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3.5.4.4: adenosine deaminase

This is an abbreviated version!
For detailed information about adenosine deaminase, go to the full flat file.

Word Map on EC 3.5.4.4

Reaction

adenosine
+
H2O
=
Inosine
 +
NH3

Synonyms

AD, ADA, ADA1, ADA2, ADAI, ADAII, ADAIII, Adenosine aminohydrolase, adenosine deaminase, adenosine deaminase 1, adenosine deaminase 2, ciADA, HadA, LADA, MadA, MJ1541, PvADA, SADA, SCO4901, TadA

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.4 In cyclic amidines
                3.5.4.4 adenosine deaminase

Engineering

Engineering on EC 3.5.4.4 - adenosine deaminase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M155D
mutation reduces kcat
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
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
-
C27Q/L227I
the mutation promotes crystallization via crystal packing and to prevents intermolecular disulfide bond formation. The surface engineered enzyme is kinetically comparable to the wild type enzyme
D176A
mutation reduces adenosine and 5'-methylthioadenosine substrate affnity
D176M
mutation reduces adenosine and 5'-methylthioadenosine substrate affnity
F136L
mutant enzyme shows increased Km (more than 10fold) for adenosine and 5'-methylthioinosine
T174A
mutation affects 5'-methylthioadenosine binding affinity
T174I
mutation affects 5'-methylthioadenosine binding affinity
D172
-
mutant is 40% less active than the wild-type. Mutant is more thightly bound to erythro-9-(2-hydroxy-3-nonly)adenine (Ki: 0.0009 mM) than wild-type
D172A
-
the mutant shows no activity with 5-methylthioadenosine and is not inhibited by 5'-methylthiocoformycin
D172E
-
the mutant shows no activity with 5-methylthioadenosine and is not inhibited by 5'-methylthiocoformycin
additional information