1fy2

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m (Protected "1fy2" [edit=sysop:move=sysop])
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[[Image:1fy2.png|left|200px]]
 
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{{STRUCTURE_1fy2| PDB=1fy2 | SCENE= }}
{{STRUCTURE_1fy2| PDB=1fy2 | SCENE= }}
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===Aspartyl Dipeptidase===
===Aspartyl Dipeptidase===
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{{ABSTRACT_PUBMED_11106384}}
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==Function==
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[[http://www.uniprot.org/uniprot/PEPE_SALTY PEPE_SALTY]] Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.[HAMAP-Rule:MF_00510]
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{{ABSTRACT_PUBMED_11106384}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:011106384</ref><references group="xtra"/>
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<ref group="xtra">PMID:011106384</ref><references group="xtra"/><references/>
[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
[[Category: Salmonella enterica subsp. enterica serovar typhimurium]]
[[Category: Hakansson, K.]]
[[Category: Hakansson, K.]]

Revision as of 11:08, 16 April 2014

Template:STRUCTURE 1fy2

Contents

Aspartyl Dipeptidase

Template:ABSTRACT PUBMED 11106384

Function

[PEPE_SALTY] Hydrolyzes dipeptides containing N-terminal aspartate residues. May play a role in allowing the cell to use peptide aspartate to spare carbon otherwise required for the synthesis of the aspartate family of amino acids.[HAMAP-Rule:MF_00510]

About this Structure

1fy2 is a 1 chain structure with sequence from Salmonella enterica subsp. enterica serovar typhimurium. Full crystallographic information is available from OCA.

Reference

  • Hakansson K, Wang AH, Miller CG. The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad. Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14097-102. PMID:11106384 doi:10.1073/pnas.260376797

Proteopedia Page Contributors and Editors (what is this?)

OCA

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