3pdx
From Proteopedia
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{{STRUCTURE_3pdx| PDB=3pdx | SCENE= }} | {{STRUCTURE_3pdx| PDB=3pdx | SCENE= }} | ||
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===Crystal structural of mouse tyrosine aminotransferase=== | ===Crystal structural of mouse tyrosine aminotransferase=== | ||
+ | {{ABSTRACT_PUBMED_21153519}} | ||
- | + | ==Function== | |
- | + | [[http://www.uniprot.org/uniprot/ATTY_MOUSE ATTY_MOUSE]] Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity for phenylalanine. | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:021153519</ref><references group="xtra"/><references/> |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Tyrosine transaminase]] | [[Category: Tyrosine transaminase]] | ||
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[[Category: Mehere, P V.]] | [[Category: Mehere, P V.]] | ||
[[Category: Robinson, H.]] | [[Category: Robinson, H.]] | ||
+ | [[Category: Alpha/bata protein]] | ||
+ | [[Category: Aminotransferase]] | ||
+ | [[Category: Plp-binding]] | ||
+ | [[Category: Transferase]] |
Revision as of 08:25, 2 May 2013
Contents |
Crystal structural of mouse tyrosine aminotransferase
Template:ABSTRACT PUBMED 21153519
Function
[ATTY_MOUSE] Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity for phenylalanine.
About this Structure
3pdx is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
- Mehere P, Han Q, Lemkul JA, Vavricka CJ, Robinson H, Bevan DR, Li J. Tyrosine aminotransferase: biochemical and structural properties and molecular dynamics simulations. Protein Cell. 2010 Nov;1(11):1023-32. Epub 2010 Dec 10. PMID:21153519 doi:10.1007/s13238-010-0128-5