Information on EC 3.5.4.31 - S-methyl-5'-thioadenosine deaminase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
3.5.4.31
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RECOMMENDED NAME
GeneOntology No.
S-methyl-5'-thioadenosine deaminase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-methyl-5'-thioadenosine + H2O = S-methyl-5'-thioinosine + NH3
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Cysteine and methionine metabolism
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Metabolic pathways
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S-methyl-5'-thioadenosine degradation III
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SYSTEMATIC NAME
IUBMB Comments
S-methyl-5'-thioadenosine amidohydrolase
The enzyme from Thermotoga maritima also functions as S-adenosylhomocysteine deaminase (EC 3.5.4.28) and has some activity against adenosine. Adenosine 5'-phosphate and S-adenosyl-L-methionine (SAM) are not substrates.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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
allopurinol + NH3
show the reaction diagram
adenosine + H2O
inosine + NH3
show the reaction diagram
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?
S-methyl-5'-thioadenosine + H2O
5'-S-methyl-5'-thioinosine + NH3
show the reaction diagram
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?
S-methyl-5'-thioadenosine + H2O
S-methyl-5'-thioinosine
show the reaction diagram
S-methyl-5'-thioadenosine + H2O
S-methyl-5'-thioinosine + NH3
show the reaction diagram
additional information
?
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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
S-methyl-5'-thioadenosine + H2O
5'-S-methyl-5'-thioinosine + NH3
show the reaction diagram
Q9X034
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?
S-methyl-5'-thioadenosine + H2O
S-methyl-5'-thioinosine + NH3
show the reaction diagram
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
additional information
metal-dependent enzyme. The metal can not be removed from the enzyme nor can the nature of the catalytic metal be established. Dialysis of the wild-type enzyme for 3 days against a dipicolinic acid containing buffer fails to show any lowering enzyme activity, again indicating that chelation is not able to remove the bound metal in the active site. The catalytic metal is not removed by EDTA
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-deoxycoformycin
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5'-methylthio-2'-deoxycoformycin
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5'-methylthiocoformycin
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5'-phenylthio-2'-deoxycoformycin
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5'-propylthio-2'-deoxycoformycin
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additional information
the presence of 0.02 M dithiothreitol has no effect on the enzymatic activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.046 - 0.25
adenosine
0.0015 - 0.11
S-methyl-5'-thioadenosine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3 - 140
adenosine
1.39 - 220
S-methyl-5'-thioadenosine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.2 - 2900
adenosine
122
19 - 16000
S-methyl-5'-thioadenosine
1578
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000037
2'-deoxycoformycin
at pH 7.4 and 25°C
0.00000008
5'-methylthio-2'-deoxycoformycin
at pH 7.4 and 25°C
0.0000000048
5'-methylthiocoformycin
at pH 7.4 and 25°C
0.00000013
5'-phenylthio-2'-deoxycoformycin
at pH 7.4 and 25°C
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0.000000067
5'-propylthio-2'-deoxycoformycin
at pH 7.4 and 25°C
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0.00009
coformycin
at pH 7.4 and 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000003
5'-methylthiocoformycin
Pseudomonas aeruginosa
Q9HZ64
at pH 7.4 and 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with 5'-methylthiocoformycin, hanging or sitting drop vapor diffusion method, using 1.26 M sodium phosphate (monobasic) and 0.14 M potassium phosphate (dibasic) at a final pH of 5.6 at 18°C
X-ray crystal structure of the complex between Tm0936 and the product resulting from the deamination of SAH, S-inosylhomocysteine
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 - 70
the enzyme shows 90% of retained activity after 10 min at 60°C and 34% of retained activity after 10 min at 70°C
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
Ni-NTA column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL cells
expressed in Escherichia coli CodonPlus(DE3)-RIL cells; 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 only 10 min at 50°C; the mutant shows about 4fold increased activity compared to the wild type
Y136R
less thermostable than wild-type enzyme, stable for only 10 min at 50°C; the mutant shows about 10fold increased activity compared to the wild type
Y136R/E150R
no activity with adenosine; the mutant shows strongly reduced activity compared to the wild type
Show AA Sequence (1993 entries)
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