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Lee, Jin-Ha,Kang, Hee-Kyoung,Moon, Young-Hwan,Cho, Dong Lyun,Kim, Doman,Choe, Jun-Yong,Honzatko, R.,Robyt, John F. Oxford University Press 2006 FEMS microbiology letters Vol.259 No.2
<P>Enolase on the surface of streptococci putatively facilitates pathogenic invasion of the host organisms. The related Leuconostoc mesenteroides 512FMCM is nonpathogenic, but it too has an extracellular enolase. Purified isolates of extracellular dextransucrase from cultures of L. mesenteroides contain minute amounts of enolase, which separate as small crystals. Expression of L. mesenteroides enolase in Escherichia coli provides a protein (calculated subunit mass of 47 546 Da) catalyzing the conversion of 2-phsopho-D-glycerate to phosphoenolpyruvate. The pH optimum is 6.8, with Km and kcat values of 2.61 mM and 27.5 s(-1), respectively. At phosphate concentrations of 1 mM and below, fluoride is a noncompetitive inhibitor with respect to 2-phospho-D-glycerate, but in the presence of 20 mM phosphate, fluoride becomes a competitive inhibitor. Recombinant enolase significantly inhibits the activity of purified dextransucrase, and does not bind human plasminogen. Results here suggest that in some organisms enolase may participate in protein interactions that have no direct relevance to pathogenic invasion.</P>
Cloning and Sequencing of the α-1->6 Dextransucrase Gene from Leuconostoc mensenteroides B-742CB
Kim, Ho Sang,Kim, Do Man,Ryu, Hwa Ja,John F.Robyt 한국미생물 · 생명공학회 2000 Journal of microbiology and biotechnology Vol.10 No.4
A dextransucrase gene (dsrB742) that expresses a dextransucrase to synthesize mostly α-1→6 linked dextran with a low amount (3-5%) of α-1→3 branching was cloned and sequenced from Leuconostoc mesenteroides B-742CB. The 6.1-kb PstI fragments were ligated with pGEM-3Zf(-) and transformed into E. coli DH5α. The recombinant clone (pDSRB742) synthesized dextran on an agar plate containing 2%(w/v) sucrose. The dextran synthesized was hydrolyzed with Penicillium endo-dextranase. The hydrolyzate was composed of glucose, isomaltose, isomaltotriose, and branched pentasaccharide. The nucleotide sequence of dsrB742 showed one open reading frame (ORF) composed of 4,524bp encoding dextransucrase. The deduced amino acid sequence revealed a calculated molecular mass of 168.6kDa. It also showed an activity band of 184kDa on a non-denaturing SDS-PAGE (10%). The amino acid sequence of DSRB742 exhibited a 50% similarity with DSRA from L. mesenteroides B-1299, a 70% similarity with DSRS from L. mesenteroides B-512 (F, FMCM) and a 45-56% similarity with Streptococcal GTFs.
김도만,류수진,박관하,ROBYT, JOHN F. 全南大學校 觸媒硏究所 1998 觸媒硏究 論文集 Vol.20 No.-
Acarbose effectively inhibited the synthesis of dextran, and the inhibition pattern was a noncompetitive type with ?? value of 1.35mM. It also inhibited the disproport-ionation reaction of dextransucrase with isomaltotriose and decreased the efficiency of the maltose acceptor reaction. Increased concentration of dextransucrase or maltose in reaction digests, however, decreased the degree of inhibition by acarbose.