA 3 (mutant) + Zn + acetyl-cysteine<br />
		+	}}
	== References ==		== References ==
	<references/>		<references/>

	[[Category:Topic Page]]		[[Category:Topic Page]]

Jaime Prilusky: D-aminoacylase moved to Aminoacylase: requested by Editor

Jaime Prilusky — Mon, 27 May 2019 08:01:38 GMT

D-aminoacylase moved to Aminoacylase: requested by Editor

←Older revision

Revision as of 08:01, 27 May 2019

Alexander Berchansky at 10:05, 20 February 2019

Alexander Berchansky — Wed, 20 Feb 2019 10:05:13 GMT

←Older revision		Revision as of 10:05, 20 February 2019
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	== Structural highlights ==		== Structural highlights ==

-	AfDAA is catalytically activated by Zn<sup>+2</sup> <scene name='57/570615/Cv/2'>bound tightly at the β site</scene> and <scene name='57/570615/Cv/3'>inhibited by the addition of a second weakly bound Zn<sup>+2</sup> at the α site</scene>. <scene name='57/570615/Cv/4'>Two sites together</scene>.<ref name="Ad">PMID:14736882</ref>	+	AfDAA is catalytically activated by Zn<sup>+2</sup> <scene name='57/570615/Cv/5'>bound tightly at the β site</scene> and <scene name='57/570615/Cv/6'>inhibited by the addition of a second weakly bound Zn<sup>+2</sup> at the α site</scene>. <scene name='57/570615/Cv/7'>Two sites together</scene>.<ref name="Ad">PMID:14736882</ref>
	</StructureSection>		</StructureSection>
	==3D structures of D-aminoacylase==		==3D structures of D-aminoacylase==

Alexander Berchansky at 13:54, 27 December 2015

Alexander Berchansky — Sun, 27 Dec 2015 13:54:08 GMT

←Older revision		Revision as of 13:54, 27 December 2015
Line 2:		Line 2:
	== Function ==		== Function ==

-	'''D-aminoacylase''' (DAA) hydrolyzes N-acyl neutral D-amino acids. DAA was found in different genera of bacteria: ''Pseudomonas'', ''Streptomyces'' and ''Alcaligenes''. Each genera has a different substrate preference. DAA from ''Alcaligenes faecalis'' (AfDAA) shows preference for D-Met, D-Phe and D-Leu and lesser effectivity for D-Trp, D-Ala and D-val. AfDAA is a zinc-assisted enzyme. <ref>PMID:14736882</ref>	+	'''D-aminoacylase''' (DAA) hydrolyzes N-acyl neutral D-amino acids. DAA was found in different genera of bacteria: ''Pseudomonas'', ''Streptomyces'' and ''Alcaligenes''. Each genera has a different substrate preference. DAA from ''Alcaligenes faecalis'' (AfDAA) shows preference for D-Met, D-Phe and D-Leu and lesser effectivity for D-Trp, D-Ala and D-val. AfDAA is a zinc-assisted enzyme. <ref name="Ad">PMID:14736882</ref>

	== Structural highlights ==		== Structural highlights ==

-	AfDAA is catalytically activated by Zn<sup>+2</sup> <scene name='57/570615/Cv/2'>bound tightly at the β site</scene> and <scene name='57/570615/Cv/3'>inhibited by the addition of a second weakly bound Zn<sup>+2</sup> at the α site</scene>. <scene name='57/570615/Cv/4'>Two sites together</scene>.	+	AfDAA is catalytically activated by Zn<sup>+2</sup> <scene name='57/570615/Cv/2'>bound tightly at the β site</scene> and <scene name='57/570615/Cv/3'>inhibited by the addition of a second weakly bound Zn<sup>+2</sup> at the α site</scene>. <scene name='57/570615/Cv/4'>Two sites together</scene>.<ref name="Ad">PMID:14736882</ref>
	</StructureSection>		</StructureSection>
	==3D structures of D-aminoacylase==		==3D structures of D-aminoacylase==

Alexander Berchansky at 13:51, 27 December 2015

Alexander Berchansky — Sun, 27 Dec 2015 13:51:03 GMT

←Older revision		Revision as of 13:51, 27 December 2015
Line 6:		Line 6:
	== Structural highlights ==		== Structural highlights ==

-	AfDAA is catalytically activated by Zn<sup>+2</sup> bound tightly at the β site and inhibited by the addition of a second weakly bound Zn<sup>+2</sup> at the α site.	+	AfDAA is catalytically activated by Zn<sup>+2</sup> <scene name='57/570615/Cv/2'>bound tightly at the β site</scene> and <scene name='57/570615/Cv/3'>inhibited by the addition of a second weakly bound Zn<sup>+2</sup> at the α site</scene>. <scene name='57/570615/Cv/4'>Two sites together</scene>.
	</StructureSection>		</StructureSection>
	==3D structures of D-aminoacylase==		==3D structures of D-aminoacylase==

Alexander Berchansky at 13:35, 27 December 2015

Alexander Berchansky — Sun, 27 Dec 2015 13:35:48 GMT

←Older revision		Revision as of 13:35, 27 December 2015
Line 1:		Line 1:
-	<StructureSection load='1v51' size='350' side='right' caption='Structure of D-aminoacylase with Zn+2 ions (grey) and acetate (PDB entry [[1v51]])' scene=''>	+	<StructureSection load='1v51' size='350' side='right' caption='Structure of D-aminoacylase with Zn+2 ions (grey) and acetate (PDB entry [[1v51]])' scene='57/570615/Cv/1'>
	== Function ==		== Function ==

Michal Harel at 07:30, 23 December 2015

Michal Harel — Wed, 23 Dec 2015 07:30:44 GMT

←Older revision		Revision as of 07:30, 23 December 2015
Line 2:		Line 2:
	== Function ==		== Function ==

-	'''D-aminoacylase''' (DAA) hydrolyzes N-acyl neutral D-amino acids. DAA from ''Alcaligenes faecalis'' (AfDAA) shows preference for D-Met, D-Phe and D-Leu and lesser effectivity for D-Trp, D-Ala and D-val. AfDAA is a zinc-assisted enzyme. <ref>PMID:14736882</ref>	+	'''D-aminoacylase''' (DAA) hydrolyzes N-acyl neutral D-amino acids. DAA was found in different genera of bacteria: ''Pseudomonas'', ''Streptomyces'' and ''Alcaligenes''. Each genera has a different substrate preference. DAA from ''Alcaligenes faecalis'' (AfDAA) shows preference for D-Met, D-Phe and D-Leu and lesser effectivity for D-Trp, D-Ala and D-val. AfDAA is a zinc-assisted enzyme. <ref>PMID:14736882</ref>

	== Structural highlights ==		== Structural highlights ==

Joel L. Sussman at 11:21, 22 December 2015

Joel L. Sussman — Tue, 22 Dec 2015 11:21:38 GMT

←Older revision		Revision as of 11:21, 22 December 2015
Line 2:		Line 2:
	== Function ==		== Function ==

-	'''D-aminoacylase''' (DAA) hydrolyzes N-acyl neutral D-amino acids. DAA from ''Alcaligenes faecalis'' (AfDAA) shows preference for D-Met, D-Phe and D-Leu and lesser effectivity for D-Trp, D-Ala and D-val. ~~DAA~~ is a zinc-assisted enzyme. <ref>PMID:14736882</ref>	+	'''D-aminoacylase''' (DAA) hydrolyzes N-acyl neutral D-amino acids. DAA from ''Alcaligenes faecalis'' (AfDAA) shows preference for D-Met, D-Phe and D-Leu and lesser effectivity for D-Trp, D-Ala and D-val. AfDAA is a zinc-assisted enzyme. <ref>PMID:14736882</ref>

	== Structural highlights ==		== Structural highlights ==

Joel L. Sussman at 11:21, 22 December 2015

Joel L. Sussman — Tue, 22 Dec 2015 11:21:09 GMT

←Older revision		Revision as of 11:21, 22 December 2015
Line 2:		Line 2:
	== Function ==		== Function ==

-	'''D-aminoacylase''' (DAA) hydrolyzes N-acyl neutral D-amino acids. DAA from ''Alcaligenes faecalis'' shows preference for D-Met, D-Phe and D-Leu and lesser effectivity for D-Trp, D-Ala and D-val. DAA is a zinc-assisted enzyme. <ref>PMID:14736882</ref>	+	'''D-aminoacylase''' (DAA) hydrolyzes N-acyl neutral D-amino acids. DAA from ''Alcaligenes faecalis'' (AfDAA) shows preference for D-Met, D-Phe and D-Leu and lesser effectivity for D-Trp, D-Ala and D-val. DAA is a zinc-assisted enzyme. <ref>PMID:14736882</ref>

	== Structural highlights ==		== Structural highlights ==

-	~~''Alcaligenes faecalis'' DAA (~~AfDAA) is catalytically activated by Zn<sup>+2</sup> bound tightly at the β site and inhibited by the addition of a second weakly bound Zn<sup>+2</sup> at the α site.	+	AfDAA is catalytically activated by Zn<sup>+2</sup> bound tightly at the β site and inhibited by the addition of a second weakly bound Zn<sup>+2</sup> at the α site.
	</StructureSection>		</StructureSection>
	==3D structures of D-aminoacylase==		==3D structures of D-aminoacylase==