4bht: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4bht|  PDB=4bht  |  SCENE=  }}
===Structural Determinants of Cofactor Specificity and Domain Flexibility in Bacterial Glutamate Dehydrogenases===


The entry 4bht is ON HOLD
==Function==
[[http://www.uniprot.org/uniprot/DHE4_ECOLI DHE4_ECOLI]] Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia.<ref>PMID:235298</ref> <ref>PMID:241744</ref> 


Authors: Oliveira, T., Sharkey, M., Engel, P., Khan, A.
==About this Structure==
[[4bht]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2yfg 2yfg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BHT OCA].  


Description: Structural Determinants of Cofactor Specificity and Domain Flexibility in Bacterial Glutamate Dehydrogenases
==Reference==
<references group="xtra"/><references/>
[[Category: Escherichia coli]]
[[Category: Engel, P.]]
[[Category: Khan, A.]]
[[Category: Oliveira, T.]]
[[Category: Sharkey, M.]]
[[Category: Oxidoreductase]]

Revision as of 13:18, 19 June 2013

Template:STRUCTURE 4bht

Structural Determinants of Cofactor Specificity and Domain Flexibility in Bacterial Glutamate Dehydrogenases

Function

[DHE4_ECOLI] Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia.[1] [2]

About this Structure

4bht is a 6 chain structure with sequence from Escherichia coli. This structure supersedes the now removed PDB entry 2yfg. Full crystallographic information is available from OCA.

Reference

  1. ↑ Veronese FM, Boccu E, Conventi L. Glutamate dehydrogenase from Escherichia coli: induction, purification and properties of the enzyme. Biochim Biophys Acta. 1975 Feb 19;377(2):217-28. PMID:235298
  2. ↑ Sakamoto N, Kotre AM, Savageau MA. Glutamate dehydrogenase from Escherichia coli: purification and properties. J Bacteriol. 1975 Nov;124(2):775-83. PMID:241744

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