Information on EC 2.1.1.7 - nicotinate N-methyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.7
-
RECOMMENDED NAME
GeneOntology No.
nicotinate N-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + nicotinate = S-adenosyl-L-homocysteine + N-methylnicotinate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
trigonelline biosynthesis
-
-
Nicotinate and nicotinamide metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:nicotinate N-methyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9029-79-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
151, duckweed
-
-
Manually annotated by BRENDA team
151, duckweed
-
-
Manually annotated by BRENDA team
pea
-
-
Manually annotated by BRENDA team
i.e. Vigna radiate
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + 1-methylnicotinate
show the reaction diagram
S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + N-methylnicotinate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + 1-methylnicotinate
show the reaction diagram
S-adenosyl-L-methionine + nicotinate
S-adenosyl-L-homocysteine + N-methylnicotinate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no requirement for divalent cations
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Benzoic acid
-
-
Heavy metal ions
-
-
-
Isonicotinic acid
-
-
Mg2+
-
slight
p-hydroxymercuribenzoate
-
-
parahydroxymercuric benzoate
-
at 0.1 mM, reversible by 10 mM DTT
Picolinic acid
-
-
Pyrazinamide
-
-
S-adenosyl-L-homocysteine
-
-
salicylic acid
-
-
SH-blocking reagents
-
-
-
Trigonelline
-
i.e. N-methylnicotinic acid
additional information
-
nicotinic acid and nicotinamide inhibit the growth of roots
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0125 - 0.4
nicotinate
0.031 - 0.1
S-adenosyl-L-methionine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000013
-
crude extract of cotyledons
0.0000032
-
crude extract of embryonic axes
0.0031
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3 - 8.8
-
half-maximal activity at pH 5.4 and pH 7.5
5 - 9
-
pH 5.0: about 50% of maximum activity, pH 9.0: nearly inactive
5.2 - 8.5
-
about 55% of maximum activity at pH 5.2 and 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 40
-
-
40 - 45
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 50
-
50% remaining activity at 50C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
heterotrophic
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
enzyme activity increases in embryonic axes, but decreases in cotyledons during germination
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85000
-
ge filtration
90000
-
ultracentrifugation, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 41500, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10 mM DTT and 20% glycerol stabilize the unstable enzyme during purification and storage
-
no stabilization by glycerol, 10-40% v/v, or nicotinic acid
-
sulfhydryl group protecting agents required for stabilization during purification
-
total loss of activity by freezing at -20C
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
rigorous exclusion of O2 by saturating the buffer with N2 allows partial stabilization during purification
-
441222
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, purified enzyme, 20 mM Tris-HCl, pH 8.0, 20 mM DTT, 20% glycerol, stable for 14 days
-
4C, 24 h, N2-atmosphere
-
4C, purified enzyme, 20 mM Tris-HCl, pH 8.0, 20 mM DTT, 20% glycerol, stable for 3 days
-
4C, purified enzyme, 20 mM Tris-HCl, pH 8.0, 20% glycerol, complete loss of activity within 24 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2650fold from leaves, to homogeneity, by ammonium sulfate fractionation, DEAE ion exchange chromatography, adenosine affinity chromatography, hydroxyl apatite chromatography, and gel filtration
-