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Enzyme Nomenclature
Information on EC 2.1.1.53 - putrescine N-methyltransferase
for references in articles please use BRENDA:EC2.1.1.53
Word Map on EC 2.1.1.53
- 2.1.1.53
-
alkaloid
- nicotine
-
tropane
- tabacum
- hyoscyamine
- n-methylputrescine
- jasmonate
- spermidine
- scopolamine
- hyoscyamus
- belladonna
- atropa
- tropinone
- datura
-
meja-induced
- stramonium
- sylvestris
- acutangulus
-
4.1.1.19
-
jasmonate-induced
-
jasmonate-responsive
- n-methyltransferases
-
calystegines
-
anisodus
- synthesis
- attenuata
-
nortropane
-
burley
- analysis
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.1.1.53
-
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RECOMMENDED NAME
GeneOntology No.
putrescine N-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + putrescine = S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:putrescine N-methyltransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9075-39-2
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
overexpression of enzyme, coexpression of hyoscyamine 6 beta-hydroxylase
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the co-expression of putrescine N-methyltransferase and tropinone reductase I genes in Anisodus acutangulus hairy roots significantly improved the yields of tropane alkaloids
physiological function
-
increased expression of putrescine N-methyltransferase I results in tropane alkaloids improvement
physiological function
-
putrescine N-methyltransferase is required in nicotinic alkaloid production in Nicotiana sp.
physiological function
-
overexpression of putrescine N-methyltransferase can promote biosynthesis of tropane alkaloids in Atropa belladonna
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 1,4-diamino-2,3-dibromo-trans-but-2-ene
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + 1,4-diamino-2-hydroxybutane
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + 1,4-diamino-2-oxobutane
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + 1,4-diamino-trans-but-2-ene
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + 4-(aminomethyl)piperidine
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + N-methylputrescine
S-adenosylhomocysteine + N,N-dimethylputrescine
-
about 8% of activity compared to putrescine
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosylhomocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + trans-1,4-diamonocyclohexane
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme is probably involved in nicotine biosynthesis
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
enzyme is probably involved in nicotine biosynthesis
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
A0PFY1;
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
best substrate
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme is probably involved in nicotine biosynthesis
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
enzyme is probably involved in nicotine biosynthesis
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme is probably involved in nicotine biosynthesis
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
enzyme is probably involved in nicotine biosynthesis
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme is probably involved in nicotine biosynthesis
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme possibly may play an additional, subtle role in alkaloid metabolsim in leaf tissue
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme is probably involved in nicotine biosynthesis
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme is probably involved in nicotine biosynthesis
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme is probably involved in nicotine biosynthesis
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
B1VK31;
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
Q2KTH4;
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
-
-
-
?
additional information
?
-
-
requirement for substrate activity: two amino groups in a trans conformation, separated by four carbon atoms
-
-
-
additional information
?
-
-
substrate with little activity: 1,4 -diamino-cis-but-2-ene, not: aliphatic monoamines, 1,3-diaminopropane, 1,5-diaminopentane, N,N`-dimethyl-1,4-diamino-trans-but-2-ene, 1,3-diamino-2-hydroxypropane, 1,3-diaminoacetone, 1,4-diaminobut-2-yne, N-carbamoylputrescine
-
-
-
additional information
?
-
inactive with n-butylamine, 1,6-diaminohexane and 1,7-diaminoheptane, the PMT enzyme of potato appears to be specific for putrescine, it does not accept other mono-, di- or tri-amines
-
-
-
additional information
?
-
-
inactive with n-butylamine, 1,6-diaminohexane and 1,7-diaminoheptane, the PMT enzyme of potato appears to be specific for putrescine, it does not accept other mono-, di- or tri-amines
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
Q9S7W8, Q9XJ42
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme is probably involved in nicotine biosynthesis
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
Q9S7W8, Q9XJ42
enzyme is probably involved in nicotine biosynthesis
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
Q9XJ41
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme is probably involved in nicotine biosynthesis
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
Q9XJ41
enzyme is probably involved in nicotine biosynthesis
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme is probably involved in nicotine biosynthesis
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
Q9SB10, Q9ZWT7, Q9ZWT8, Q9ZWT9
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
Q9SB10, Q9ZWT7, Q9ZWT8, Q9ZWT9
enzyme is probably involved in nicotine biosynthesis
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme is probably involved in nicotine biosynthesis
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme possibly may play an additional, subtle role in alkaloid metabolsim in leaf tissue
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme is probably involved in nicotine biosynthesis
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme is probably involved in nicotine biosynthesis
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme catalyzes the initial reaction in the biosynthesis of tropane and pyrrolidine alkaloids from putrescine
-
?
S-adenosyl-L-methionine + putrescine
S-adenosyl-L-homocysteine + N-methylputrescine
-
enzyme is probably involved in nicotine biosynthesis
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
n-butylamine
strong inhibitor; strong inhibitor; strong inhibitor; strong inhibitor
N-methylputrescine
inhibitor with approximately competitive interaction kinetics to putrescine; inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
-
inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
-
inhibitor with approximately competitive interaction kinetics to putrescine; inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
-
inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
-
inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
-
inhibitor with approximately competitive interaction kinetics to putrescine; inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
A0PFY1;
inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
-
inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
-
inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
-
inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
inhibitor with approximately competitive interaction kinetics to putrescine; inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
-
inhibitor with approximately competitive interaction kinetics to putrescine; inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
inhibitor with approximately competitive interaction kinetics to putrescine; inhibitor with approximately competitive interaction kinetics to putrescine; inhibitor with approximately competitive interaction kinetics to putrescine; inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
-
inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
B1VK31;
inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
-
inhibitor with approximately competitive interaction kinetics to putrescine
N-methylputrescine
-
inhibitor with approximately competitive interaction kinetics to putrescine
additional information
-
no enzyme activity without the addition of S-adenosyl-L-methionine
-
additional information
-
monoamines p.e. cyclohexylamine, exo-2-aminonorborane, n-butylamine, 4-methylcyclohexylamine, cyclopentylamine; not: 1,3-diaminopropane, 2-(2-aminoethyl)pyridine, 2-aminopyridine, 3-aminopyridine, 4-aminopyridine
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
methyl jasmonate
-
considerable increase of PMTase either in the transgenic hairy roots or the control
methyl jasmonate
-
considerably increases PMTase in tobacco pmt overexpressed Hyoscyamus niger plants; enhances PMTase activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0758
putrescine
-
SPDS-PMT chimeric enzyme consisting of 144 N-terminal amino acids of spermidine synthase and 162 C-terminal amino acids of putrescine N-methyltransferase, in 20 mM HEPES, pH 8.0, 2 mM dithiothreitol, 1 mM ascorbic acid, at 37°C
0.2054
putrescine
-
wild type enzyme, in 20 mM HEPES, pH 8.0, 2 mM dithiothreitol, 1 mM ascorbic acid, at 37°C
0.5299
putrescine
-
PMT-SPDS chimeric enzyme consisting of 181 N-terminal amino acids of putrescine N-methyltransferase and 165 C-terminal amino acids of spermidine synthase, in 20 mM HEPES, pH 8.0, 2 mM dithiothreitol, 1 mM ascorbic acid, at 37°C
0.0561
S-adenosyl-L-methionine
-
wild type enzyme, in 20 mM HEPES, pH 8.0, 2 mM dithiothreitol, 1 mM ascorbic acid, at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4
putrescine
-
PMT-SPDS chimeric enzyme consisting of 181 N-terminal amino acids of putrescine N-methyltransferase and 165 C-terminal amino acids of spermidine synthase, in 20 mM HEPES, pH 8.0, 2 mM dithiothreitol, 1 mM ascorbic acid, at 37°C
0.69
putrescine
-
SPDS-PMT chimeric enzyme consisting of 144 N-terminal amino acids of spermidine synthase and 162 C-terminal amino acids of putrescine N-methyltransferase, in 20 mM HEPES, pH 8.0, 2 mM dithiothreitol, 1 mM ascorbic acid, at 37°C
5.14
putrescine
-
wild type enzyme, in 20 mM HEPES, pH 8.0, 2 mM dithiothreitol, 1 mM ascorbic acid, at 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
transcript only in potato tuber eyes at sprouting start and in 1 and 3 mm long sprouts
expressed strongly in roots; expressed strongly in roots
-
PMT activity in transgenic hairy root cultures is 5fold higher than that in the wild-type root
-
roots of decapitated plants show highest activity, no activity in leaves
-
young and old roots in developing plants, accumulates in young roots
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homology-based modeling of Datura stramonium spermidine synthase SPDS1 and putrescine N-methyltransferase PMT
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
3 h: 75% loss of activity, presence of 12.5% w/v glucose: 35% loss of activity
4
-
3 h: 75% loss of activity, presence of 12.5% w/v glucose: 35% loss of activity
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.05 M phosphate buffer, pH 7.5, 0.01 M 2-mercaptoethanol, 12.5% glucose, stable for several weeks
-
0°C, without addition of a sulfhydryl compound, most activity is lost within a few days
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration, approximately 95% pure
gel filtration, approximately 95% pure; gel filtration, approximately 95% pure
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AbPMT1 is expressed more strongly than ABPMT2 in the root; AbPMT1 is expressed more strongly than ABPMT2 in the root
-
expressed in Escherichia coli
expressed in Escherichia coli Rosetta-gami (DE3), transformed with a pET-21d vector encoding pmt
-
expressed in Escherichia coli, three genes isolated from Nicotiana sylvestris: NsPMT1, NsPMT2, NsPMT3; expressed in Escherichia coli, three genes isolated from Nicotiana sylvestris: NsPMT1, NsPMT2, NsPMT3; expressed in Escherichia coli, three genes isolated from Nicotiana sylvestris: NsPMT1, NsPMT2, NsPMT3
Q9SB10;
expressed in Escherichia coli; expressed in Escherichia coli
expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli; expressed in Escherichia coli
expressed in Rosetta-gami (DE3) cells; expressed in Rosetta-gami (DE3) cells; into vector pET21d and transferred into Escherichia coli Rosetta-gami (DE3) cells; into vector pET21d and transferred into Escherichia coli Rosetta-gami (DE3) cells
-
expressed in Rosetta-gami (DE3) cells; into vector pET21d and transferred into Escherichia coli Rosetta-gami (DE3) cells
expressed in xylem-tissues of roots, three genes isolated from Nicotiana sylvestris: NsPMT1, NsPMT2, NsPMT3, a highly conserved NsPMT 5'-flanking region is sufficient for tissue-specific and jasmonate-responsive expression of all three PMT genes; expressed in xylem-tissues of roots, three genes isolated from Nicotiana sylvestris: NsPMT1, NsPMT2, NsPMT3, a highly conserved NsPMT 5'-flanking region is sufficient for tissue-specific and jasmonate-responsive expression of all three PMT genes; expressed in xylem-tissues of roots, three genes isolated from Nicotiana sylvestris: NsPMT1, NsPMT2, NsPMT3, a highly conserved NsPMT 5'-flanking region is sufficient for tissue-specific and jasmonate-responsive expression of all three PMT genes
-
into pETat-32a(+) vector and expressed in Escherichia coli BL21trxB(DE3)
-
pmt1 and pmt2 cloned into pET-21d vector, PMT1 expressed in Escherichia coli Rosetta-gami (DE3), PMT2 expressed in Escherichia coli BL21 (DE3) and Rosetta-gami (DE3), pmt1 yields active enzymes, while pmt2 expression results in insoluble protein
-
T1 progeny of transgenic Atropa belladonna, in which putrescine N-methyltransferase (EC 2.1.1.53) from Nicotiana tabacum (NtPMT) and hyoscyamine 6beta-hydroxylase (EC 1.14.11.14) from Hyoscyamus niger (HnH6H) are overexpressed, are established to investigate tropane alkaloids biosynthesis and distribution in ripe fruits, leaves, stems, primary roots and secondary roots under field conditions. Both NtPMT and HnH6H are detected at the transcriptional level in transgenic plants, whereas they are not detected in wild-type plants. Metabolically engineering Atropa belladonna based on overexpressing NtPMT and HnH6H shows a chemotype of rich scopolamine that greatly improves the commercial and pharmaceutical properties of Atropa belladonna
-
tobacco pmt gene with a selectable marker (nptII) gene and the T-DNA of pRiA4 of Agrobacterium rhizogenes introduced into Hyoscyamus niger leaf explants using disarmed Agrobacterium tumefaciens C58C1 strain
expressed in Escherichia coli; expressed in Escherichia coli
expressed in Escherichia coli; expressed in Escherichia coli
expressed in Rosetta-gami (DE3) cells; into vector pET21d and transferred into Escherichia coli Rosetta-gami (DE3) cells
-
expressed in Rosetta-gami (DE3) cells; into vector pET21d and transferred into Escherichia coli Rosetta-gami (DE3) cells
-
expressed in Rosetta-gami (DE3) cells; into vector pET21d and transferred into Escherichia coli Rosetta-gami (DE3) cells
-
expressed in Rosetta-gami (DE3) cells; into vector pET21d and transferred into Escherichia coli Rosetta-gami (DE3) cells
-
expressed in Rosetta-gami (DE3) cells; into vector pET21d and transferred into Escherichia coli Rosetta-gami (DE3) cells
-
tobacco pmt gene with a selectable marker (nptII) gene and the T-DNA of pRiA4 of Agrobacterium rhizogenes introduced into Hyoscyamus niger leaf explants using disarmed Agrobacterium tumefaciens C58C1 strain
-
tobacco pmt gene with a selectable marker (nptII) gene and the T-DNA of pRiA4 of Agrobacterium rhizogenes introduced into Hyoscyamus niger leaf explants using disarmed Agrobacterium tumefaciens C58C1 strain
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Ag+ increases expression of putrescine N-methyltransferase I (maximum after 48 h). The expression of PMT1 reaches the highest level at 24 h treatment in ethanol
-
dark conditions and the absence of auxin upregulate enzyme promoter activity, with light being dominant to the repressive effects of auxin. Under highly repressive conditions for alkaloid synthesis, including normal culture conditions in the light, both reactive oxygen species scavengers result in significant induction of enzyme promoter activity. Treatment of callus with catalase results in the upregulation of enzyme promoter activity
-
isoform PMT1 expression is upregulated by methyl jasmonate in all tissues, reaching the highest level after 24 h of the treatment; isoform PMT2 expression is upregulated by methyl jasmonate in all tissues, reaching the highest level after 24 h of the treatment
treatments with diphenyleneiodinium chloride, Rose Bengal diacetate, and 1,2-dihydroxybenzene-3,5-disulfonic acid do not induce or repress enzyme expression
-
under normal callus growth conditions in the presence of light and auxin, enzyme promoter activity is strongly repressed
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H108L
-
40% maximal turn over velocity of wild-type, Km for S-adenosyl-L-methionine is slightly elevated, but putrescine saturation appears only at very high concentrations
additional information
-
cDNA from Nicotiana tabacum encoding PMT is introduced into the genome of a scopolamine-producing Hyoscyamus niger mediated by the disarmed Agrobacterium tumefaciens strain C58C1, which also carries Agrobacterium rhizogenes Ri plasmid pRiA4, and expressed under the control of the CaMV 35S promoter. Hairy root lines transformed with pmt present 5fold higher PMT activity than the control, and the methylputrescine levels of the resulting engineered hairy roots increase up to 5fold compared to the control and wild-type roots, but no increase in tropane alkaloids measured. After methyl jasmonate treatment, a considerable increase of PMTase and endogenous H6Hase as well as an increase in scopolamine content is found either in the transgenic hairy roots or the control
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
convenient and accurate enzyme-coupled colorimetric PMT assay, based on the conversion of S-adenosyl-L-homocysteine by 5'-methylthioacenosine/S-adenosylhomocysteine nucleosidase and S-ribosylhomocysteine lyase
synthesis
additional information
synthesis
-
overexpression of enzyme leads to enhanced N-methylputrescine levels, but the subsequent alkaloid metabolites are not affected
synthesis
-
overexpression of enzyme is not sufficient to boost scopolamine biosynthesis. Simultaneous overexpression of enzyme and hyoscyamine 6 beta-hydroxylase results in sígnificant enhancement of scopolamine accumulation
additional information
-
protein model of PMT based on the crystal structure of SPDS suggests that overall protein folds are comparable, the respective cosubstrates S-adenosylmethionine and decarboxylated S-adenosylmethionine, however, appear to bind differentially to the active sites of both enzymes, and the substrate putrescine adopts a different position
additional information
-
different polyamine catabolic processes in hypergeous and hypogeous tissues, duality in polyamine catabolic pathways involves correlation of amine oxidases with PMT for the production of nicotine alkaloids, and with POX for the lignification, cell wall formation, and vascular differentiation
additional information
-
chimera proteins obtained by fusion of fragments of Solanum tuberosum pmt2 and Hyoscyamus niger pmt are active as PMT
additional information
-
no functional protein translated from Solanum tuberosum pmt2, chimera proteins obtained by fusion of fragments of Solanum tuberosum pmt2 and Hyoscyamus niger pmt are active as PMT, if the initial part of pmt2 is used, indicating that a mutation in the terminal part of the gene causes insolubility of the enzyme
additional information
-
the deduced amino acid sequence of Anisodus tanguticus shows 92% identity with both Hyoscyamus niger and Atropa belladonna PMT
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LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.53)
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