Convergent evolution of nitrogen-adding enzymes in the purine nucleotide biosynthetic pathway, based on structural analysis of adenylosuccinate synthetase (PurA)-Reference-Cited by-同舟云学术

Convergent evolution of nitrogen-adding enzymes in the purine nucleotide biosynthetic pathway, based on structural analysis of adenylosuccinate synthetase (PurA)

Published:2023 Issue:2 Volume:69 Page:109-116
ISSN:0022-1260
Container-title:The Journal of General and Applied Microbiology
language:en
Short-container-title:J. Gen. Appl. Microbiol.

Author:

Sampei Gen-ichi¹,Ishii Hironori¹,Taka Hiroyuki¹,Kawai Gota²

Affiliation:

1. Department of Engineering Science, Graduate School of Informatics and Engineering, The University of Electro-Communications

2. Department of Life Science, Faculty of Advanced Engineering, Chiba Institute of Technology

Publisher

Microbiology Research Foundation

Subject

Applied Microbiology and Biotechnology,Microbiology

Link

https://www.jstage.jst.go.jp/article/jgam/69/2/69_2023.05.002/_pdf

Reference37 articles.

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2. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P. et al. (1998) Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Cryst., D54, 905-921.

3. Buchanan, J. M. (1973) The amidotransferases. Adv. Enzymol. Relat. Areas Mol. Biol., 21, 199-261.

4. Dong, Q. and Fromm, H. J. (1990) Chemical modification of adenylosuccinate synthetase from Escherichia coli by pyridoxal 5'-phosphate. Identification of an active site lysyl residue. J. Biol. Chem., 265, 6235-6240.

5. Dong, Q., Liu, F., Myers, A. M., and Fromm, H. J. (1991) Evidence for an arginine residue at the substrate binding site of Escherichia coli adenylosuccinate synthetase as studied by chemical modification and site-directed mutagenesis. J. Biol. Chem., 266, 12228-12233.

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