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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
nanmt, trigonelline synthase, nicotinate n-methyltransferase, s-adenosyl-l-methionine:nicotinic acid-n-methyltransferase,
more
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furanocoumarin 8-methyltransferase
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furanocoumarin 8-O-methyltransferase
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methyltransferase, nicotinate
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nicotinate methyltransferase
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nicotinic acid methyltransferase
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S-adenosyl-L-methionine:nicotinic acid-N-methyltransferase
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trigonelline synthase
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S-adenosyl-L-methionine + nicotinate = S-adenosyl-L-homocysteine + N-methylnicotinate
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methyl group transfer
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S-adenosyl-L-methionine:nicotinate N-methyltransferase
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S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + 1-methylnicotinate
S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + N-methylnicotinate
S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + 1-methylnicotinate
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S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + 1-methylnicotinate
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high specificity for nicotinate, no other pyridine derivative is a suitable methyl group acceptor
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?
S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + 1-methylnicotinate
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S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + 1-methylnicotinate
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S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + 1-methylnicotinate
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i.e. trigonelline
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S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + 1-methylnicotinate
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trigonelline biosynthesis
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S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + N-methylnicotinate
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S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + N-methylnicotinate
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key enzyme in regulating the metabolic flux through the nicotinamide pathway
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S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + N-methylnicotinate
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specific for nicotinic acid
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S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + N-methylnicotinate
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S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + N-methylnicotinate
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enzyme is involved in metabolism of nicotinic acid and nicotinamide, trigonelline and pyridine nucleotide pathway overview
i.e. trigonelline
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?
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S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + 1-methylnicotinate
S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + N-methylnicotinate
S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + 1-methylnicotinate
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S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + 1-methylnicotinate
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S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + 1-methylnicotinate
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S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + 1-methylnicotinate
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trigonelline biosynthesis
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S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + N-methylnicotinate
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key enzyme in regulating the metabolic flux through the nicotinamide pathway
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?
S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + N-methylnicotinate
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enzyme is involved in metabolism of nicotinic acid and nicotinamide, trigonelline and pyridine nucleotide pathway overview
i.e. trigonelline
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?
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additional information
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no requirement for divalent cations
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p-hydroxymercuribenzoate
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parahydroxymercuric benzoate
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at 0.1 mM, reversible by 10 mM DTT
S-adenosyl-L-homocysteine
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SH-blocking reagents
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Trigonelline
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i.e. N-methylnicotinic acid
additional information
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nicotinic acid and nicotinamide inhibit the growth of roots
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Hg2+
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Hg2+
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at 1 mM, reversible by 10 mM DTT
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0.031 - 0.1
S-adenosyl-L-methionine
0.0125
nicotinate
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pH 7.0, 35°C
0.0387
nicotinate
pH 7.5, 28°C
0.031
S-adenosyl-L-methionine
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pH 7.0, 35°C
0.055
S-adenosyl-L-methionine
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0.055
S-adenosyl-L-methionine
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nicotinate
0.1
S-adenosyl-L-methionine
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3.52
nicotinate
pH 7.5, 28°C
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91
nicotinate
pH 7.5, 28°C
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0.0000013
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crude extract of cotyledons
0.0000032
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crude extract of embryonic axes
additional information
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additional information
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determination of trigonelline content in vivo in seedlings during germination, overview
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4.3 - 8.8
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half-maximal activity at pH 5.4 and pH 7.5
5 - 9
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pH 5.0: about 50% of maximum activity, pH 9.0: nearly inactive
5.2 - 8.5
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about 55% of maximum activity at pH 5.2 and 8.5
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30
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40 - 50
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50% remaining activity at 50°C
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UniProt
brenda
151, duckweed
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brenda
151, duckweed
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brenda
pea
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brenda
i.e. Vigna radiate
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brenda
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brenda
soybean
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brenda
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heterotrophic
brenda
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brenda
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enzyme activity increases in embryonic axes, but decreases in cotyledons during germination
brenda
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brenda
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brenda
additional information
product N-methylnicotinate accumulates predominantly in inflorescence tissues
brenda
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brenda
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etiolated
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physiological function
homozygous mutant lines show marked reductions in N-methylnicotinate accumulation in inflorescence tissues, whereas the levels of nicotinate, glucosylated nicotinate, nicotinate mononucleotide, and NAD are increased. Overexpressing lines have higher N-methylnicotinate content and lower nicotinate, glucosylated nicotinate, nicotinate mononucleotide, and NAD contents
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NAMT1_ARATH
359
0
39688
Swiss-Prot
other Location (Reliability: 5 )
NAMT1_ORYSJ
365
0
38647
Swiss-Prot
other Location (Reliability: 2 )
NAMT1_SOYBN
355
0
39914
Swiss-Prot
other Location (Reliability: 4 )
C3VIX6_9ASTR
362
0
40849
TrEMBL
other Location (Reliability: 3 )
L7RZC0_9ERIC
367
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41307
TrEMBL
other Location (Reliability: 2 )
K7W3L6_9NOST
1064
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122847
TrEMBL
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MTH1_HAEPH
327
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36996
Swiss-Prot
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41500
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2 * 41500, SDS-PAGE
90000
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ultracentrifugation, gel filtration
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dimer
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2 * 41500, SDS-PAGE
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10 mM DTT and 20% glycerol stabilize the unstable enzyme during purification and storage
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no stabilization by glycerol, 10-40% v/v, or nicotinic acid
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sulfhydryl group protecting agents required for stabilization during purification
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total loss of activity by freezing at -20°C
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rigorous exclusion of O2 by saturating the buffer with N2 allows partial stabilization during purification
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441222
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-20°C, purified enzyme, 20 mM Tris-HCl, pH 8.0, 20 mM DTT, 20% glycerol, stable for 14 days
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4°C, 24 h, N2-atmosphere
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4°C, purified enzyme, 20 mM Tris-HCl, pH 8.0, 20 mM DTT, 20% glycerol, stable for 3 days
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4°C, purified enzyme, 20 mM Tris-HCl, pH 8.0, 20% glycerol, complete loss of activity within 24 h
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2650fold from leaves, to homogeneity, by ammonium sulfate fractionation, DEAE ion exchange chromatography, adenosine affinity chromatography, hydroxyl apatite chromatography, and gel filtration
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Joshi, J.G.; Handler, P.
Biosynthesis of trigonelline
J. Biol. Chem.
235
2981-2983
1960
Pisum sativum
brenda
Taguchi, H.; Nishitani, H.; Okumura, K.; Shimabayashi, Y.; Iwai, K.
Biosynthesis and metabolism of trigonelline in Lemna paucicostata 151
Agric. Biol. Chem.
53
2867-2871
1989
Lemna aequinoctialis, Lemna aequinoctialis 151
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brenda
Upmeier, B.; Gross, W.; Kster, S.; Barz, W.
Purification and properties of S-adenosyl-L-methionine:nicotinic acid-N-methyltransferase from cell suspension cultures of Glycine max L
Arch. Biochem. Biophys.
262
445-454
1988
Glycine max
brenda
Chen, X.; Wood, A.J.
Purification and characterization of S-adenosyl-L-methionine:nicotinic acid-N-methyltransferase from leaves of Glycine max
Biol. Plant.
48
531-535
2004
Glycine max
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brenda
Zheng, X.Q.; Hayashibe, E.; Ashihara, H.
Changes in trigonelline (N-methylnicotinic acid) content and nicotinic acid metabolism during germination of mungbean (Phaseolus aureus) seeds
J. Exp. Bot.
56
1615-1623
2005
Vigna radiata var. radiata
brenda
Li, W.; Zhang, F.; Wu, R.; Jia, L.; Li, G.; Guo, Y.; Liu, C.; Wang, G.
A novel N-methyltransferase in Arabidopsis appears to feed a conserved pathway for nicotinate detoxification among land plants and is associated with lignin biosynthesis
Plant Physiol.
174
1492-1504
2017
Arabidopsis thaliana (Q9SCP7)
brenda
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