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Int. J. Mol. Sci. 2016, 17(4), 446; doi:10.3390/ijms17040446

Structure of the PLP-Form of the Human Kynurenine Aminotransferase II in a Novel Spacegroup at 1.83 Å Resolution

1
Group in Biomolecular Structure and Informatics, Faculty of Pharmacy, University of Sydney, Sydney, NSW 2006, Australia
2
MX Beamlines, Australian Synchrotron, 800 Blackburn Road, Clayton, VIC 3168, Australia
3
Faculty of Pharmacy, University of Sydney, Sydney, NSW 2006, Australia
*
Author to whom correspondence should be addressed.
Academic Editor: Charles A. Collyer
Received: 12 February 2016 / Revised: 10 March 2016 / Accepted: 22 March 2016 / Published: 25 March 2016
(This article belongs to the Section Biochemistry, Molecular and Cellular Biology)
View Full-Text   |   Download PDF [2100 KB, uploaded 25 March 2016]   |  

Abstract

Kynurenine aminotransferase II (KAT-II) is a 47 kDa pyridoxal phosphate (PLP)-dependent enzyme, active as a homodimer, which catalyses the transamination of the amino acids kynurenine (KYN) and 3-hydroxykynurenine (3-HK) in the tryptophan pathway, and is responsible for producing metabolites that lead to kynurenic acid (KYNA), which is implicated in several neurological diseases such as schizophrenia. In order to fully describe the role of KAT-II in the pathobiology of schizophrenia and other brain disorders, the crystal structure of full-length PLP-form hKAT-II was determined at 1.83 Å resolution, the highest available. The electron density of the active site reveals an aldimine linkage between PLP and Lys263, as well as the active site residues, which characterize the fold-type I PLP-dependent enzymes. View Full-Text
Keywords: kynurenine aminotransferase; crystal structure; neurodegenerative diseases; pyridoxal phosphate (PLP) kynurenine aminotransferase; crystal structure; neurodegenerative diseases; pyridoxal phosphate (PLP)
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Nematollahi, A.; Sun, G.; Harrop, S.J.; Hanrahan, J.R.; Church, W.B. Structure of the PLP-Form of the Human Kynurenine Aminotransferase II in a Novel Spacegroup at 1.83 Å Resolution. Int. J. Mol. Sci. 2016, 17, 446.

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