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Homo sapiens Reaction: 2.1.1.77

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.1.1.77

Enzymes and Genes:
protein-L-isoaspartate(D-aspartate) O-methyltransferase : PCMT1

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

Mass balance status: Balanced.

Enzyme Commission Primary Name: protein-L-isoaspartate(D-aspartate) O-methyltransferase

Enzyme Commission Synonyms: protein-L-isoaspartate O-methyltransferase, protein-β-aspartate O-methyltransferase, D-aspartyl/L-isoaspartyl methyltransferase, L-isoaspartyl/D-aspartyl protein carboxyl methyltransferase, protein (D-aspartate) methyltransferase, protein D-aspartate methyltransferase, protein L-isoaspartate methyltransferase, protein L-isoaspartyl methyltransferase, protein O-methyltransferase (L-isoaspartate), L-aspartyl/L-isoaspartyl protein methyltransferase

Enzyme Commission Summary:
D-Aspartate (but not L-aspartate) residues in proteins can also act as acceptors. Previously also listed as EC 2.1.1.24.

Citations: [Clarke85, Kim70, Ota87]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:2.1.1.77 , ENZYME:EC:2.1.1.77 , IUBMB-ExplorEnz:EC:2.1.1.77


References

Clarke85: Clarke S (1985). "Protein carboxyl methyltransferases: two distinct classes of enzymes." Annu Rev Biochem 54;479-506. PMID: 3896126

Kim70: Kim S, Paik WK (1970). "Purification and properties of protein methylaase II." J Biol Chem 245(7);1806-13. PMID: 5438363

Ota87: Ota IM, Ding L, Clarke S (1987). "Methylation at specific altered aspartyl and asparaginyl residues in glucagon by the erythrocyte protein carboxyl methyltransferase." J Biol Chem 262(18);8522-31. PMID: 3597386


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Please cite the following article in publications resulting from the use of HumanCyc: Genome Biology 6(1):1-17 2004
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