Information on EC 3.5.4.40 - aminodeoxyfutalosine deaminase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.4.40
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RECOMMENDED NAME
GeneOntology No.
aminodeoxyfutalosine deaminase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
6-amino-6-deoxyfutalosine + H2O = futalosine + NH3
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1,4-dihydroxy-6-naphthoate biosynthesis I
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Biosynthesis of secondary metabolites
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Ubiquinone and other terpenoid-quinone biosynthesis
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1,4-dihydroxy-6-naphthoate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
6-amino-6-deoxyfutalosine deaminase
The enzyme, found in several bacterial species, is part of the futalosine pathway for menaquinone biosynthesis.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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the enzyme is part of the futalosine pathway for menaquinone biosynthesis
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-(6-amino-9H-purin-9-yl)-1-deoxy-N-ethyl-beta-D-ribofuranuronamide + H2O
?
show the reaction diagram
2'-deoxyadenosine + H2O
?
show the reaction diagram
3'-deoxyadenosine + H2O
?
show the reaction diagram
5'-deoxyadenosine + H2O
?
show the reaction diagram
5'-methylthioadenosine + H2O
?
show the reaction diagram
6-amino-6-deoxyfutalosine + H2O
futalosine + NH3
show the reaction diagram
adenosine + H2O
?
show the reaction diagram
AMP + H2O
?
show the reaction diagram
S-adenosyl-L-homocysteine + H2O
?
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
6-amino-6-deoxyfutalosine + H2O
futalosine + NH3
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.061
1-(6-amino-9H-purin-9-yl)-1-deoxy-N-ethyl-beta-D-ribofuranuronamide
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wild type enzyme, at pH 7.5 and at 30C
0.037
2'-deoxyadenosine
wild type enzyme, at pH 7.5 and at 30C
0.042
5'-deoxyadenosine
wild type enzyme, at pH 7.5 and at 30C
0.094 - 1
5'-methylthioadenosine
0.0009 - 0.008
6-amino-6-deoxyfutalosine
0.0083 - 0.01
adenosine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007
1-(6-amino-9H-purin-9-yl)-1-deoxy-N-ethyl-beta-D-ribofuranuronamide
Acidothermus cellulolyticus
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wild type enzyme, at pH 7.5 and at 30C
0.72
2'-deoxyadenosine
Deinococcus radiodurans
Q9RW45
wild type enzyme, at pH 7.5 and at 30C
0.017
5'-deoxyadenosine
Nitratiruptor sp. SB155-2
A6Q234
wild type enzyme, at pH 7.5 and at 30C
0.31 - 0.4
5'-methylthioadenosine
0.094 - 8.6
6-amino-6-deoxyfutalosine
0.106 - 0.41
adenosine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.034 - 10
1-(6-amino-9H-purin-9-yl)-1-deoxy-N-ethyl-beta-D-ribofuranuronamide
194865
0.005 - 19
2'-deoxyadenosine
357
0.006 - 0.24
3'-deoxyadenosine
2127
0.047 - 74
5'-deoxyadenosine
943
0.028 - 34
5'-methylthioadenosine
400
27 - 4800
6-amino-6-deoxyfutalosine
6387
0.011 - 41
adenosine
122
0.003 - 0.045
AMP
30
0.024 - 7
S-adenosyl-L-homocysteine
36
PDB
SCOP
CATH
ORGANISM
UNIPROT
Nitratiruptor sp. (strain SB155-2)
Nitratiruptor sp. (strain SB155-2)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 30% (w/v) PEG MME500, 0.1 M Bis-Tris, pH 6.5, and 50 mM calcium chloride
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex 200 gel filtration
Strep-Tactin column column chromatography, HisTrap column chromatography, and Superdex 200 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta2 (DE3) cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R87A
the mutant shows reduced activity towards 6-amino-6-deoxyfutalosine and adenosine compared to the wild type enzyme
R87M
the mutant shows reduced activity towards 6-amino-6-deoxyfutalosine and increased activity towards adenosine compared to the wild type enzyme
R87A
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the mutant shows reduced activity towards 6-amino-6-deoxyfutalosine and adenosine compared to the wild type enzyme
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R87M
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the mutant shows reduced activity towards 6-amino-6-deoxyfutalosine and increased activity towards adenosine compared to the wild type enzyme
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