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Start Over Descriptor "Phosphotransferases (Carboxyl Group Acceptor) biosynthesis" Topic amino-acid n-acetyltransferase

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1 results on '"Phosphotransferases (Carboxyl Group Acceptor) biosynthesis"'

1. Expression, crystallization and preliminary crystallographic studies of a novel bifunctional N-acetylglutamate synthase/kinase from Xanthomonas campestris homologous to vertebrate N-acetylglutamate synthase.

Author

Shi D, Caldovic L, Jin Z, Yu X, Qu Q, Roth L, Morizono H, Hathout Y, Allewell NM, and Tuchman M

Subjects
Amino-Acid N-Acetyltransferase biosynthesis, Crystallization, Crystallography, X-Ray, Multienzyme Complexes biosynthesis, Phosphotransferases (Carboxyl Group Acceptor) biosynthesis, Recombinant Proteins biosynthesis, Selenomethionine metabolism, Amino-Acid N-Acetyltransferase chemistry, Multienzyme Complexes chemistry, Phosphotransferases (Carboxyl Group Acceptor) chemistry, Xanthomonas campestris enzymology
Abstract

A novel N-acetylglutamate synthase/kinase bifunctional enzyme of arginine biosynthesis that was homologous to vertebrate N-acetylglutamate synthases was identified in Xanthomonas campestris. The protein was overexpressed, purified and crystallized. The crystals belong to the hexagonal space group P6(2)22, with unit-cell parameters a = b = 134.60, c = 192.11 A, and diffract to about 3.0 A resolution. Selenomethionine-substituted recombinant protein was produced and selenomethionine substitution was verified by mass spectroscopy. Multiple anomalous dispersion (MAD) data were collected at three wavelengths at SER-CAT, Advanced Photon Source, Argonne National Laboratory. Structure determination is under way using the MAD phasing method.

Published
2006
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