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Information on EC 2.1.1.163 - demethylmenaquinone methyltransferase and Organism(s) Escherichia coli and UniProt Accession P0A887

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.163 demethylmenaquinone methyltransferase
IUBMB Comments
The enzyme catalyses the last step in menaquinone biosynthesis. It is able to accept substrates with varying polyprenyl side chain length (the chain length is determined by polyprenyl diphosphate synthase). The enzyme from Escherichia coli also catalyses the conversion of 2-methoxy-6-octaprenyl-1,4-benzoquinone to 5-methoxy-2-methyl-3-octaprenyl-1,4-benzoquinone during the biosynthesis of ubiquinone . The enzyme probably acts on menaquinol rather than menaquinone.
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Escherichia coli
UNIPROT: P0A887
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
demethylmenaquinone methyltransferase, dmkt1, 2-heptaprenyl-1,4-naphthoquinone methyltransferase, dmth protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methione:demethylmenaquinone methyltransferase
The enzyme catalyses the last step in menaquinone biosynthesis. It is able to accept substrates with varying polyprenyl side chain length (the chain length is determined by polyprenyl diphosphate synthase)[1]. The enzyme from Escherichia coli also catalyses the conversion of 2-methoxy-6-octaprenyl-1,4-benzoquinone to 5-methoxy-2-methyl-3-octaprenyl-1,4-benzoquinone during the biosynthesis of ubiquinone [4]. The enzyme probably acts on menaquinol rather than menaquinone.
CAS REGISTRY NUMBER
COMMENTARY hide
37259-80-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
6-methoxy-2-octaprenyl-1,4-benzoquinol + S-adenosyl-L-methionine
6-methoxy-3-methyl-2-octaprenyl-1,4-benzoquinol + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
?
demethylmenaquinol + S-adenosyl-L-methionine
menaquinol + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
?
2-octaprenyl-1,4-naphthoquinone + S-adenosyl-L-methionine
2-octaprenyl-3-methyl-1,4-naphthoquinone + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
i.e. menaquinone
-
?
2-octaprenyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-octaprenyl-1,4-naphthoquinone + S-adenosyl-L-methionine
2-octaprenyl-3-methyl-1,4-naphthoquinone + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
i.e. menaquinone
-
?
2-octaprenyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
strains containing either a disruption or point mutation G142D in ubiE accumulate 2-octaprenyl-6-methoxy-1,4-benzoquinone and demethylmenaquinone as predominant intermediates. Disruption mutants show defects in growth on succinate. The UbiE polypeptide is required for the C methylation reactions in both ubiquinone and menaquinone biosynthesis
malfunction
-
in the uniE-lacking mutant strain AN70, a lack of ubiquinone occurs due to the missing methylation reaction. The mutant also contains only demethylmenaquinone, no menaquinone. Mutant respiration of DMSO is increased, while the respiration of fumarate is reduced compared to the wild-type enzyme
metabolism
-
the enzyme catalyzes a step in the menaquinone pathway as well as the methylation step in ubiquinone pathway, overview. Menaquinne activates the respiration of fumarate, trimethylamine N-oxide, nitrate, and DMSO
physiological function
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G142D
mutant accumulates 2-octaprenyl-6-methoxy-1,4-benzoquinone and demethylmenaquinone as predominant intermediates
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wissenbach, U.; Ternes, D.; Unden, G.
An Escherichia coli mutant containing only demethylmenaquinone, but not menaquinone: effects on fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate respiration
Arch. Microbiol.
158
68-73
1992
Escherichia coli, Escherichia coli AN387
Manually annotated by BRENDA team
Tyson, K.; Metheringham, R.; Griffiths, L.; Cole, J.
Characterisation of Escherichia coli K-12 mutants defective in formate-dependent nitrite reduction: essential roles for hemN and the menFDBCE operon
Arch. Microbiol.
168
403-411
1997
Escherichia coli
Manually annotated by BRENDA team
Lee, P.T.; Hsu, A.Y.; Ha, H.T.; Clarke, C.F.
A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: isolation and identification of the Escherichia coli ubiE gene
J. Bacteriol.
179
1748-1754
1997
Escherichia coli (P0A887)
Manually annotated by BRENDA team