2.1.1.28: phenylethanolamine N-methyltransferase
This is an abbreviated version!
For detailed information about phenylethanolamine N-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.28
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2.1.1.28
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catecholamine
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medulla
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hydroxylase
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adrenergic
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dopamine
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chromaffin
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beta-hydroxylase
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glucocorticoid
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sympathetic
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rostrally
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catecholaminergic
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noradrenergic
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innervation
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ventrolateral
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hypothalamic
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corticosterone
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catecholamine-synthesizing
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oblongata
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dopamine-beta-hydroxylase
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pnmt-immunoreactive
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perikarya
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tractus
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adrenomedullary
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proenkephalin
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dorsomedial
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sympathoadrenal
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intermediolateral
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alpha2-adrenoceptor
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1,2,3,4-tetrahydroisoquinoline
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coeruleus
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phenylethanolamine-n-methyltransferase
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postrema
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pnmt-ir
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medicine
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bulbospinal
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normetanephrine
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solitarii
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analysis
- 2.1.1.28
- catecholamine
- medulla
- hydroxylase
-
adrenergic
- dopamine
-
chromaffin
- beta-hydroxylase
- glucocorticoid
-
sympathetic
-
rostrally
-
catecholaminergic
-
noradrenergic
-
innervation
-
ventrolateral
- hypothalamic
- corticosterone
-
catecholamine-synthesizing
- oblongata
- dopamine-beta-hydroxylase
-
pnmt-immunoreactive
- perikarya
-
tractus
-
adrenomedullary
- proenkephalin
-
dorsomedial
-
sympathoadrenal
-
intermediolateral
-
alpha2-adrenoceptor
- 1,2,3,4-tetrahydroisoquinoline
-
coeruleus
-
phenylethanolamine-n-methyltransferase
-
postrema
-
pnmt-ir
- medicine
-
bulbospinal
- normetanephrine
-
solitarii
- analysis
Reaction
Synonyms
hPNMT, methyltransferase, noradrenaline N-, NMT, noradrenalin methyltransferase, noradrenalin N-methyltransferase, noradrenaline N-methyltransferase, norepinephrin N-methyltransferase, norepinephrine methyltransferase, norepinephrine N-methyltransferase, phenethanolamine methyltransferase, phenethanolamine N-methyltransferase, PNMT
ECTree
2.1.1.28 phenylethanolamine N-methyltransferaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.1.1.28 - phenylethanolamine N-methyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C131S
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mutant enzyme shows similar KM-values and maximal velocity to those of the wild-type enzyme
C139A
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the C139A mutant separates into two forms on gel filtration, consistent with a monomer and dimer form, the equilibrium is significantly shifted in favour of the monomer. C139A mutant has similar kinetic constants as the wild type human phenylethanolamine N-methyltransferase
C139S
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mutant enzyme shows similar KM-values and maximal velocity to those of the wild-type enzyme
C183S
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mutant enzyme shows markedly reduced enzyme activity with less than 3% of the maximal activity of the wild-type enzyme, and ca. sixfold increased apparent KM-value for both substrates
C48A
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the C48A mutant separates into two forms on gel filtration, consistent with a monomer and dimer form, the equilibrium is significantly shifted in favour of the monomer. C48A mutant has similar kinetic constants as the wild type human phenylethanolamine N-methyltransferase. The monomer-dimer equilibrium in analytical ultracentrifugation for the dimer fractions of phenylethanolamine N-methyltransferase-His and C48A phenylethanolamine N-methyltransferase is 10fold lower than for the monomer fractions (Kd 35-64 microM and 305-551 microM, respectively). The relative Kd values show that C48A phenylethanolamine N-methyltransferase is less likely to form dimer than phenylethanolamine N-methyltransferase-His.
C48A/C139A
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similar kinetic constants as the wild type human phenylethanolamine N-methyltransferase
C48S
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mutant enzyme shows similar KM-values and maximal velocity to those of the wild-type enzyme
C60S
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mutant enzyme shows similar KM-values and maximal velocity to those of the wild-type enzyme
C91S
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mutant enzyme shows similar KM-values and maximal velocity to those of the wild-type enzyme
E185A
Kcat value is reduced by 15fold. Similar Km for phenylethanolamine and slightly lower Km for AdoMet than the wild type enzyme.
E185D
Kcat value is reduced by 3fold. Moderately increased Km values for phenylethanolamine and AdoMet
E185Q
E219Q
K75A
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crystal structure determination and comparison to the wild-type enzyme structure
Y35F
reduced level of binding of phenylethanolamine and AdoMet. The catalytic rate is not greatly affected by the Y35F mutation.
additional information
E185Q
kcat value reduced by about 300fold. Similar Km for phenylethanolamine and slightly lower Km for AdoMet than the wild type enzyme.
E185Q
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mutant has the same Km value as the wild-type hPNMT but extremely lower kcat value. E185Q mutation presents obvious structural changes in the active site
E219Q
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mutation has little effect on the kcat value. The bridge water still forms two hydrogen bonds between Gln219 and Glu185
additional information
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rs3764351 and rs876493 polymorphisms in gene PNMT are correlated to reward dependence, overview
additional information
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construction of enzyme knockout mutant mice, that show resting cardiovascular function, including blood pressure, heart rate, and cardiac output similar to that in wild-type mice, and the basal norepinephrine plasma level is unaltered. However, inhibition of sympathetic innervation with the ganglion blocker hexamethonium causes a 54% smaller decrease in blood pressure in KO mice compared to wild-type mice, and treadmill exercise causes an 11% higher increase in blood pressure, both suggesting impaired vasodilation in KO mice, the enzyme knockout does not change the heart rate response to ganglionic blockade and exercise. KO mice have an increased ratio of left ventricular posterior wall thickness to internal dimensions but do not have cardiac hypertrophy, in restrained, awake KO mice, heart rate and ejection fraction remain unaltered, but cardiac output is significantly reduced because of diminished end-diastolic volume, phenotype, overview
additional information
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construction of PNMT promoter constructs using nested deletion constructs treated with DEX or sequentially with GDNF/cAMP/DEX, the suppression of PNMT induction is reversible
additional information
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construction of enzyme knockout mutant mice, that show resting cardiovascular function, including blood pressure, heart rate, and cardiac output similar to that in wild-type mice, and the basal norepinephrine plasma level is unaltered. However, inhibition of sympathetic innervation with the ganglion blocker hexamethonium causes a 54% smaller decrease in blood pressure in KO mice compared to wild-type mice, and treadmill exercise causes an 11% higher increase in blood pressure, both suggesting impaired vasodilation in KO mice, the enzyme knockout does not change the heart rate response to ganglionic blockade and exercise. KO mice have an increased ratio of left ventricular posterior wall thickness to internal dimensions but do not have cardiac hypertrophy, in restrained, awake KO mice, heart rate and ejection fraction remain unaltered, but cardiac output is significantly reduced because of diminished end-diastolic volume, phenotype, overview
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