1onw

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[[Image:1onw.png|left|200px]]
 
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{{STRUCTURE_1onw| PDB=1onw | SCENE= }}
{{STRUCTURE_1onw| PDB=1onw | SCENE= }}
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===Crystal structure of Isoaspartyl Dipeptidase from E. coli===
===Crystal structure of Isoaspartyl Dipeptidase from E. coli===
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{{ABSTRACT_PUBMED_12718528}}
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==Function==
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[[http://www.uniprot.org/uniprot/IADA_ECOLI IADA_ECOLI]] Catalyzes the hydrolytic cleavage of a subset of L-isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. The best substrate for the enzyme reported thus far is iso-Asp-Leu.<ref>PMID:7876157</ref> <ref>PMID:4880759</ref> <ref>PMID:12718528</ref> <ref>PMID:15882050</ref>
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{{ABSTRACT_PUBMED_12718528}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:012718528</ref><references group="xtra"/>
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<ref group="xtra">PMID:012718528</ref><references group="xtra"/><references/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Holden, H M.]]
[[Category: Holden, H M.]]

Revision as of 11:04, 16 April 2014

Template:STRUCTURE 1onw

Contents

Crystal structure of Isoaspartyl Dipeptidase from E. coli

Template:ABSTRACT PUBMED 12718528

Function

[IADA_ECOLI] Catalyzes the hydrolytic cleavage of a subset of L-isoaspartyl (L-beta-aspartyl) dipeptides. Used to degrade proteins damaged by L-isoaspartyl residues formation. The best substrate for the enzyme reported thus far is iso-Asp-Leu.[1] [2] [3] [4]

About this Structure

1onw is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Thoden JB, Marti-Arbona R, Raushel FM, Holden HM. High-resolution X-ray structure of isoaspartyl dipeptidase from Escherichia coli. Biochemistry. 2003 May 6;42(17):4874-82. PMID:12718528 doi:http://dx.doi.org/10.1021/bi034233p
  1. ↑ Gary JD, Clarke S. Purification and characterization of an isoaspartyl dipeptidase from Escherichia coli. J Biol Chem. 1995 Feb 24;270(8):4076-87. PMID:7876157
  2. ↑ Haley EE. Purification and properties of a beta-aspartyl peptidase from Escherichia coli. J Biol Chem. 1968 Nov 10;243(21):5748-52. PMID:4880759
  3. ↑ Thoden JB, Marti-Arbona R, Raushel FM, Holden HM. High-resolution X-ray structure of isoaspartyl dipeptidase from Escherichia coli. Biochemistry. 2003 May 6;42(17):4874-82. PMID:12718528 doi:http://dx.doi.org/10.1021/bi034233p
  4. ↑ Marti-Arbona R, Fresquet V, Thoden JB, Davis ML, Holden HM, Raushel FM. Mechanism of the reaction catalyzed by isoaspartyl dipeptidase from Escherichia coli. Biochemistry. 2005 May 17;44(19):7115-24. PMID:15882050 doi:10.1021/bi050008r

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