Structural insight into dihydrodipicolinate reductase from corybebacterium glutamicum for lysine biosynthesis

Journal of Microbiology and Biotechnology

Volumn 26, Issue 2, 2015, Pages 226-232

  Sagong, Hye Young ^a   Kim, Kyung Jin ^a  

^a Kyungpook National University   (South Korea)

Author keywords

Corynebacterium glutamicum; Dihydrodipicolinate reductase; L lysine

Indexed keywords

DIHYDRODIPICOLINATE REDUCTASE; LYSINE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SULFATE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE;

AMINO ACID SYNTHESIS; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; COMPARATIVE STUDY; CORYNEBACTERIUM GLUTAMICUM; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME COFACTOR BINDING; ENZYME CONFORMATION; ENZYME SUBSTRATE COMPLEX; MOLECULAR BIOLOGY; MYCOBACTERIUM TUBERCULOSIS; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; BIOCATALYSIS; BIOSYNTHESIS; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; KINETICS; METABOLISM; MOLECULAR MODEL; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BINDING SITES; BIOCATALYSIS; CORYNEBACTERIUM GLUTAMICUM; CRYSTALLOGRAPHY, X-RAY; DIHYDRODIPICOLINATE REDUCTASE; KINETICS; LYSINE; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; NAD; NADP; OXIDOREDUCTASES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SUBSTRATE SPECIFICITY;

EID: 84975778601     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.1508.08086     Document Type: Article

References (20)

1. Brünger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, et al. 1998. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54: 905-921
2. Cirilli M, Zheng R, Scapin G, Blanchard JS. 2003. The threedimensional structures of the Mycobacterium tuberculosis dihydrodipicolinate reductase-NADH-2,6-PDC and-NADPH-2,6-PDC complexes. Structural and mutagenic analysis of relaxed nucleotide specificity. Biochemistry 42: 10644-10650
3. Emsley P, Cowtan K. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60: 2126-2132
4. Ikeda M, Nakagawa S 2003. The Corynebacterium glutamicum genome: features and impacts on biotechnological processes. Appl. Microbiol. Biotechnol. 62: 99-109
5. Ikeda M, Takeno S. 2013. Amino acid production by Corynebacterium glutamicum, pp. 107-147. In: Corynebacterium glutamicum. Springer
6. Kalinowski J, Bathe B, Bartels D, Bischoff N, Bott M, Burkovski A, et al. 2003. The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins. J. Biotechnol. 104: 5-25
7. Kinoshita S, Udaka S, Shimono M. 2004. Studies on the amino acid fermentation. Part 1. Production of L-glutamic acid by various microorganisms. J. Gen. Appl. Microbiol. 50: 331-343
8. Lesk AM. 1995. NAD-binding domains of dehydrogenases. Curr. Opin. Struct. Biol. 5: 775-783
9. Male KB, Storey KB. 1982. Regulation of coenzyme utilization by bovine liver glutamate dehydrogenase: investigations using thionicotinamide analogues of NAD and NADP in a dual wavelength assay. Int. J. Biochem. 14: 1083-1089
10. Matthews BW. 1968. Solvent content of protein crystals. J. Mol. Biol. 33: 491-497
11. McCoy AJ, Adams NE, Hudson AO, Gilvarg C, Leustek T, Maurelli AT. 2006. L,L-Diaminopimelate aminotransferase, a trans-kingdom enzyme shared by Chlamydia and plants for synthesis of diaminopimelate/lysine. Proc. N atl. A cad. S ci. USA 103: 17909-17914
12. Murshudov GN, Vagin AA, Dodson EJ. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53: 240-255
13. Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276: 307-326
14. Pavelka M, Jacobs WR. 1996. Biosynthesis of diaminopimelate, the precursor of lysine and a component of peptidoglycan, is an essential function of Mycobacterium smegmatis. J. Bacteriol. 178: 6496-6507
15. Purich DL. 2009. Advances in Enzymology and Related Areas of Molecular Biology, Amino Acid Metabolism. Vol 72. John Wiley & Sons
16. Rossman MG, Liljas A, Brandén CI, Banaszak LJ. 1975. Evolutionary and structural relationships among dehydrogenases, pp. 61-102. In Boyer PD (ed.). The Enzymes, 3rd Ed. Vol. XI. Academic Press, NY
17. Schrumpf B, Schwarzer A, Kalinowski J, Pühler A, Eggeling L, Sahm H. 1991. A functionally split pathway for lysine synthesis in Corynebacterium glutamicium. J. Bacteriol. 173: 4510-4516
18. Schulz GE. 1992. Binding of nucleotides by proteins: Current opinion in structural biology 1992, 2: 61…-67. Curr. Opin. Struct. Biol. 2: 61-67
19. Vagin A, Teplyakov A. 2009. Molecular replacement with MOLREP. Acta Crystallogr. D Biol. Crystallogr. 66: 22-25
20. Yeh P, Sicard AM, Sinskey AJ. 1988. General organization of the genes specifically involved in the diaminopimelate-lysine biosynthetic pathway of Corynebacterium glutamicum. Mol. Gen. Genet. 212: 105-111.