The Enzyme Database

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EC 2.5.1.120     
Accepted name: aminodeoxyfutalosine synthase
Reaction: S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O = 6-amino-6-deoxyfutalosine + L-methionine + HCO3-
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
Other name(s): MqnE; AFL synthase; aminofutalosine synthase; S-adenosyl-L-methionine:3-[(1-carboxyvinyl)-oxy]benzoate adenosyltransferase (bicarbonate-hydrolysing, 6-amino-6-deoxyfutalosine-forming)
Systematic name: S-adenosyl-L-methionine:3-[(1-carboxyvinyl)-oxy]benzoate adenosyltransferase (HCO3--hydrolysing, 6-amino-6-deoxyfutalosine-forming)
Comments: This enzyme is a member of the ‘AdoMet radical’ (radical SAM) family. S-Adenosyl-L-methionine acts as both a radical generator and as the source of the transferred adenosyl group. 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.  Mahanta, N., Fedoseyenko, D., Dairi, T. and Begley, T.P. Menaquinone biosynthesis: formation of aminofutalosine requires a unique radical SAM enzyme. J. Am. Chem. Soc. 135 (2013) 15318–15321. [DOI] [PMID: 24083939]
[EC 2.5.1.120 created 2014]
 
 
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
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]
 
 
EC 3.5.4.40     
Accepted name: aminodeoxyfutalosine deaminase
Reaction: 6-amino-6-deoxyfutalosine + H2O = futalosine + NH3
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
futalosine = 3-{3-[(3S,4R)-3,4-dihydroxy-5-(6-oxo-1,6-dihydro-9H-purin-9-yl)tetrahydrofuran-2-yl]propanoyl}benzoate
Other name(s): AFL deaminase; aminofutalosine deaminase; mqnX (gene name)
Systematic name: 6-amino-6-deoxyfutalosine deaminase
Comments: 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.  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]
2.  Goble, A.M., Toro, R., Li, X., Ornelas, A., Fan, H., Eswaramoorthy, S., Patskovsky, Y., Hillerich, B., Seidel, R., Sali, A., Shoichet, B.K., Almo, S.C., Swaminathan, S., Tanner, M.E. and Raushel, F.M. Deamination of 6-aminodeoxyfutalosine in menaquinone biosynthesis by distantly related enzymes. Biochemistry 52 (2013) 6525–6536. [DOI] [PMID: 23972005]
[EC 3.5.4.40 created 2014]
 
 


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