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Title of Journal: Curr Microbiol

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Abbravation: Current Microbiology

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Springer-Verlag

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1432-0991

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Molecular Cloning and Expression of a Novel Cholin

Authors: Noriko Ishida Daisuke Irikura Kazuhiro Matsuda Seiji Sato Teruo Sone Michiko Tanaka Kozo Asano
Publish Date: 2009/02/14
Volume: 58, Issue: 6, Pages: 535-540
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Abstract

A gene mf1 encoding a novel cholinephosphotransferase in glycoglycerophospholipid GGPL biosynthesis of Mycoplasma fermentans PG18 was identified by genomic analysis cloned and expressed in Escherichia coli The mf1 gene comprises an open reading frame of 777 bp encoding 258 amino acids The mf1 gene product Mf1 has 23 amino acid homology with LicD of Haemophilus influenzae but no homology with genes of other Mycoplasma species in the GenBank database The reaction product of Mf1 using αglucopyranosyl12dipalmitoilglycerol and cytidine 5′diphosphocholine CDPcholine as substrates showed the specific protonated molecule at m/z 896 which corresponded to GGPLI as determined by matrixassisted laser desorption/ionization–timeofflight mass spectrometry MALDITOF MS Furthermore the product ions of choline phosphocholine and hexosebound phosphocholine were detected by tandem mass spectrometry MS analysis of protonated molecules at m/z 896 These results identified mf1 as a novel cholinephosphotransferase and showed that the phosphocholine transfer step is involved in the GGPL biosynthesis pathway of M fermentans This is the first report of a GGPL biosynthesis enzyme

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