Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.1.273 extracted from

  • Murfitt, L.M.; Kolosova, N.; Mann, C.J.; Dudareva, N.
    Purification and characterization of S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase, the enzyme responsible for biosynthesis of the volatile ester methyl benzoate in flowers of Antirrhinum majus (2000), Arch. Biochem. Biophys., 382, 145-151.
    View publication on PubMed
Search for more literature for 2.1.1.273

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ 5 mM, slight inhibitory effect, less than 10% inhibition Antirrhinum majus
Cu2+ 5 mM, strong inhibitory effect, 75–100% inhibition Antirrhinum majus
Fe2+ 5 mM, strong inhibitory effect, 75–100% inhibition Antirrhinum majus
Mn2+ 5 mM, slight inhibitory effect, less than 10% inhibition Antirrhinum majus
Na+ 5 mM, slight inhibitory effect, less than 10% inhibition Antirrhinum majus
S-adenosyl-L-homocysteine competitive inhibition with respect to S-adenosyl-L-methionine and noncompetitive inhibition with respect to benzoate Antirrhinum majus
Zn2+ 5 mM, slight inhibitory effect, less than 10% inhibition Antirrhinum majus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.028
-
 S-adenosyl-L-methionine apparent Km-value of plant-purified protein, pH 7.5, 20°C Antirrhinum majus
0.087
-
 S-adenosyl-L-methionine apparent Km-value of recombinant protein, pH 7.5, 20°C Antirrhinum majus
1.1
-
 benzoate apparent Km-value of plant-purified protein, pH 7.5, 20°C Antirrhinum majus
1.6
-
 benzoate apparent Km-value of recombinant protein, pH 7.5, 20°C Antirrhinum majus

Metals/Ions

Metals/Ions Comment Organism Structure
K+ 5 mM, stimulates BAMT activity by a factor of 2 Antirrhinum majus
Mg2+ BAMT activity not affected by the presence of 5 mM Antirrhinum majus
NH4+ 5 mM, stimulates BAMT activity by a factor of 2 Antirrhinum majus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41000
-
 calculated molecular mass of the protein encoded by BAMT cDNA Antirrhinum majus
49000
-
 denatured protein, SDS–PAGE Antirrhinum majus
100000
-
 native protein, gel filtration chromatography on Superdex 200-HR Antirrhinum majus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + benzoate Antirrhinum majus
-
 S-adenosyl-L-homocysteine + methyl benzoate
-
 ?

Organism

Organism UniProt Comment Textmining
Antirrhinum majus
-
 snapdragon
-

Purification (Commentary)

Purification (Comment) Organism
enzyme purified from upper and lower petal lobes of 5- to 10-day-old snapdragon flowers using DE53 anion exchange chromatography, hydrophobic interaction chromatography using Phenyl-Sepharose 6FF, and Mono-Q chromatography Antirrhinum majus

Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine + benzoate = S-adenosyl-L-homocysteine + methyl benzoate ordered bi–bi mechanism, derived from kinetic analysis, S-adenosyl-L-methionine appears to be the first substrate to bind to the enzyme and methyl benzoate would be the first to be released and S-adenosyl-L-homocysteine the last Antirrhinum majus
a

Source Tissue

Source Tissue Comment Organism Textmining
petal enzyme is expressed in the upper and lower lobes of petals of snapdragon flowers Antirrhinum majus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.01962
-
 purified BAMT protein, pH 7.5, 20°C Antirrhinum majus

Storage Stability

Storage Stability Organism
the purified proteins, both from petal tissue and from Escherichia coli, are highly stable for several months when stored at -80°C. When stored in a buffer containing 50 mM Bis–Tris–HCl, pH 6.9, 10% glycerol, and 10 mM beta-mercaptoethanol at 4°C, BAMT protein is stable for 1 week Antirrhinum majus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no activity toward other naturally occurring substrates like salicylic acid, trans-cinnamic acid, and their derivatives 3-hydroxybenzoic acid, 4-hydroxybenzoic acid, benzyl alcohol, and 2-coumaric, 3-coumaric, and 4-coumaric acid Antirrhinum majus ?
-
 ?
S-adenosyl-L-methionine + benzoate
-
 Antirrhinum majus S-adenosyl-L-homocysteine + methyl benzoate
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 49000 Antirrhinum majus

Synonyms

Synonyms Comment Organism
BAMT
-
 Antirrhinum majus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
-
 Antirrhinum majus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
20 65 BAMT is 100% stable for 30 min at 20°C and 60% stable for 30 min at 30°C, it is 20% stable for 30 min at 42°C but after 30 min incubation at 65°C, it completely loses activity Antirrhinum majus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Antirrhinum majus

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
 the enzyme is active in both Tris- and phosphate–citrate-based buffers Antirrhinum majus
5.5 9.5 with 65% of maximum activity at both pH 6.5 and 8.5 and at pH 5.5 and 9.5, the enzyme activity falls to about 50% of the optimal value Antirrhinum majus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.007
-
 S-adenosyl-L-homocysteine for S-adenosyl-L-methionine, pH 7.5, 20°C Antirrhinum majus
0.014
-
 S-adenosyl-L-homocysteine for benzoate, pH 7.5, 20°C Antirrhinum majus