Rajaram, V and Prasad, K and Prasuna, Ratna P and Ramachandra, N and Bharath, SR and Savithri, HS and Murthy, MRN (2006) Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of the biosynthetic N-acetylornithine aminotransferases from Salmonella typhimurium and Escherichia coli. In: Acta Crystallographica Section F, 62 (10). pp. 980-983.
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Acetylornithine aminotransferase (AcOAT) is a type I pyridoxal 5\prime-phosphate-dependent enzyme catalyzing the conversion of N-acetylglutamic semialdehyde to N-acetylornithine in the presence of \alpha-ketoglutarate, a step involved in arginine metabolism. In Escherichia coli, the biosynthetic AcOAT also catalyzes the conversion of N-succinyl-L-2-amino-6-oxopimelate to N-succinyl-L,L-diaminopimelate, one of the steps in lysine biosynthesis. It is closely related to ornithine aminotransferase. AcOATwas cloned from Salmonella typhimurium and E. coli, overexpressed in E. coli and purified using Ni–NTA affinity column chromatography. The enzymes crystallized in the presence of gabaculine. Crystals of E. coli AcOAT (eAcOAT) only diffracted X-rays to 3.5\AA and were twinned. The crystals of S. typhimurium AcOAT (sAcOAT) diffracted to 1.9 \AA and had a dimer in the asymmetric unit. The structure of sAcOAT was solved by the molecular-replacement method.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Blackwell Synergy|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit
Division of Biological Sciences > Biochemistry
|Date Deposited:||22 Nov 2006|
|Last Modified:||19 Sep 2010 04:32|
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