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Information on EC 3.5.4.4 - adenosine deaminase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58936

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IUBMB Comments
The enzyme, found in a wide variety of microorganisms, plants, invertebrates, and animals, plays a role in purine metabolism.
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This record set is specific for:
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: Eukaryota, Bacteria, Archaea
Reaction Schemes
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adenosine
+
H2O
=
inosine
+
NH3
+
=
+
Synonyms
adenosine deaminase, adenosine deaminase 2, adenosine aminohydrolase, adenosine deaminase 1, adaii, pvada, mj1541, ciada, sco4901, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Adenosine aminohydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
adenosine aminohydrolase
The enzyme, found in a wide variety of microorganisms, plants, invertebrates, and animals, plays a role in purine metabolism.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-93-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adenosine + H2O
inosine + NH3
show the reaction diagram
catalytic efficiency of the enzyme for 5'-deoxyadenosine is 1000fold higher than for S-methyl-5'-thioadenosine, and 10000fold hgher than with S-adenosyl-L-homocysteine or adenosine
-
-
?
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
0.072 - 0.15
adenosine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
110 - 140
adenosine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
750 - 2900
adenosine
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 only 10 min at 50°C
Y136R
less thermostable than wild-type enzyme, stable for only 10 min at 50°C
Y136R/E150R
no activity with adenosine
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