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Literature summary for 2.1.1.165 extracted from

  • Ni, X.; Hager, L.P.
    cDNA cloning of Batis maritima methyl chloride transferase and purification of the enzyme (1998), Proc. Natl. Acad. Sci. USA, 95, 12866-12871.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Batis maritima

Protein Variants

Protein Variants Comment Organism
additional information the disparity between the observed (22500 Da) and calculated molecular mass (25761 Da) suggests that the methylase undergoes posttranslational cleavage, possibly during purification Batis maritima

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
22474
-
x * 22474, the methylase can function in either a monomeric or oligomeric form, mass spectrometry Batis maritima
22500
-
x * 22500, the methylase can function in either a monomeric or oligomeric form, SDS-PAGE Batis maritima
25761
-
x * 25761, the methylase can function in either a monomeric or oligomeric form, calculated from sequence Batis maritima

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + chloride Batis maritima an obvious function for a halophytic methylase would be the maintenance of homeostatic levels of cytoplasmic chloride ion. The secretion of excess chloride into the soil could not greatly benefit a halophytic plant. On the other hand, the synthesis and distillation of a volatile gas, methyl chloride, into the atmosphere could be a useful mechanism for disposing of excess chloride S-adenosyl-L-homocysteine + methyl chloride
-
?

Organism

Organism UniProt Comment Textmining
Batis maritima Q9ZSZ7
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 2700fold to homogeneity by ammonium sulfate fractionation, gel filtration, adenosine affinity chromatography, and a second step of gel filtration Batis maritima

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Batis maritima
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.3
-
purified enzyme, substrate iodide Batis maritima

Storage Stability

Storage Stability Organism
-20°C, enzyme forms an aggregate with molecular mass of approximately 500000 Da Batis maritima

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information purified enzyme is unable to use bisulfide (HS-) as an acceptor Batis maritima ?
-
?
S-adenosyl-L-methionine + chloride
-
Batis maritima S-adenosyl-L-homocysteine + methyl chloride
-
?
S-adenosyl-L-methionine + chloride an obvious function for a halophytic methylase would be the maintenance of homeostatic levels of cytoplasmic chloride ion. The secretion of excess chloride into the soil could not greatly benefit a halophytic plant. On the other hand, the synthesis and distillation of a volatile gas, methyl chloride, into the atmosphere could be a useful mechanism for disposing of excess chloride Batis maritima S-adenosyl-L-homocysteine + methyl chloride
-
?
S-adenosyl-L-methionine + iodide iodide is the preferred substrate Batis maritima S-adenosyl-L-homocysteine + methyl iodide
-
?

Subunits

Subunits Comment Organism
? x * 22474, the methylase can function in either a monomeric or oligomeric form, mass spectrometry Batis maritima
? x * 22500, the methylase can function in either a monomeric or oligomeric form, SDS-PAGE Batis maritima
? x * 25761, the methylase can function in either a monomeric or oligomeric form, calculated from sequence Batis maritima

Synonyms

Synonyms Comment Organism
MCT
-
Batis maritima
methyl chloride transferase
-
Batis maritima

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Batis maritima

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
assay at Batis maritima

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
Batis maritima

pI Value

Organism Comment pI Value Maximum pI Value
Batis maritima calculated from sequence
-
5.1