2005
DOI: 10.1016/j.chembiol.2005.04.012
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A Nucleosidase Required for In Vivo Function of the S-Adenosyl-L-Methionine Radical Enzyme, Biotin Synthase

Abstract: Biotin synthase is an S-adenosyl-L-methionine (SAM) radical enzyme that inserts sulfur into dethiobiotin to produce biotin. The reaction proceeds through 5'-deoxyadenosyl radical intermediates that become reduced during the sulfur insertion step to give another product of the reaction, 5'-deoxyadenosine. We report that Escherichia coli strains lacking the 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase encoded by the pfs gene are deficient in biotin synthase activity due to accumulation of 5'-deoxya… Show more

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Cited by 70 publications
(100 citation statements)
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“…MTANs are required in a diverse array of biosynthetic pathways (37)(38)(39) that have yet to be implicated in Chlamydia (e.g. polyamine biosynthesis, quorum sensing, DNA methylation, etc.).…”
Section: Discussionmentioning
confidence: 99%
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“…MTANs are required in a diverse array of biosynthetic pathways (37)(38)(39) that have yet to be implicated in Chlamydia (e.g. polyamine biosynthesis, quorum sensing, DNA methylation, etc.).…”
Section: Discussionmentioning
confidence: 99%
“…6A), the enzymatic characterization of CT263 indicates that only AFL can be hydrolyzed at a physiological rate. Traditionally, MTANs hydrolyze intermediates of AdoMet utilization pathways (37)(38)(39), which include substrates that were not processed by CT263 (e.g. MTA and AdoHcy, Fig.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…Enzyme group 4 consisted of C-5 cytosinespecific DNA methylase and SP-beta prophage DNA (cytosine-5-)-methyltransferase (Bsubtilis_ydiO Bsubtilis _ydiP Bsubtilis_mtbP; EC 2.1.1.37; COG0270L, K00558, and PF00145 [51,81]), and 5=-methylthioadenosine nucleosidase and S-adenosylhomocysteine nucleosidase (mtn Streptococci_pfs; EC 3.2.2.16 and EC 3.2.2.9; COG0775F, K01243, and PF1048 [10,55]). …”
Section: Methodsmentioning
confidence: 99%
“…pfs is central to this process, as both characterized pfs enzymatic reactions produce adenine (from either S-adenosylhomocysteine or methylthioadenosine), which is recycled during exponential growth (not shown in Fig. 7) and broken down and detected in the medium of stationary-phase cells (4,20,25,26). Thus, pfs and dgt work together to break down purine under conditions of purine excess.…”
Section: Vol 188 2006mentioning
confidence: 99%