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Literature summary extracted from

  • Takata, Y.; Huang, Y.; Komoto, J.; Yamada, T.; Konishi, K.; Ogawa, H.; Gomi, T.; Fujioka, M.; Takusagawa, F.
    Catalytic mechanism of glycine N-methyltransferase (2003), Biochemistry, 42, 8394-8402.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.20 hanging drop method of vapor diffusion, crystal structure of the enzyme complexed with S-adenosyl-L-methionine and acetate (a potent competitive inhibitor of Gly) and the R175K mutated enzyme complexed with S-adenosyl-L-methionine are determined at 2.8 A and 3.0 A resolution, respectively Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.20 Y194F the ratio of turnover-number to KM-value for S-adenosyl-L-methionine is 2.4fold lower than the wild-type value, the ratio of turnover-number to KM-value for Gly is 16.4fold lower than the wild-type value Rattus norvegicus
2.1.1.20 Y21F the ratio of turnover-number to KM-value for S-adenosyl-L-methionine is 5fold lower than the wild-type value, the ratio of turnover-number to KM-value for Gly is 2.4fold lower than the wild-type value Rattus norvegicus
2.1.1.20 Y220F the ratio of turnover-number to KM-value for S-adenosyl-L-methionine is nearly identical to the wild-type value, the ratio of turnover-number to KM-value for Gly is 179fold lower than the wild-type value Rattus norvegicus
2.1.1.20 Y242F the ratio of turnover-number to KM-value for S-adenosyl-L-methionine is 1.14fold higher than the wild-type value, the ratio of turnover-number to KM-value for Gly is 2325fold lower than the wild-type value Rattus norvegicus
2.1.1.20 Y33F the ratio of turnover-number to KM-value for S-adenosyl-L-methionine is nearly identical to the wild-type value, the ratio of turnover-number to KM-value for Gly is 123fold lower than the wild-type value Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.20 S-adenosyl-L-homocysteine weak Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.20 0.014
-
 S-adenosyl-L-methionine pH 7.2, mutant enzyme Y220F Rattus norvegicus
2.1.1.20 0.017
-
 S-adenosyl-L-methionine pH 7.2, mutant enzyme Y33F Rattus norvegicus
2.1.1.20 0.032
-
 S-adenosyl-L-methionine pH 7.2, mutant enzyme Y242F Rattus norvegicus
2.1.1.20 0.035
-
 S-adenosyl-L-methionine pH 7.2, mutant enzyme Y194F Rattus norvegicus
2.1.1.20 0.036
-
 S-adenosyl-L-methionine pH 7.2, wild-type enzyme Rattus norvegicus
2.1.1.20 0.042
-
 S-adenosyl-L-methionine pH 7.2, mutant enzyme Y21F Rattus norvegicus
2.1.1.20 0.24
-
 Gly pH 7.2, mutant enzyme Y21F Rattus norvegicus
2.1.1.20 0.43
-
 Gly pH 7.2, wild-type enzyme Rattus norvegicus
2.1.1.20 0.44
-
 Gly pH 7.2, mutant enzyme Y242F Rattus norvegicus
2.1.1.20 2.8
-
 Gly pH 7.2, mutant enzyme Y194F Rattus norvegicus
2.1.1.20 25
-
 Gly pH 7.2, mutant enzyme Y33F Rattus norvegicus
2.1.1.20 30
-
 Gly pH 7.2, mutant enzyme Y220F Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.20 Rattus norvegicus P13255
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.20 S-adenosyl-L-methionine + glycine mechanism: the bound S-adenosyl-L-methionine is firmly connected to protein and a „Gly pocket" is created near the bound S-adenosyl-L-methionine. The second substrate Gly binds to Arg175 and is brought into the Gly pocket. Five hydrogen bonds connect the Gly in the proximity of the bound S-adenosyl-L-methionine and orient the lone pair orbital on the amino nitrogen of Gly towards the donor methyl group of S-adenosyl-L-methionine. Thermal motion of the enzyme leads to a collision of the N and C(E) so that a SN2 methyltransfer reaction occurs Rattus norvegicus S-adenosyl-L-homocysteine + sarcosine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.20 GNMT
-
 Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.1.20 0.105
-
 S-adenosyl-L-methionine pH 7.2, mutant enzyme Y21F Rattus norvegicus
2.1.1.20 0.105
-
 Gly pH 7.2, mutant enzyme Y21F Rattus norvegicus
2.1.1.20 0.18
-
 S-adenosyl-L-methionine pH 7.2, mutant enzyme Y194F Rattus norvegicus
2.1.1.20 0.18
-
 Gly pH 7.2, mutant enzyme Y194F Rattus norvegicus
2.1.1.20 0.18
-
 S-adenosyl-L-methionine pH 7.2, mutant enzyme Y220F Rattus norvegicus
2.1.1.20 0.18
-
 Gly pH 7.2, mutant enzyme Y220F Rattus norvegicus
2.1.1.20 0.21
-
 S-adenosyl-L-methionine pH 7.2, mutant enzyme Y33F Rattus norvegicus
2.1.1.20 0.21
-
 Gly pH 7.2, mutant enzyme Y33F Rattus norvegicus
2.1.1.20 0.45
-
 S-adenosyl-L-methionine pH 7.2, wild-type enzyme Rattus norvegicus
2.1.1.20 0.45
-
 Gly pH 7.2, wild-type enzyme Rattus norvegicus
2.1.1.20 0.47
-
 S-adenosyl-L-methionine pH 7.2, mutant enzyme Y242F Rattus norvegicus
2.1.1.20 0.47
-
 Gly pH 7.2, mutant enzyme Y242F Rattus norvegicus