Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

2.5.1.16: spermidine synthase

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

Word Map on EC 2.5.1.16

Reaction

S-adenosyl 3-(methylsulfanyl)propylamine
+
putrescine
=
S-methyl-5'-thioadenosine
+
spermidine

Synonyms

aminopropyltransferase, aminopropyltransferase spermidine synthase, AtSPDS1, AtSPDS2, MdSPDS1, PAPT, PgSPD, putrescine aminopropyltransferase, Spd synthase, SPDS, SPDS2, SPDSYN, spe-sdh, spe3, SpeE, spermidine synthase, spermidine synthase 1, spermidine synthetase, Spm synthase, SpSyn, Synpcc7942_0628, synthase, spermidine

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.16 spermidine synthase

Engineering

Engineering on EC 2.5.1.16 - spermidine synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C159A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D158A
site-directed mutagenesis, inactive mutant
D161A
site-directed mutagenesis, inactive mutant
I163A
site-directed mutagenesis, replacement of Ile163 has no influence on EcSDPS activity
P162A
site-directed mutagenesis, replacement of Pro162 has no influence on EcSDPS activity
P165Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T160A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D196N
-
site-directed mutagenesis, the mutant activity is reduced by 89% compared to the wild-type enzyme
S197A
-
site-directed mutagenesis, the mutant activity is reduced by 24% compared to the wild-type enzyme
Y102A
-
site-directed mutagenesis, the mutant activity is reduced by 91% compared to the wild-type enzyme
D101I
site-directed mutagenesis, almost inactive mutant
D170A
site-directed mutagenesis, the mutsnt shows reduced activity compared to the wild-type enzyme
D173A
site-directed mutagenesis, the mutsnt shows reduced activity compared to the wild-type enzyme
Y76F
site-directed mutagenesis, the mutsnt shows reduced activity compared to the wild-type enzyme
additional information