NDLI: The structure of NtdA, a sugar aminotransferase involved in the kanosamine biosynthetic pathway in Bacillus subtilis, reveals a new subclass of aminotransferases.

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The structure of NtdA, a sugar aminotransferase involved in the kanosamine biosynthetic pathway in Bacillus subtilis, reveals a new subclass of aminotransferases.

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The structure of NtdA, a sugar aminotransferase involved in the kanosamine biosynthetic pathway in Bacillus subtilis, reveals a new subclass of aminotransferases.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Van Straaten, Karin E. Sanders, David A. R. Anjum, Shazia Jagdhane, Rajendra Palmer, David R. J. Ko, Jong Bum
Description	Author Affiliation: van Straaten KE ( From the Department of Chemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5C9, Canada.)
Abstract	NtdA from Bacillus subtilis is a sugar aminotransferase that catalyzes the pyridoxal phosphate-dependent equatorial transamination of 3-oxo- -D-glucose 6-phosphate to form -D-kanosamine 6-phosphate. The crystal structure of NtdA shows that NtdA shares the common aspartate aminotransferase fold (Type 1) with residues from both monomers forming the active site. The crystal structures of NtdA alone, co-crystallized with the product -D-kanosamine 6-phosphate, and incubated with the amine donor glutamate reveal three key structures in the mechanistic pathway of NtdA. The structure of NtdA alone reveals the internal aldimine form of NtdA with the cofactor pyridoxal phosphate covalently attached to Lys-247. The addition of glutamate results in formation of pyridoxamine phosphate. Co-crystallization with kanosamine 6-phosphate results in the formation of the external aldimine. Only -D-kanosamine 6-phosphate is observed in the active site of NtdA, not the ß-anomer. A comparison of the structure and sequence of NtdA with other sugar aminotransferases enables us to propose that the VIß family of aminotransferases should be divided into subfamilies based on the catalytic lysine motif.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	47
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-11-22
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacillus Subtilis Enzymology Bacterial Proteins Chemistry Transaminases Amino Acid Motifs Metabolism Catalytic Domain Crystallography, X-Ray Glucosamine Biosynthesis Pyridoxal Phosphate Pyridoxamine Analogs & Derivatives Structural Homology, Protein Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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