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3.5.4.2: adenine deaminase

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

Word Map on EC 3.5.4.2

Reaction

adenine
+
H2O
=
hypoxanthine
 +
NH3

Synonyms

aadA, AAH, Aah1p, AAur1117, ADA, ADase, ADE, adenase, adenine aminase, adenine deaminase, KLLAOE2317, MJ1459, NadA, Pa0148, Sgx9403e, Sgx9403g

ECTree

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

Engineering

Engineering on EC 3.5.4.2 - adenine deaminase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D118N
-
mutant is able to bind 2 metals per active site, kcat (adenine): 173/sec
D284A
-
mutants is able to bind two equivalents of Mn2+ or Fe2+ in the active site but mutant is unable to catalyze the deaminase reaction
D285A
-
mutant is able to bind 2 metals per active site, kcat (adenine): 37/sec
D474N
-
mutant is able to bind 2 metals per active site, kcat (adenine): 171/sec
E121Q
-
mutant is able to bind 2 metals per active site, kcat (adenine): 57/sec
E185Q
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
E236Q
-
mutants is able to bind two equivalents of Mn2+ or Fe2+ in the active site but mutant is unable to catalyze the deaminase reaction
H120N
-
mutant is able to bind 2 metals per active site, kcat (adenine): 0.13/sec
H214N
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H214Q
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H235C
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H235D
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H235N
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H235Q
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H473N
-
mutant is able to bind 2 metals per active site, kcat (adenine): 178/sec
H90C
-
mutant is unable to bind either iron or manganese
H90D
-
mutant is unable to bind either iron or manganese
H90N
-
mutant is able to bind two equivalents of Mn2+ or Fe2+ per monomer and shows a kcat of about 5% of the wild-type enzyme
H90Q
-
mutant is unable to bind either iron or manganese
H92C
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H92D
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H92N
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
H92Q
-
mutant shows total loss of catalytic activity as well as the ability to bind divalent metals in the active site
S95A
-
mutant is able to bind 2 metals per active site, kcat (adenine): 78/sec
C127A
-
10fold decrease in kcat over the wild-type
C127S
-
complete loss of activity
C127A
-
10fold decrease in kcat over the wild-type
-
C127S
-
complete loss of activity
-
additional information