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HORT640 - Metabolic Plant Physiology
References, homoserine kinase
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Baum HJ, Madison JT, Thompson JF. Feedback inhibition of homoserine kinase from radish leaves. Phytochemistry 22: 2409-2412 (1983).
Belfaiza J, Fazel A, Muller K, Cohen GN. E. coli aspartokinase II-homoserine dehydrogenase II polypeptide chain has a triglobular structure. Biochem. Biophys. Res. Commun. 123: 16-20 (1984).
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Colon GE, Jetten MS, Nguyen TT, Gubler ME, Follettie MT, Sinskey AJ, Stephanopoulos G. Effect of inducible thrB expression on amino acid production in Corynebacterium lactofermentum ATCC 21799. Appl. Environ. Microbiol. 61: 74-78 (1995).
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Eikmanns BJ, Eggeling L, Sahm H. Molecular aspects of lysine, threonine, and isoleucine biosynthesis in Corynebacterium glutamicum. Antonie Van Leeuwenhoek 64: 145-163 (1993).
Eikmanns BJ, Metzger M, Reinscheid D, Kircher M, Sahm H. Amplification of three threonine biosynthesis genes in Corynebacterium glutamicum and its influence on carbon flux in different strains. Appl. Microbiol. Biotechnol. 34: 617-622 (1991).
Fazel A, Guillou Y, Cohen GN. A hybrid proteolytic fragment of Escherichia coli aspartokinase I-homoserine dehydrogenase I. Structure, inhibition pattern, dissociation properties, and generation of two homodimers. J. Biol. Chem. 258: 13570-13574 (1983).
Fazel A, Muller K, Le Bras G, Garel JR, Veron M, Cohen GN. A triglobular model for the polypeptide chain of aspartokinase I-homoserine dehydrogenase I of Escherichia coli. Biochemistry 22: 158-165 (1983).
Fernandez M, Cuadrado Y, Recio E, Aparicio JF, Martin JF. Characterization of the hom-thrC-thrB cluster in aminoethoxyvinylglycine-producing Streptomyces sp NRRL 5331. Microbiology 148: 1413-1420 (2002).
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Follettie MT, Shin HK, Sinskey AJ. Organization and regulation of the Corynebacterium glutamicum hom-thrB and thrC loci. Mol. Microbiol. 2: 53-62 (1988).
Garel JR, Dautry-Varsat A. Sequential folding of a bifunctional allosteric protein. Proc. Natl. Acad. Sci. U.S.A. 77: 3379-3383 (1980).
Garrido-Franco M, Ehlert S, Messerschmidt A, Marinkovic S, Huber R, Laber B, Bourenkov GP, Clausen T. Structure and function of threonine synthase from yeast. J. Biol. Chem. 277: 12396-12405 (2002).
Gaziola SA, Alessi ES, Guimaraes PEO, Damerval C, Azevedo RA. Quality protein maize: a biochemical study of enzymes involved in lysine metabolism. J. Agric. Food Chem. 47: 1268-1275 (1999).
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Huo X, Viola RE. Substrate specificity and identification of functional groups of homoserine kinase from Escherichia coli. Biochemistry 35: 16180-16185 (1996).
Jullien M, Baudet S, Rodier F, Le Bras G. Allosteric transition of aspartokinase I-homoserine dehydrogenase I studied by time-resolved fluorescence. Biochimie 70: 1807-1814 (1988).
Kalcheva EO, Shanskaya VO, Maliuta SS. Activities and regulation of the enzymes involved in the first and the third steps of the aspartate biosynthetic pathway in Enterococcus faecium. Arch. Microbiol. 161: 359-362 (1994).
Karsten WE, Hunsley JR, Viola RE. Purification of aspartase and aspartokinase-homoserine dehydrogenase I from Escherichia coli by dye-ligand chromatography. Anal. Biochem. 147: 336-341 (1985).
Komatsubara S, Kisumi M, Chibata I. Transductional construction of a threonine-hyperproducing strain of Serratia marcescens: lack of feedback controls of three aspartokinases and two homoserine dehydrogenases. Appl. Environ. Microbiol. 45: 1445-1452 (1983).
Komatsubara S, Kisumi M, Chibata I. Participation of lysine-sensitive aspartokinase in threonine production by S-2-aminoethyl cysteine-resistant mutants of Serratia marcescens. Appl. Environ. Microbiol. 38: 777-782 (1979).
Lee M, Leustek T. Identification of the gene encoding homoserine kinase from Arabidopsis thaliana and characterization of the recombinant enzyme derived from the gene. Arch. Biochem. Biophys. 372: 135-142 (1999).
Lee M, Martin MN, Hudson AO, Lee J, Muhitch MJ, Leustek T. Methionine and threonine synthesis are limited by homoserine availability and not the activity of homoserine kinase in Arabidopsis thaliana. Plant J. 41: 685-696 (2005).
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Mannhaupt G, Pohlenz HD, Seefluth AK, Pilz U, Feldmann H. Yeast homoserine kinase. Characteristics of the corresponding gene, THR1, and the purified enzyme, and evolutionary relationships with other enzymes of threonine metabolism. Eur. J. Biochem. 191: 115-122 (1990).
Manucharian KG, Gening LV, Gusiatiner MM, Gazarian KG. Design of a gene coding encoding a polypeptide, mixing the enzyme activity of Escherichia coli homoserine kinase and threonine synthetase. Mol. Gen. Mikrobiol. Virusol. 2: 12-15 (1991).
Marchenko GN, Marchenko ND, Tsygankov YD, Chistoserdov AY. Organization of threonine biosynthesis genes from the obligate methylotroph Methylobacillus flagellatus. Microbiology 145: 3273-3282 (1999).
Martin-Rendon E, Calderon IL. Identification of yeast cloned genes by genetic analysis. Microbiologia 8: 82-93 (1992).
Mateos LM, del Real G, Aguilar A, Martin JF. Nucleotide sequence of the homoserine kinase (thr B) gene of Brevibacterium lactofermentum. Nucleic Acids Res. 15: 3922 (1987).
Mateos LM, Pisabarro A, Patek M, Malumbres M, Guerrero C, Eikmanns BJ, Sahm H, Martin JF. Transcriptional analysis and regulatory signals of the hom-thrB cluster of Brevibacterium lactofermentum. J. Bacteriol. 176: 7362-7371 (1994).
Matthews BF, Widholm JM. Expression of aspartokinase, dihydrodipicolinic acid synthase and homoserine dehydrogenase during growth of carrot cell suspension cultures on lysine- and threonine-supplemented media. Z. Naturforsch. [C] 34: 1177-1185 (1979).
Mendelovitz S, Aharonowitz Y. Regulation of cephamycin C synthesis, aspartokinase, dihydrodipicolinic acid synthetase, and homoserine dehydrogenase by aspartic acid family amino acids in Streptomyces clavuligerus. Antimicrob. Agents Chemother. 21: 74-84 (1982).
Motoyama H, Yano H, Ishino S, Anazawa H, Teshiba S. Effects of the amplification of the genes coding for the L-threonine biosynthetic enzymes on the L-threonine production from methanol by a gram-negative obligate methylotroph, Methylobacillus glycogenes. Appl. Microbiol. Biotechnol. 42: 67-72 (1994).
Muehlbauer GJ, Somers DA, Matthews BF, Gengenbach BG. Molecular genetics of the maize (Zea mays L.) aspartate kinase-homoserine dehydrogenase gene family. Plant Physiol. 106: 1303-1312 (1994).
Muller K, Garel JR. Stepwise inactivation of Escherichia coli aspartokinase-homoserine dehydrogenase I. Biochemistry 23: 651-654 (1984).
Nakabachi A, Ishikawa H. Differential display of mRNAs related to amino acid metabolism in the endosymbiotic system of aphids. Insect Biochem. Mol. Biol. 27: 1057-1062 (1997).
Okorokov AL, Bukanov NO, Beskrovnaia OIu, Voroshilova EB, Gusiatiner MM, Gritsenko VG, Iankovskii NK, Debabov VG. Development of the vector-host system in Corynebacterium. Cloning and expression of homoserine dehydrogenase and homoserine kinase genes in Corynebacterium cells. Genetika 26: 648-656 (1990).
Omori K, Imai Y, Suzuki S, Komatsubara S. Nucleotide sequence of the Serratia marcescens threonine operon and analysis of the threonine operon mutations which alter feedback inhibition of both aspartokinase I and homoserine dehydrogenase I. J. Bacteriol. 175: 785-794 (1993).
Omori K, Komatsubara S. Role of serine 352 in the allosteric response of Serratia marcescens aspartokinase I-homoserine dehydrogenase I analyzed by using site-directed mutagenesis. J. Bacteriol. 175: 959-965 (1993).
Parsot C. Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase. EMBO J. 5: 3013-3019 (1986).
Parsot C, Cohen GN. Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding for homoserine dehydrogenase. Structural and evolutionary relationships with Escherichia coli aspartokinases-homoserine dehydrogenases I and II. J. Biol. Chem. 263: 14654-14660 (1988).
Parsot C, Mazel D. Cloning and nucleotide sequence of the thrB gene from the cyanobacterium Calothrix PCC 7601. Mol. Microbiol. 1: 45-52 (1987).
Patte JC, Clepet C, Bally M, Borne F, Mejean V, Foglino M. ThrH, a homoserine kinase isozyme with in vivo phosphoserine phosphatase activity in Pseudomonas aeruginosa. Microbiology 145: 845-853 (1999).
Pavagi S, Kochhar S, Kochhar VK, Sane PV. Purification and characterization of homoserine dehydrogenase from spinach leaves. Biochem. Mol. Biol. Int. 36: 649-658 (1995).
Polodienko OB, Chistoserdov AIu, Totskii VN, Tsygankov IuD. The effect of amino acids in the asparagine family on the aspartate kinase and homoserine dehydrogenase of ethionine-resistant mutants of Pseudomonas putida. Mikrobiol. Zh. 53: 63-67 (1991).
Prorok M, Sukumaran DK, Lawrence DS. The cyclic AMP-dependent protein kinase from bovine cardiac muscle is a homoserine kinase. J. Biol. Chem. 264: 17727-17733 (1989).
Rafalski JA, Falco SC. Structure of the yeast HOM3 gene which encodes aspartokinase. J. Biol. Chem. 263: 2146-2151 (1988).
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Ramos C, Delgado MA, Calderon IL. Inhibition by different amino acids of the aspartate kinase and the homoserine kinase of the yeast Saccharomyces cerevisiae. FEBS Lett. 278: 123-126 (1991).
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Shames SL, Wedler FC. Homoserine kinase of Escherichia coli: kinetic mechanism and inhibition by L-aspartate semialdehyde. Arch. Biochem. Biophys. 235: 359-370 (1984).
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Number of references = 93
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