Any feedback?
No. of entries
Information on EC 2.5.1.120 - aminodeoxyfutalosine synthase
for references in articles please use BRENDA:EC2.5.1.120
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.5 Transferring alkyl or aryl groups, other than methyl groups
2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
2.5.1.120 aminodeoxyfutalosine synthase
IUBMB 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.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
aminofutalosine synthase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MqnE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O = 6-amino-6-deoxyfutalosine + L-methionine + HCO3-
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
1,4-dihydroxy-6-naphthoate biosynthesis I, 1,4-dihydroxy-6-naphthoate biosynthesis II
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:3-[(1-carboxyvinyl)-oxy]benzoate adenosyltransferase (bicarbonate-hydrolysing, 6-amino-6-deoxyfutalosine-forming)
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O
6-amino-6-deoxyfutalosine + L-methionine + bicarbonate
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O
6-amino-6-deoxyfutalosine + L-methionine + HCO3-
S-adenosyl-L-methionine + 3-[(3-amino-3-oxoprop-1-en-2-yl)oxy]benzoic acid + H2O
5'-deoxy-5'-(4-(4-carboxyphenoxy)-4-carboxybutyl)adenosine + ?
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 3-[[(Z)-2-bromo-1-carboxyethenyl]oxy]benzoic acid + H2O
9-[(6E)-7-O-(3-carboxyphenyl)-5,6-dideoxy-beta-D-ribo-oct-6-enofuranuronosyl]adenine + 9-[6-(bromomethylidene)-5,6-dideoxy-beta-D-ribo-heptofuranuronosyl]adenine + ?
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 4-bromo-3-[(1-carboxyethenyl)oxy]benzoic acid + H2O
9-[8-(3-carboxyphenyl)-5,6,7-trideoxy-beta-D-ribo-octodialdo-1,4-furanosyl]adenine + 9-[8-(2-bromo-5-carboxyphenyl)-5,6,7-trideoxy-beta-D-ribo-octodialdo-1,4-furanosyl]adenine + ?
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O
6-amino-6-deoxyfutalosine + L-methionine + bicarbonate
Substrates: the enzyme is part of the futalosine pathway for menaquinone biosynthesis
Products: 6-amino-6-deoxyfutalosine i.e. 3-[3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]propanoyl]benzoate
Products: 6-amino-6-deoxyfutalosine i.e. 3-[3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]propanoyl]benzoate
?
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O
6-amino-6-deoxyfutalosine + L-methionine + bicarbonate
Substrates: -
Products: 6-amino-6-deoxyfutalosine i.e. 3-[3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]propanoyl]benzoate
Products: 6-amino-6-deoxyfutalosine i.e. 3-[3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]propanoyl]benzoate
?
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O
6-amino-6-deoxyfutalosine + L-methionine + HCO3-
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O
6-amino-6-deoxyfutalosine + L-methionine + HCO3-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O
6-amino-6-deoxyfutalosine + L-methionine + HCO3-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O
6-amino-6-deoxyfutalosine + L-methionine + HCO3-
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O
6-amino-6-deoxyfutalosine + L-methionine + HCO3-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O
6-amino-6-deoxyfutalosine + L-methionine + bicarbonate
Substrates: the enzyme is part of the futalosine pathway for menaquinone biosynthesis
Products: 6-amino-6-deoxyfutalosine i.e. 3-[3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]propanoyl]benzoate
Products: 6-amino-6-deoxyfutalosine i.e. 3-[3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]propanoyl]benzoate
?
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O
6-amino-6-deoxyfutalosine + L-methionine + HCO3-
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O
6-amino-6-deoxyfutalosine + L-methionine + HCO3-
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O
6-amino-6-deoxyfutalosine + L-methionine + HCO3-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O
6-amino-6-deoxyfutalosine + L-methionine + HCO3-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O
6-amino-6-deoxyfutalosine + L-methionine + HCO3-
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + 3-[(1-carboxyvinyl)oxy]benzoate + H2O
6-amino-6-deoxyfutalosine + L-methionine + HCO3-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
the enzyme is a member of the AdoMet radical family. S-Adenosyl-L-methionine acts as both a radical generator and as the source of the transferred adenosyl group
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
[4Fe-4S] cluster
presence of the predicted [4Fe-4S] cluster. Iron and sulfide analysis yields 2.4 irons and 2.8 sulfides per monomer of MqnE, indicating incomplete reconstitution of the cluster
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9-[8-[(3-carboxyphenyl)methyl]-5,6,7,8-tetradeoxy-beta-D-ribo-nonofuranuronosyl]-9H-purin-6-amine
9-[8-[(3-carboxyphenyl)methyl]-5,6,7,8-tetradeoxy-beta-D-ribo-nonofuranuronosyl]-9H-purin-6-amine
-
-
9-[8-[(3-carboxyphenyl)methyl]-5,6,7,8-tetradeoxy-beta-D-ribo-nonofuranuronosyl]-9H-purin-6-amine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0161 - 0.0833
9-[8-[(3-carboxyphenyl)methyl]-5,6,7,8-tetradeoxy-beta-D-ribo-nonofuranuronosyl]-9H-purin-6-amine
0.0018
3-(2-carboxyprop-2-en-1-yl)benzoic acid
Helicobacter pylori
pH and temperature not specified in the publication
0.0136
3-(2-carboxyprop-2-en-1-yl)benzoic acid
Campylobacter jejuni
-
pH and temperature not specified in the publication
0.0161
9-[8-[(3-carboxyphenyl)methyl]-5,6,7,8-tetradeoxy-beta-D-ribo-nonofuranuronosyl]-9H-purin-6-amine
Helicobacter pylori
pH and temperature not specified in the publication
0.0833
9-[8-[(3-carboxyphenyl)methyl]-5,6,7,8-tetradeoxy-beta-D-ribo-nonofuranuronosyl]-9H-purin-6-amine
Campylobacter jejuni
-
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme is part of the futalosine pathway for menaquinone biosynthesis
Show AA Sequence and Transmembrane Helices (2302 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into the pQE-30 expression vector, and overexpressed in Escherichia coli M15 (pREP4)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mahanta, N.; Fedoseyenko, D.; Dairi, T.; Begley, T.P.
Menaquinone biosynthesis: formation of aminofutalosine requires a unique radical SAM enzyme
J. Am. Chem. Soc.
135
15318-15321
2013
Thermus thermophilus (Q5SK48)
brenda
Joshi, S.; Fedoseyenko, D.; Mahanta, N.; Ducati, R.G.; Feng, M.; Schramm, V.L.; Begley, T.P.
Antibacterial strategy against H. pylori Inhibition of the radical SAM enzyme MqnE in menaquinone biosynthesis
ACS Med. Chem. Lett.
10
363-366
2019
Campylobacter jejuni, Helicobacter pylori (O25368), Helicobacter pylori, Helicobacter pylori ATCC 700392 (O25368)
brenda
Joshi, S.; Mahanta, N.; Fedoseyenko, D.; Williams, H.; Begley, T.P.
Aminofutalosine synthase Evidence for captodative and aryl radical intermediates using beta-scission and SRN1 trapping reactions
J. Am. Chem. Soc.
139
10952-10955
2017
Thermus thermophilus
brenda
Joshi, S.; Fedoseyenko, D.; Mahanta, N.; Begley, T.P.
Aminofutalosine synthase (MqnE) A new catalytic motif in radical SAM enzymology
Methods Enzymol.
606
179-198
2018
Thermus thermophilus (Q5SK48)
brenda
EXTERNAL LINKS (specific for EC-Number 2.5.1.120)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
