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2.1.1.77: protein-L-isoaspartate(D-aspartate) O-methyltransferase

This is an abbreviated version!
For detailed information about protein-L-isoaspartate(D-aspartate) O-methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.77

Reaction

S-adenosyl-L-methionine
+
protein L-isoaspartate
=
S-adenosyl-L-homocysteine
 +
protein L-isoaspartate alpha-methyl ester

Synonyms

chaperone protein L-isoaspartate (D-aspartyl) O-methyltransferase, D-aspartyl/L-isoaspartyl methyltransferase, EC 2.1.1.24, HPIMT, IAMT, isoaspartyl peptide methyltransferase, isoaspartyl protein carboxyl-O-methyltransferase, L-aspartyl/L-isoaspartyl protein methyltransferase, L-IAMT, L-isoaspartate O-methyltransferase, L-isoaspartyl (D-aspartyl) methyltransferase, L-isoaspartyl (D-aspartyl) O-methyltransferase, L-isoaspartyl methyltransferase, L-isoaspartyl O-methyltransferase, L-isoaspartyl protein carboxyl methyltransferase, L-isoaspartyl-O-methyltransferase, L-isoaspartyl/D-aspartyl O-methyltransferase, L-isoaspartyl/D-aspartyl protein carboxyl methyltransferase, methyltransferase, protein (D-aspartate), PCM, PCM-1, PCMT, PCMT1, PIMT, PIMT1, PIMT2, PIMT2 TISIalphaomega, PIMT2 TISIalphapsi, PIMT2 TISIbetapsi, PIMT2 TISIIalphaomega, PIMT2 TISIIalphapsi, PIMT2 TISIIbetapsi, PIMT2 TISIIIalphaomega, PIMT2 TISIIIalphapsi, PIMT2 TISIIIbetapsi, PIMT2', protein (L-isoaspartate) O-methyltransferase, protein carboxyl methyltransferase type II, protein D-aspartate methyltransferase, protein isoaspartate methyl transferase, protein isoaspartate methyltransferase, protein isoaspartyl carboxyl O-methyltransferase, protein isoaspartyl methyltransferase, protein isoaspartyl methyltransferase 1, protein L-isoaspartate (D-aspartate) O-methyltransferase, protein L-isoaspartate methyltransferase, protein L-isoaspartate O-methyltransferase, protein L-isoaspartate-O-methyltransferase, protein L-isoaspartyl (D-aspartate) O-methyltransferase, protein L-isoaspartyl (D-aspartyl) methyltransferase, protein L-isoaspartyl (D-aspartyl) O-methyltransferase, protein L-isoaspartyl methyl transferase, protein L-isoaspartyl methyltransferase, protein L-isoaspartyl methyltransferase1, protein L-isoaspartyl methyltransferase2, protein L-isoaspartyl O-methyltransferase, protein L-isoaspartyl-O-methyltransferase, protein L-isoaspartyl/D-aspartyl O-methyltransferase, protein repair L-isoaspartyl methyltransferase, protein repair L-isoaspartyl methyltransferase 1, protein-beta-aspartate O-methyltransferase, protein-L-isoaspartate (D-aspartate) O-methyltransferase, protein-L-isoaspartate methyltransferase, protein-L-isoaspartate O-methyltransferase, protein-L-isoaspartyl methyltransferase, RPA0376, RPA2838, StoPIMT, type II methyltransferase

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.77 protein-L-isoaspartate(D-aspartate) O-methyltransferase

Engineering

Engineering on EC 2.1.1.77 - protein-L-isoaspartate(D-aspartate) O-methyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S60A
inactive mutant protein
S60Q
the ratio of turnover number to KM-value for ovalbumin L-isoaspartate is 24.3fold lower than the wild-type value, the ratio of turnover-number to KM-value for KASA(iso-D)LAKY is 21fold lower than wild-type value
S60T
the ratio of turnover number to KM-value for ovalbumin L-isoaspartate is 6.2fold lower than the wild-type value, the ratio of turnover-number to KM-value for KASA(iso-D)LAKY is 2fold lower than the wild-type value
A150V
-
the mutant shows 64% loss of activity compared to the wild type activity
A65V
-
the mutant shows 11% loss of activity compared to the wild type activity
A7P
-
the mutant shows 34% of wild type catalytic efficiency
D83F
-
negative dominant mutant
F72L
-
the mutant shows 67% of wild type catalytic efficiency
G88A
-
catalytically inactive
I58V
-
the mutant shows 60% of wild type catalytic efficiency
L191S
-
the mutant shows 72% loss of activity compared to the wild type activity
P174H
-
the mutant shows 61% loss of activity compared to the wild type activity
R36A
-
the mutant shows near complete loss of activity (<1%)
R36C
-
the mutant shows near complete loss of activity (<1%)
R36K
-
the mutant shows near complete loss of activity (4.6%)
V119I
the variant enzyme has lower activity and thermal stability but about 30% increased affinity for endogenous substrates compared to the I119I variant
DELTA206-231
-
hexameric structure and thermostability retained
additional information
-
livers of male Wistar rats, fed the Lieber DeCarli control, ethanol or 1% betaine-supplemented diets for 4 weeks, are processed for PIMT-related analyses. A significant increase in the accumulation of modified proteins bearing isoaspartyl residues (substrates for PIMT), in homogenate samples and various subcellular fractions of livers from ethanol-fed rats are observed. Betaine supplementation prevents this accumulation of damaged proteins. Ethanol exposure induces no changes in the PIMT enzyme activity levels as compared to controls. The accumulation of damaged proteins negatively correlates with hepatic S-adenosylmethionine to S-adenosylhomocysteine ratios