Malate/lactate dehydrogenase in mollicutes: Evidence for a multienzyme protein

Gene

Volumn 195, Issue 2, 1997, Pages 113-120

  Cordwell, Stuart J ^a   Basseal, David J ^a   Pollack, J Dennis ^b   Humphery Smith, Ian ^a  

^a National Innovation Centre   (Australia)

^b OHIO STATE UNIVERSITY   (United States)

Author keywords

Enzyme evolution; Genome sequencing; Malate lactate dehydrogenase; Mycoplasma genitalium; Proteome; Spiroplasma melliferum

Indexed keywords

LACTATE DEHYDROGENASE; MALATE DEHYDROGENASE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME SPECIFICITY; MOLLICUTES; MYCOPLASMA; NONHUMAN; PRIORITY JOURNAL; SPIROPLASMA;

AMINO ACID SEQUENCE; ARGININE; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GENES, BACTERIAL; GENOME, BACTERIAL; L-LACTATE DEHYDROGENASE; MALATE DEHYDROGENASE; MOLECULAR SEQUENCE DATA; MOLLICUTES; MYCOPLASMA; PEPTIDE MAPPING; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY, AMINO ACID; SPIROPLASMA; TRICARBOXYLIC ACIDS;

BACTERIA (MICROORGANISMS); MOLLICUTES; MYCOPLASMA GENITALIUM; SPIROPLASMA; SPIROPLASMA MELLIFERUM;

EID: 0030794705     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(97)00063-2     Document Type: Article

References (36)

1. Bairoch A. The PROSITE dictionary of sites and patterns, its current status. Nucl. Acids Res. 21:1993;3097-3103.
2. Bairoch A., Boeckmann B. The SWISS-PROT protein sequence databank. Nucl. Acids Res. 20:1992;2019-2022.
3. Boerncke W.E., Millard C.S., Stevens P.W., Kakar S.N., Stevens F.J., Donnelly M.I. Stringency of substrate specificity of Escherichia coli malate dehydrogenase. Arch. Biochem. Biophys. 322:1995;43-52.
4. Cendrin F., Chroboczek J., Zaccai G., Eisenberg H., Mevarech M. Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui. Biochemistry. 32:1993;4308-4313.
5. Chastel C., LeGoff F., Humphery-Smith I. Multiplication and persistence of Spiroplasma melliferum strain A56 in experimentally infected suckling mice. Res. Microbiol. 142:1991;411-417.
6. Clarke A.R., Atkinson T., Campbell J.W., Holbrook J.J. The assembly mechanism of the lactate dehydrogenase tetramer from Bacillus stearothermophilus; the equilibrium relationships between quaternary structure and the binding of fructose 1,6-bisphosphate, NADH and oxamate. Biochim. Biophys. Acta. 829:1985;387-396.
7. Clarke A.R., Smith C.J., Hart K.W., Wilks H.M., Chia W.N., Lee T.V., Birkoft J.J., Banaszak L.J., Barstow D.A., Atkinson T., Holbrook J.J. Rational construction of a 2-hydroxyacid dehydrogenase with new substrate specificity. Biochem. Biophys. Res. Comm. 148:1987;15-23.
8. Clarke A.R., Wigley D.B., Chia W.N., Barstow D., Atkinson T., Holbrook J.J. Site-directed mutagenesis reveals role of mobile arginine residue in lactate dehydrogenase catalysis. Nature. 324:1986;699-702.
9. Colston M.J., Davis E.O. The ins and outs of protein splicing elements. Mol. Microbiol. 12:1994;359-363.
10. Cordwell, S.J., Basseal, D.J., Humphery-Smith, I., 1997a. Proteome analysis of Spiroplasma melliferum (A56) and protein characterisation across species boundaries. Electrophoresis, 18, in press.
11. Cordwell S.J., Wasinger V.C., Cerpa-Poljak A., Duncan M.W., Humphery-Smith I. Conserved motifs as the basis for recognition of homologous proteins across species boundaries using peptide-mass fingerprinting. J. Mass Spec. 32:1997;370-378.
12. Cordwell S.J., Wilkins M.R., Cerpa-Poljak A., Gooley A.A., Duncan M., Williams K.L., Humphery-Smith I. Cross-species identification of proteins separated by two-dimensional gel electrophoresis using matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry and amino acid composition. Electrophoresis. 16:1995;438-443.
13. Davis E.O., Jenner P.J., Brooks P.C., Colston M.J., Sedgwick S.G. Protein splicing in the maturation of Mycobacterium tuberculosis RecA protein: a mechanism for tolerating a novel class of intervening sequence. Cell. 71:1992;201-210.
14. Dym O., Mevarech M., Sussman J.L. Structural features that stabilize halophilic malate dehydrogenase from an archaebacterium. Science. 267:1995;1344-1346.
15. Eventoff W., Rossman M.G., Taylor S.S., Torff H.-J., Meyer H., Keil W., Klitz H.H. Structural adaptations of lactate dehydrogenase isozymes. Proc. Natl. Acad. Sci. USA. 74:1977;2677-2681.
16. Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G., Kelley J.M., Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J., Nguyen D., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C. The minimal gene complement of Mycoplasma genitalium. Science. 270:1995;397-403.
17. GCG, Program Manual for the Wisconsin Package, Version 8, 1994.
18. Haldimann A., Nicolet J., Frey J. DNA sequence determination and biochemical analysis of the immunogenic protein P36, the lactate dehydrogenase (LDH) of Mycoplasma hyopneumoniae. J. Gen. Microbiol. 23:1993;317-323.
19. Hall M.D., Banaszak L.J. Crystal structure of a ternary complex of Escherichia coli malate dehydrogenase, citrate and NAD at 1.9Å J. Mol. Biol. 232:1993;213-222.
20. Hall M.D., Levitt D.G., Banaszak L.J. Crystal structure of Escherichia coli malate dehydrogenase - a complex of the apoenzyme and citrate at 1.87Å resolution. J. Mol. Biol. 226:1992;867-882.
21. Hobohm U., Houthaeve T., Sander C. Amino acid analysis and protein database search as a rapid and inexpensive method to identify proteins. Anal. Biochem. 222:1994;202-209.
22. Honka E., Fabry S., Niermann T., Palm P., Hensel R. Properties and primary structure of the L-malate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus. Eur. J. Biochem. 188:1990;623-632.
23. Humphery-Smith I., LeGoff F., Chastel C. Spiroplasmas and spongiform encephalopathies. Med. J. Aust. 156:1992;142.
24. Kobayashi K., Doi S., Negoro S., Urabe I., Okada H. Structure and properties of malic enzyme from Bacillus stearothermophilus. J. Biol. Chem. 264:1989;3200-3205.
25. Manoloukas J., Barile M.F., Chandler D.K.F., Pollack J.D. Presence of anaplerotic reactions, transamination, and the absence of the tricarboxylic acid cycle in Mollicutes. J. Gen. Microbiol. 134:1988;791-800.
26. McAllister-Henn L. Evolutionary relationships among the malate dehydrogenases. TIBS. 13:1988;178-181.
27. Nicholls D.J., Miller J., Scawen M.D., Clarke A.R., Holbrook J.J., Atkinson T., Goward C.R. The importance of arginine 102 for the substrate specificity of Escherichia coli malate dehydrogenase. Biochem. Biophys. Res. Comm. 189:1992;1057-1062.
28. Pappin D.J.C., Højrup P., Bleasby A.J. Rapid identification of proteins by peptide-mass fingerprinting. Curr. Biol. 3:1993;327-332.
29. Pearson W.R., Lipman D.J. Improved tools for biological sequence comparisons. Proc. Natl. Acad. Sci. USA. 85:1988;2444-2448.
30. Pollack, J.D., 1992. Carbohydrate metabolism and energy conservation. In: Maniloff, J., McElhaney, R.N., Finch, L.R., Baseman, J.B. (Eds), Mycoplasmas: Molecular Biology and Pathogenesis. ASM, Washington, D.C., pp. 181-200.
31. Pollack J.D., McElwain M.C., DeSantis D., Manolukas J.T., Tully J.G., Chang C.-J., Whitcomb R.F., Hackett K.J., Williams M.V. Metabolism of members of the Spiroplasmataceae. Int. J. Syst. Bacteriol. 39:1989;406-412.
32. Shaw G. Rapid identification of proteins. Proc. Natl. Acad. Sci. USA. 90:1993;5138-5142.
33. Wasinger V., Cordwell S.J., Cerpa-Poljak A., Yan J.X., Gooley A.A., Wilkins M.R., Duncan M.W., Harris R., Williams K.L., Humphery-Smith I. Progress with gene-product mapping of the mollicutes: Mycoplasma genitalium. Electrophoresis. 16:1995;1090-1094.
34. Wigley D.B., Gamblin S.J., Turkenburg J.P., Dodson E.J., Piontek K., Muirhead H., Holbrook J.J. Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5Å resolution. J. Mol. Biol. 223:1992;317-335.
35. Wilks H.M., Hart K.W., Feeney R., Dunn C.R., Muirhead H., Chia W.N., Barstow D.A., Atkinson T., Clarke A.R., Holbrook J.J. A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework. Science. 242:1988;1541-1544.
36. Yoon H., Anderson B.M. Kinetic studies of Haemophilus influenzae malate dehydrogenase. Biochim. Biophys. Acta. 955:1988;10-18.