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Information on EC 3.5.4.41 - 5'-deoxyadenosine deaminase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58936

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IUBMB Comments
The enzyme from the archaeon Methanocaldococcus jannaschii is involved in the recycling of 5'-deoxyadenosine.
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Methanocaldococcus jannaschii
UNIPROT: Q58936
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
5'-deoxyadenosine deaminase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
5'-deoxyadenosine aminohydrolase
The enzyme from the archaeon Methanocaldococcus jannaschii is involved in the recycling of 5'-deoxyadenosine.
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 SUBSTRATE
NATURAL 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
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
-
-
?
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
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Miller, D.; O'Brien, K.; Xu, H.; White, R.H.
Identification of a 5'-deoxyadenosine deaminase in Methanocaldococcus jannaschii and its possible role in recycling the radical S-adenosylmethionine enzyme reaction product 5'-deoxyadenosine
J. Bacteriol.
196
1064-1072
2013
Methanocaldococcus jannaschii (Q58936), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58936)
Manually annotated by BRENDA team