The Enzyme Database

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EC 1.21.98.1     
Accepted name: cyclic dehypoxanthinyl futalosine synthase
Reaction: dehypoxanthine futalosine + S-adenosyl-L-methionine = cyclic dehypoxanthinyl futalosine + 5′-deoxyadenosine + L-methionine
For diagram of the futalosine pathway, click here
Glossary: dehypoxanthine futalosine = 3-{3-[(2R,3S,4R)-3,4,5-trihydroxytetrahydrofuran-2-yl]propanoyl}benzoate
cyclic dehypoxanthinyl futalosine = (2R,3S,4R)-3,4,5-trihydroxy-4′-oxo-3′,4,4′,5-tetrahydro-2’H,3H-spiro[furan-2,1′-naphthalene]-6′-carboxylate
Other name(s): MqnC; dehypoxanthinyl futalosine cyclase
Systematic name: dehypoxanthine futalosine:S-adenosyl-L-methionine oxidoreductase (cyclizing)
Comments: This enzyme is a member of the ‘AdoMet radical’ (radical SAM) family. The enzyme, found in several bacterial species, is part of the futalosine pathway for menaquinone biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hiratsuka, T., Furihata, K., Ishikawa, J., Yamashita, H., Itoh, N., Seto, H. and Dairi, T. An alternative menaquinone biosynthetic pathway operating in microorganisms. Science 321 (2008) 1670–1673. [DOI] [PMID: 18801996]
2.  Cooper, L.E., Fedoseyenko, D., Abdelwahed, S.H., Kim, S.H., Dairi, T. and Begley, T.P. In vitro reconstitution of the radical S-adenosylmethionine enzyme MqnC involved in the biosynthesis of futalosine-derived menaquinone. Biochemistry 52 (2013) 4592–4594. [DOI] [PMID: 23763543]
[EC 1.21.98.1 created 2014 as EC 1.21.99.2, transferred 2014 to EC 1.21.98.1]
 
 
EC 1.21.99.2      
Transferred entry: EC 1.21.99.2, cyclic dehypoxanthinyl futalosine synthase. Now classified as EC 1.21.98.1, cyclic dehypoxanthinyl futalosine synthase.
[EC 1.21.99.2 created 2014, deleted 2014]
 
 
EC 3.2.2.26     
Accepted name: futalosine hydrolase
Reaction: futalosine + H2O = dehypoxanthine futalosine + hypoxanthine
For diagram of the futalosine pathway, click here
Glossary: futalosine = 3-(3-((3S,4R)-3,4-dihydroxy-5-(6-oxo-3H-purin-9(6H)-yl)tetrahydrofuran-2-yl)propanoyl)benzoate
dehypoxanthine futalosine = 7-(3-carboxyphenyl)-D-ribo-7-dehydro-5,6-dideoxyheptose
Other name(s): futalosine nucleosidase; MqnB (ambiguous)
Systematic name: futalosine ribohydrolase
Comments: This enzyme, which is specific for futalosine, catalyses the second step of a novel menaquinone biosynthetic pathway that is found in some prokaryotes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hiratsuka, T., Furihata, K., Ishikawa, J., Yamashita, H., Itoh, N., Seto, H. and Dairi, T. An alternative menaquinone biosynthetic pathway operating in microorganisms. Science 321 (2008) 1670–1673. [DOI] [PMID: 18801996]
[EC 3.2.2.26 created 2008]
 
 
EC 3.2.2.30     
Accepted name: aminodeoxyfutalosine nucleosidase
Reaction: 6-amino-6-deoxyfutalosine + H2O = dehypoxanthine futalosine + adenine
For diagram of the futalosine pathway, click here
Glossary: 6-amino-6-deoxyfutalosine = 3-{3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]propanoyl}benzoate
dehypoxanthine futalosine = 3-{3-[(2R,3S,4R)-3,4,5-trihydroxytetrahydrofuran-2-yl]propanoyl}benzoate
Other name(s): AFL nucleosidase; aminofutalosine nucleosidase; methylthioadenosine nucleosidase; MqnB (ambiguous)
Systematic name: 6-amino-6-deoxyfutalosine ribohydrolase
Comments: The enzyme, found in several bacterial species, catalyses a step in a modified futalosine pathway for menaquinone biosynthesis. While the enzyme from some organisms also has the activity of EC 3.2.2.9, adenosylhomocysteine nucleosidase, the enzyme from Chlamydia trachomatis is specific for 6-amino-6-deoxyfutalosine [7].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Hiratsuka, T., Furihata, K., Ishikawa, J., Yamashita, H., Itoh, N., Seto, H. and Dairi, T. An alternative menaquinone biosynthetic pathway operating in microorganisms. Science 321 (2008) 1670–1673. [DOI] [PMID: 18801996]
2.  Li, X., Apel, D., Gaynor, E.C. and Tanner, M.E. 5′-methylthioadenosine nucleosidase is implicated in playing a key role in a modified futalosine pathway for menaquinone biosynthesis in Campylobacter jejuni. J. Biol. Chem. 286 (2011) 19392–19398. [DOI] [PMID: 21489995]
3.  Arakawa, C., Kuratsu, M., Furihata, K., Hiratsuka, T., Itoh, N., Seto, H. and Dairi, T. Diversity of the early step of the futalosine pathway. Antimicrob. Agents Chemother. 55 (2011) 913–916. [DOI] [PMID: 21098241]
4.  Wang, S., Haapalainen, A.M., Yan, F., Du, Q., Tyler, P.C., Evans, G.B., Rinaldo-Matthis, A., Brown, R.L., Norris, G.E., Almo, S.C. and Schramm, V.L. A picomolar transition state analogue inhibitor of MTAN as a specific antibiotic for Helicobacter pylori. Biochemistry 51 (2012) 6892–6894. [DOI] [PMID: 22891633]
5.  Mishra, V. and Ronning, D.R. Crystal structures of the Helicobacter pylori MTAN enzyme reveal specific interactions between S-adenosylhomocysteine and the 5′-alkylthio binding subsite. Biochemistry 51 (2012) 9763–9772. [DOI] [PMID: 23148563]
6.  Kim, R.Q., Offen, W.A., Davies, G.J. and Stubbs, K.A. Structural enzymology of Helicobacter pylori methylthioadenosine nucleosidase in the futalosine pathway. Acta Crystallogr. D Biol. Crystallogr. 70 (2014) 177–185. [DOI] [PMID: 24419390]
7.  Barta, M.L., Thomas, K., Yuan, H., Lovell, S., Battaile, K.P., Schramm, V.L. and Hefty, P.S. Structural and biochemical characterization of Chlamydia trachomatis hypothetical protein CT263 supports that menaquinone synthesis occurs through the futalosine pathway. J. Biol. Chem. 289 (2014) 32214–32229. [DOI] [PMID: 25253688]
[EC 3.2.2.30 created 2014]
 
 


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