Information on EC 3.5.4.41 - 5'-deoxyadenosine deaminase

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The expected taxonomic range for this enzyme is: Methanocaldococcus jannaschii

EC NUMBER
COMMENTARY hide
3.5.4.41
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RECOMMENDED NAME
GeneOntology No.
5'-deoxyadenosine deaminase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5'-deoxyadenosine + H2O = 5'-deoxyinosine + NH3
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
5'-deoxyadenosine aminohydrolase
The enzyme from the archaeon Methanocaldococcus jannaschii is involved in the recycling of 5'-deoxyadenosine.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme is involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5'-deoxyadenosine + H2O
5'-deoxyinosine + NH3
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
5'-deoxyadenosine + H2O
5'-deoxyinosine + NH3
show the reaction diagram
Q58936
the enzyme is involved in the recycling of 5'-deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal
Ni2+
the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal
Zn2+
the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.014 - 0.05
5'-deoxyadenosine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.12 - 120000
5'-deoxyadenosine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
31 - 9100000
5'-deoxyadenosine
943
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
10 min, mutant enzyme Y136R/E150R loses 65% of its activity, mutant enzyme Y136R loses 20% of its activity, mutant enzyme E150R loses% of its activity
60
10 min, wild-type enzyme loses 10% of its activity, mutant enzyme Y136R loses 60% of its activity, mutant enzyme E150R loses 75% of its activity
70
10 min, mutant enzyme loses 66% of its activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C294S
the wild-type and the C294S mutant strains are stable after heating for 10 min at 60°C
E150R
less thermostable than wild-type enzyme, stable for 10 min at 50°C, showing a significant loss of activity at 60°C. kcat/Km for 5'-deoxyadenosine is 93fold lower than the kcat/Km for the wild-type enzyme
Y136R
less thermostable than wild-type enzyme, stable for 10 min at 50°C, showing a significant loss of activity at 60°C. kcat/Km for 5'-deoxyadenosine is 535fold lower than the kcat/Km for the wild-type enzyme
Y136R/E150R
less thermostable than wild-type enzyme. kcat/Km for 5'-deoxyadenosine is 290000fold lower than the kcat/Km for the wild-type enzyme
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