Literature summary for 3.1.1.89 extracted from

Xing, Y.; Li, Z.; Chen, Y.; Stock, J.; Jeffrey, P.; Shi, Y.
Structural mechanism of demethylation and inactivation of protein phosphatase 2A (2008), Cell, 133, 154-163.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of methylesterase PME-1 by itself and in complex with a protein phosphatase PP2A heterodimeric core enzyme, to 2.0 and 2.7 A resolution. PME-1 directly binds to the active site of protein phosphatase PP2A and this interaction results in the activation of PME-1 by rearranging the catalytic triad into an active conformation. These interactions also lead to inactivation of protein phosphatase PP2A by evicting the manganese ions that are required for the phosphatase activity of PP2A. PME-1 fdisplays a dual role that regulates protein phosphatase PP2A activation, methylation, and holoenzyme assembly in cells	Homo sapiens

Crystallization (Comment)

Organism

crystal structures of methylesterase PME-1 by itself and in complex with a protein phosphatase PP2A heterodimeric core enzyme, to 2.0 and 2.7 A resolution. PME-1 directly binds to the active site of protein phosphatase PP2A and this interaction results in the activation of PME-1 by rearranging the catalytic triad into an active conformation. These interactions also lead to inactivation of protein phosphatase PP2A by evicting the manganese ions that are required for the phosphatase activity of PP2A. PME-1 fdisplays a dual role that regulates protein phosphatase PP2A activation, methylation, and holoenzyme assembly in cells

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9Y570	-	-

Synonyms

Synonyms	Comment	Organism
PME1	-	Homo sapiens
PPME1	-	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)