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Literature summary for 3.6.5.5 extracted from

  • Takahashi, K.; Otomo, M.; Yamaguchi, N.; Nakashima, H.; Miyoshi, H.
    Replacement of Arg-386 with Gly in dynamin 1 middle domain reduced GTPase activity and oligomer stability in the absence of lipids (2012), Biosci. Biotechnol. Biochem., 76, 2195-2200.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His6-tagged or FLAG-tagged wild-type and mutant enzymes in HeLa cells Mus musculus

Protein Variants

Protein Variants Comment Organism
R386G site-directed mutagenesis, replacement of Arg386 with Gly in dynamin 1 middle domain reduces GTPase activity and oligomer stability in the absence of lipids, while in presence of phosphatidylserine liposomes, the intermolecular interactions of dynamin 1 are not affected. The mutant is a monomer with reduced GTPase activity compared to the wild-type enzyme Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + H2O Mus musculus
-
GDP + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus P39053 gene Dyn1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
Mus musculus GDP + phosphate
-
?

Subunits

Subunits Comment Organism
More the enzyme's middle domain is involved in the formation of functional oligomers. Wild-type enzyme forms oligomers, while enzyme mutant R386G prefers to form monomers Mus musculus

Synonyms

Synonyms Comment Organism
Dyn1
-
Mus musculus
dynamin 1
-
Mus musculus

General Information

General Information Comment Organism
malfunction R386G mutation in dynamin 1 middle domain reduces GTPase activity and oligomer stability in the absence of lipids. Vesicle formed in endocytosis are smaller in enzyme mutant R386G cells compared to wild-type Mus musculus
physiological function dynamin plays an important role in membrane fission during endocytosis. The dynammin GTPase is important for dynamin oligomer complex dissociation in absence of lipids Mus musculus