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2.3.1.57: diamine N-acetyltransferase

This is an abbreviated version!
For detailed information about diamine N-acetyltransferase, go to the full flat file.

Word Map on EC 2.3.1.57

Reaction

acetyl-CoA
+
an alkane-alpha,omega-diamine
=
CoA
 +
an N-acetyldiamine

Synonyms

acetyl-coenzyme A-1,4-diaminobutane N-acetyltransferase, acetyltransferase, putrescine, bltD, CpSSAT, diamine acetyltransferase, More, N1-SAT, N1-spermidine/spermine acetyltransferase, N1SSAT, PaiA, putrescine (diamine)-acetylating enzyme, putrescine acetylase, putrescine acetyltransferase, putrescine N-acetyltransferase, SAT, SAT1, SpeG, spermidine /spermine N1-acetyltransferase, spermidine acetyltransferase, spermidine N-acetyltransferase, spermidine N1-acetyltransferase, spermidine-spermine acetyltransferase, spermidine-spermine N1-acetyltransferase, spermidine/spermine acetyltransferase, spermidine/spermine N-acetyltransferase, spermidine/spermine N1-acetyltransferase, spermidine/spermine N1-acetyltransferase 1, spermidine/spermine N1-acetyltransferase 2, spermidine/spermine N1-acetyltransferase-1, spermidine/spermine-N 1-acetyltransferase, spermidine/spermine-N1-acetyltransferase, spermidine/spermine-N1-acetyltransferase activity, SSAT, SSAT-1, SSAT-2, SSAT1, SSAT2, SSATX, Ste27, Ta0374, VCA0947

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.57 diamine N-acetyltransferase

Engineering

Engineering on EC 2.3.1.57 - diamine N-acetyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L156F
-
mutant enzyme shows about 20fold reduced activity and over 70fold reduced activation by the polyamine analogue N1,N11-bis(ethyl)norspermine compared to the wild-type enzyme, expression of the mutant enzymes decreases cellular sensitivity to N1,N11-bis(ethyl)norspermine
E33Q
the mutant shows greatly reduced enzyme activity compared to the wild type enzyme
E55Q
the mutant shows greatly reduced enzyme activity compared to the wild type enzyme
E74Q
the mutant shows greatly reduced enzyme activity compared to the wild type enzyme
E83Q
the mutant shows greatly reduced enzyme activity compared to the wild type enzyme
O85E
the mutant shows greatly reduced enzyme activity compared to the wild type enzyme
Q53A
the mutant shows greatly reduced enzyme activity compared to the wild type enzyme
Y133F
the mutant shows increased enzyme activity compared to the wild type enzyme
E33Q
-
the mutant shows greatly reduced enzyme activity compared to the wild type enzyme
-
E55Q
-
the mutant shows greatly reduced enzyme activity compared to the wild type enzyme
-
E71Q
-
inactive
-
E74Q
-
the mutant shows greatly reduced enzyme activity compared to the wild type enzyme
-
Y133F
-
the mutant shows increased enzyme activity compared to the wild type enzyme
-
E152Q
-
mutation disrupts binding of stabilizing N1,N12-bis(ethyl)spermine to enzyme
E170Stop
-
mutation stabilizes enzyme, due to the lack of ubiquinated complexes
E171Q
-
mutation results in a marked stabilization of enzyme, due to the lack of formation of high-molecular-mass complexes with ubiquitin
E172A
-
mutation stabilizes enzyme, due to the lack of ubiquinated complexes
E173A
-
mutation stabilizes enzyme, due to the lack of ubiquinated complexes
K111R
-
mutant with the same activity as wild-type enzyme, but reduced half-life
K141R
-
mutant with 35% of activity of wild-type enzyme, increased Km for spermidine and reduced half-life
K158R
-
mutant with 139% of activity of wild-type enzyme
K161R
-
mutant with the same activity as wild-type enzyme
K166R
-
mutant with 78% of activity of wild-type enzyme
K22R
-
mutant with 149% of activity of wild-type enzyme, but reduced half-life
K26R
-
mutant with 120% of activity of wild-type enzyme
K39R
-
mutant with the same activity as wild-type enzyme
K3R
-
mutant with 134% of activity of wild-type enzyme
K61R
-
mutant with the same activity as wild-type enzyme
K87R
-
mutant with 70% of activity of wild-type enzyme, but significantly longer half-life, suggesting that Lys-87 may be the preferred site for ubiquination
R101K
site-directed mutagenesis of SSAT1 protein, ability to promote hypoxia-inducible factor-1 (HIF-1alpha) degradation reduced
S82D/T83A
-
inactive mutant
D93N
site-directed mutagenesis, the mutation affects both substrate binding and catalysis without changing the pH dependence of the enzyme
E92Q
site-directed mutagenesis, the mutation has a detrimental effect on both substrate binding and catalysis and shifts the optimal pH for enzyme activity further into alkaline solution conditions
K87R
-
the mutant has a longer half-life than wild type or any of the other mutants
additional information