Contribution of Lys276 to the conformational flexibility of the active site of glutamate decarboxylase fromEscherichia coli-Reference-Cited by-同舟云学术

Contribution of Lys276 to the conformational flexibility of the active site of glutamate decarboxylase fromEscherichia coli

Published:2002-09-27 Issue:20 Volume:269 Page:4913-4920
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:

Author:

Tramonti Angela,John Robert A.,Bossa Francesco,De Biase Daniela

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1432-1033.2002.03149.x/fullpdf

Reference32 articles.

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3. Lysine 87 in the β subunit of tryptophan synthase that forms an internal aldimine with pyridoxal phosphate serves critical roles in transamination, catalysis and product release;Lu;J. Biol. Chem.,1993

4. Effect of substituion of a lysyl residue that binds pyridoxal phosphate in thermostable d-amino acid aminotransferase by arginine and alanine;Nishimura;Biochemistry,1991

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