Literature summary for 2.1.1.77 extracted from

Dutta, T.; Banerjee, S.; Soren, D.; Lahiri, S.; Sengupta, S.; Rasquinha, J.A.; Ghosh, A.K.
Regulation of enzymatic activity by deamidation and their subsequent repair by protein L-isoaspartyl methyl transferase (2012), Appl. Biochem. Biotechnol., 168, 2358-2375.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-adenosyl-L-methionine + acid trehalase D-aspartate	Homo sapiens	-	S-adenosyl-L-homocysteine + acid trehalase D-aspartate methyl ester	-	?
S-adenosyl-L-methionine + protein L-isoaspartate	Homo sapiens	-	S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + acid trehalase D-aspartate	-	Homo sapiens	S-adenosyl-L-homocysteine + acid trehalase D-aspartate methyl ester	-	?
S-adenosyl-L-methionine + protein L-isoaspartate	-	Homo sapiens	S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester	-	?

Synonyms

Synonyms	Comment	Organism
PIMT	-	Homo sapiens
protein L-isoaspartyl methyl transferase	-	Homo sapiens

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Release 2023.1 (January 2023)