1fy2: Difference between revisions
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{{STRUCTURE_1fy2| PDB=1fy2 | SCENE= }} | {{STRUCTURE_1fy2| PDB=1fy2 | SCENE= }} | ||
===Aspartyl Dipeptidase=== | ===Aspartyl Dipeptidase=== | ||
{{ABSTRACT_PUBMED_11106384}} | |||
==Function== | |||
[[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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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:011106384</ref><references group="xtra"/> | <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
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
