An activator for pyruvoyl-dependent l-aspartate α-decarboxylase is conserved in a small group of the γ-proteobacteria including Escherichia coli

MicrobiologyOpen

Volumn 1, Issue 3, 2012, Pages 298-310

  Nozaki, Shingo ^a   Webb, Michael E ^b   Niki, Hironori ^a,c  

^a NATIONAL INSTITUTE OF GENETICS   (Japan)

^b UNIVERSITY OF LEEDS   (United Kingdom)

^c GRADUATE UNIVERSITY FOR ADVANCED STUDIES   (Japan)

Author keywords

alanine; ADC; Coenzyme A; PanD; Pantothenate; YhhK

Indexed keywords

ACYLTRANSFERASE; ALANINE; ASPARAGINE; ASPARTATE ALPHA DECARBOXYLASE; CARBOXYLYASE; ENZYME PRECURSOR; ESCHERICHIA COLI PROTEIN; PANTOTHENIC ACID; PROTEIN PANZ; UNCLASSIFIED DRUG;

AMINO ACID SYNTHESIS; ARTICLE; BACTERIAL GENE; BACTERIAL METABOLISM; BINDING AFFINITY; BIOSYNTHESIS; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME REGULATION; ESCHERICHIA COLI; GAMMAPROTEOBACTERIA; GENETIC CONSERVATION; IN VITRO STUDY; IN VIVO STUDY; KLEBSIELLA; NONHUMAN; PAND GENE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CLEAVAGE; PROTEIN DOMAIN; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; SALMONELLA; SHIGELLA; SITE DIRECTED MUTAGENESIS; YERSINIA;

EID: 84884212615     PISSN: None     EISSN: 20458827     Source Type: Journal    
DOI: 10.1002/mbo3.34     Document Type: Article

References (28)

1. Adams, M. D., L. M. Wagner, T. J. Graddis, R. Landick, T. K. Antonucci, A. L. Gibson, et al.1990. Nucleotide sequence and genetic characterization reveal six essential genes for the LIV-I and LS transport systems of Escherichia coli. J. Biol. Chem. 265:11436-11443.
2. Albert, A., V. Dhanaraj, U. Genschel, G. Khan, M. K. Ramjee, R. Pulido, et al.1998. Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing. Nat. Struct. Biol. 5:289-293.
3. Baba, T., T. Ara, M. Hasegawa, Y. Takai, Y. Okumura, M. Baba, et al.2006. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol. Syst. Biol. 2:8.
4. Brown, G. M. 1959. The metabolism of pantothenic acid. J. Biol. Chem. 234:370-378.
5. Chakauya, E., K. M. Coxon, M. Wei, M. V. Macdonald, T. Barsby, C. Abell, et al.2008. Towards engineering increased pantothenate (vitamin B(5)) levels in plants. Plant Mol. Biol. 68:493-503.
6. Cronan, J. E., Jr.. 1980. Β-alanine synthesis in Escherichia coli. J. Bacteriol. 141:1291-1297.
7. Cronan, J. E. Jr, K. J. Littel, and S. Jackowski 1982. Genetic and biochemical analyses of pantothenate biosynthesis in Escherichia coli and Salmonella typhimurium. J. Bacteriol. 149:916-922.
8. Datsenko, K. A., and B. L. Wanner 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
9. Dusch, N., A. Puhler, and J. Kalinowski 1999. Expression of the Corynebacterium glutamicum PanD gene encoding L-aspartate-α-decarboxylase leads to pantothenate overproduction in Escherichia coli. Appl. Environ. Microbiol. 65:1530-1539.
10. Fouad, W. M., and B. Rathinasabapathi 2006. Expression of bacterial L-aspartate-α-decarboxylase in tobacco increases β-alanine and pantothenate levels and improves thermotolerance. Plant Mol. Biol. 60:495-505.
11. Guzman, L. M., D. Belin, M. J. Carson, and J. Beckwith 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130.
12. Jackowski, S., and C. O. Rock 1981. Regulation of coenzyme A biosynthesis. J. Bacteriol. 148:926-932.
13. Joyce, A. R., J. L. Reed, A. White, R. Edwards, A. Osterman, T. Baba, et al.2006. Experimental and computational assessment of conditionally essential genes in Escherichia coli. J. Bacteriol. 188:8259-8271.
14. Karimova, G., J. Pidoux, A. Ullmann, and D. Ladant 1998. A bacterial two-hybrid system based on a reconstituted signal transduction pathway. Proc. Natl. Acad. Sci. USA 95:5752-5756.
15. Kitagawa, M., T. Ara, M. Arifuzzaman, T. Ioka-Nakamichi, E. Inamoto, H. Toyonaga, et al.2005. Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res. 12:291-299.
16. Ortega, M. V., A. Cardenas, and D. Ubiera 1975. PanD, a new chromosomal locus of Salmonella typhimurium for the biosynthesis of β-alanine. Mol. Gen. Genet. 140:159-164.
17. van Poelje, P. D., and E. E. Snell 1990. Pyruvoyl-dependent enzymes. Annu. Rev. Biochem. 59:29-59.
18. Primerano, D. A., and R. O. Burns 1983. Role of acetohydroxy acid isomeroreductase in biosynthesis of pantothenic acid in Salmonella typhimurium. J. Bacteriol. 153:259-269.
19. Ramjee, M. K., U. Genschel, C. Abell, and A. G. Smith 1997. Escherichia coli L-aspartate-α-decarboxylase: preprotein processing and observation of reaction intermediates by electrospray mass spectrometry. Biochem. J. 323(Pt 3):661-669.
20. Schmitzberger, F., M. L. Kilkenny, C. M. Lobley, M. E. Webb, M. Vinkovic, D. Matak-Vinkovic, et al.2003. Structural constraints on protein self-processing in L-aspartate-α-decarboxylase. EMBO J. 22:6193-6204.
21. Spry, C., K. Kirk, and K. J. Saliba 2008. Coenzyme A biosynthesis: an antimicrobial drug target. FEMS Microbiol. Rev. 32:56-106.
22. Trip, H., N. L. Mulder, F. P. Rattray, and J. S. Lolkema 2011. HdcB, a novel enzyme catalysing maturation of pyruvoyl-dependent histidine decarboxylase. Mol. Microbiol. 79:861-871.
23. Vallari, D. S., and S. Jackowski 1988. Biosynthesis and degradation both contribute to the regulation of coenzyme A content in Escherichia coli. J. Bacteriol. 170:3961-3966.
24. Vallari, D. S., and C. O. Rock 1985. Isolation and characterization of Escherichia coli pantothenate permease (panF) mutants. J. Bacteriol. 164:136-142.
25. Vallari, D. S., and C. O. Rock 1987. Isolation and characterization of temperature-sensitive pantothenate kinase (coaA) mutants of Escherichia coli. J. Bacteriol. 169:5795-5800.
26. Webb, M. E., A. G. Smith, and C. Abell 2004. Biosynthesis of pantothenate. Nat. Prod. Rep. 21:695-721.
27. Webb, M. E., C. M. C. Lobley, F. Soliman, M. L. Kilkenny, A. G. Smith, T. L. Blundell, et al.2012. The crystal structure of Escherichia coli aspartate alpha-decarboxylase Asn72Ala: probing the role of Asn72 in pyruvoyl cofactor formation. Acta. Cryst. 68:414-417.
28. Williamson, J. M., and G. M. Brown 1979. Purification and properties of L-Aspartate α-decarboxylase, an enzyme that catalyzes the formation of β-alanine in Escherichia coli. J. Biol. Chem. 254:8074-8082.