2.5.1.22: spermine synthase
This is an abbreviated version!
For detailed information about spermine synthase, go to the full flat file.
Word Map on EC 2.5.1.22
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2.5.1.22
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polyamine
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putrescine
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s-adenosylmethionine
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ornithine
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aminopropyltransferases
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snyder-robinson
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alpha-difluoromethylornithine
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acaulis5
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thermospermine
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trans-4-methylcyclohexylamine
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gyro
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kyphoscoliosis
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agriculture
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adometdc
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2.5.1.16
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medicine
- 2.5.1.22
- polyamine
- putrescine
- s-adenosylmethionine
- ornithine
- aminopropyltransferases
-
snyder-robinson
- alpha-difluoromethylornithine
- acaulis5
- thermospermine
- trans-4-methylcyclohexylamine
-
gyro
-
kyphoscoliosis
- agriculture
- adometdc
-
2.5.1.16
- medicine
Reaction
Synonyms
ACL5, aminopropyltransferase, spermidine, OsSPMS1, SMS, spermidine aminopropyltransferase, spermine synthase, spermine synthase 1, spermine synthetase, Spm synthase, SpmS, SPMS1, SpmSyn, synthase, spermine
ECTree
2.5.1.22 spermine synthaseAdvanced search results
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results (Engineering
Engineering on EC 2.5.1.22 - spermine synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D201A
D201N
D276N
DELTA347-366
truncation of the protein at position 346 removing the last 20 residues lead to a complete loss of activity
DELTA358-366A
smaller truncation of only 9 residues has a smaller effect but still reduced activity by 75%
E353Q
G191S
the mutation at a site far away from the active pocket affects the active site dynamics and thus the functionality of SpmSyn. This suggests that SpmSyn functionality is regulated by networks of interacting residues and thus expands the functional and structural importance beyond the amino acids directly involved in the catalysis
G56S
I150T
S165D/L175E/T178H/C206R
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the mutant shows increased activity compared to the wild type enzyme
V132G
additional information
D201A
mutation of Asp201 to Ala decreases the kcat/Km for decarboxylated S-adenosylmethionine by more than 100000fold
D201N
mutation of Asp201 to Asn decreases the kcat/Km for decarboxylated S-adenosylmethionine by more than 100000fold
D276N
alteration of this residue reduces the kcat/Km for spermidine by more than 200000fold
G56S
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point mutation, leads to a large loss of spermine synthase activity, an inability to form dimers
G56S
naturally occuring missense mutation involved in Snyder-Robinson Syndrome, the mutation affects dimer and monomer stability and perturb the hydrogen bond network of the functionally important amino acids
G56S
the mutation destabilizes the enzyme homodimer and thus abolishes enzymatic activity
I150T
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point mutation, leads to a large loss of spermine synthase activity, an inability to form dimers
I150T
naturally occuring missense mutation involved in Snyder-Robinson Syndrome, the mutation affects dimer and monomer stability and perturb the hydrogen bond network of the functionally important amino acids
V132G
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point mutation, leads to a large loss of spermine synthase activity, an inability to form dimers
V132G
naturally occuring missense mutation involved in Snyder-Robinson Syndrome, the mutation affects dimer and monomer stability and perturb the hydrogen bond network of the functionally important amino acids
additional information
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the loss-of-function mutant of gene ACAULIS5 shows a severe defect in stem elongation, isolation of a T-DNA insertion mutant of gene SPMS, i.e. spms-1, showing decreased spermine levels but no obvious phenotypic alterations, an acl5-spms-1 double mutant contains no spermine but is fully viable as the wild-type and shows no phenotypic alterations under normal growth conditions, overview
additional information
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enzyme overexpression in transgenic mice under control of a composite CMV-IE enhancer-chicken beta-actin promotor causes no deleterious effects, the mice show normal growth, fertility, and behaviour, the content of S-adenosylmethionine in transgenic mice is important for viability, overview
additional information
deletion of the N-terminal domain leads to a complete loss of spermine synthase activity
additional information
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deletion of the N-terminal domain leads to a complete loss of spermine synthase activity
additional information
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mutation p.G56S in the N-terminal region of spermine synthase greatly reduces spermine synthase activity and leads to severe epilepsy and cognitive impairment related to Snyder-Robinson X-linked recessive mental retardation syndrome
additional information
enzyme is able to functionally complement spermine deficiency in yeast
additional information
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enzyme is able to functionally complement spermine deficiency in yeast
additional information
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enzyme null mutant, lack of spermine increases sensitivity of cells to anti-tumor agents
additional information
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yeast does not require spermine synthase since mutants in which this enzyme is deleted are viable and grow at a normal rate
