Literature: Asp/Glu racemase, active site 1 (IPR018187)
References used in this entry
The following publications were referred to in the abstract:
Purification, cloning, and cofactor independence of glutamate racemase from Lactobacillus.
Gallo KA, Knowles JR.
Biochemistry 32 3981-90 1993
PMID: 8385993 Related citations
The following publications were not referred to in the abstract, but provide useful additional information:
Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications for inhibitor design.
May M, Mehboob S, Mulhearn DC, Wang Z, Yu H, Thatcher GR, Santarsiero BD, Johnson ME, Mesecar AD.
J. Mol. Biol. 371 1219-37 2007
PMID: 17610893 Related citations
Structure of aspartate racemase complexed with a dual substrate analogue, citric acid, and implications for the reaction mechanism.
Ohtaki A, Nakano Y, Iizuka R, Arakawa T, Yamada K, Odaka M, Yohda M.
Proteins 70 1167-74 2008
PMID: 17847084 Related citations
Structural basis for glutamate racemase inhibition.
Kim KH, Bong YJ, Park JK, Shin KJ, Hwang KY, Kim EE.
J. Mol. Biol. 372 434-43 2007
PMID: 17658548 Related citations
Exploitation of structural and regulatory diversity in glutamate racemases.
Lundqvist T, Fisher SL, Kern G, Folmer RH, Xue Y, Newton DT, Keating TA, Alm RA, de Jonge BL.
Nature 447 817-22 2007
PMID: 17568739 Related citations
Substrate-induced conformational changes in Bacillus subtilis glutamate racemase and their implications for drug discovery.
Ruzheinikov SN, Taal MA, Sedelnikova SE, Baker PJ, Rice DW.
Structure 13 1707-13 2005
PMID: 16271894 Related citations