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CATH domain | Related DB codes (homologues) |
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3.40.50.150 : Rossmann fold | S00637,S00639,S00262,S00261,S00291,S00412,D00075,D00076,D00079,D00080,D00082,D00083 |
Enzyme Name | UniProtKB | KEGG |
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| Q56308 |
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Protein name | Protein-L-isoaspartate O-methyltransferase | Protein-L-isoaspartate(D-aspartate) O-methyltransferaseProtein-L-isoaspartate O-methyltransferaseProtein-beta-aspartate O-methyltransferaseD-Aspartyl/L-isoaspartyl methyltransferaseL-Isoaspartyl/D-aspartyl protein carboxyl methyltransferaseProtein (D-aspartate) methyltransferaseProtein D-aspartate methyltransferaseProtein L-isoaspartate methyltransferaseProtein L-isoaspartyl methyltransferaseProtein O-methyltransferase (L-isoaspartate)L-Aspartyl/L-isoaspartyl protein methyltransferase |
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Synonyms | EC 2.1.1.77L-isoaspartyl protein carboxyl methyltransferaseProtein L-isoaspartyl methyltransferaseProtein-beta-aspartate methyltransferasePIMT |
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RefSeq | NP_228513.1 (Protein) NC_000853.1 (DNA/RNA sequence)
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Pfam | PF01135 (PCMT) [Graphical view]
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UniProtKB:Accession Number | Q56308 |
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Entry name | PIMT_THEMA |
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Activity | S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester. |
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Subunit | Monomer. |
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Subcellular location | Cytoplasm (By similarity). |
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Cofactor |
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Compound table: links to PDB-related databases & PoSSuM |
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| Substrates | Products |
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KEGG-id | C00019 | C03306 | C00021 | C04311 |
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Compound | S-adenosyl-L-methionine | protein L-isoaspartate | S-adenosyl-L-homocysteine | protein L-isoaspartate alpha-methyl ester |
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Type | amino acids,amine group,nucleoside,sulfonium ion | carboxyl group,peptide/protein | amino acids,amine group,nucleoside,sulfide group | carbohydrate,peptide/protein |
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ChEBI | 67040
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| 16680 57856
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PubChem | 34755
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| 25246222 439155
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| | | | | | | | | | | |
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1dl5A01 |  |  |  |  |  |  |  | Unbound | Unbound | Bound:SAH | Unbound |
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1dl5B01 |  |  |  |  |  |  |  | Unbound | Unbound | Bound:SAH | Unbound |
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1dl5A02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound |
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1dl5B02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[2] | Fig.5c, p.1196-1198 |
| [7] | p.12850-12852 |
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references | [1] |
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Comments | X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-284 |
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PubMed ID | 9115443 |
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Journal | Structure |
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Year | 1997 |
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Volume | 5 |
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Pages | 545-58 |
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Authors | Djordjevic S, Stock AM |
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Title | Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine. |
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Related PDB | 1af7 |
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Related UniProtKB | P07801 |
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[2] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). |
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PubMed ID | 11080641 |
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Journal | Structure |
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Year | 2000 |
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Volume | 8 |
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Pages | 1189-201 |
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Authors | Skinner MM, Puvathingal JM, Walter RL, Friedman AM |
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Title | Crystal structure of protein isoaspartyl methyltransferase: a catalyst for protein repair. |
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Related PDB | 1dl5 |
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Related UniProtKB | Q56308 |
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[3] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS). |
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PubMed ID | 11700066 |
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Journal | J Mol Biol |
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Year | 2001 |
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Volume | 313 |
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Pages | 1103-16 |
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Authors | Griffith SC, Sawaya MR, Boutz DR, Thapar N, Katz JE, Clarke S, Yeates TO |
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Title | Crystal structure of a protein repair methyltransferase from Pyrococcus furiosus with its L-isoaspartyl peptide substrate. |
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Related PDB | 1jg1,1jg2,1jg3,1jg4 |
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Related UniProtKB | Q8TZR3 |
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[4] |
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PubMed ID | 12504684 |
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Journal | Curr Opin Struct Biol |
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Year | 2002 |
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Volume | 12 |
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Pages | 783-93 |
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Authors | Martin JL, McMillan FM |
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Title | SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold. Curr Opin Struct Biol. 2002 Dec;12(6):783-93. Review. |
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[5] |
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Comments | X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). |
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PubMed ID | 11792715 |
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Journal | J Biol Chem |
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Year | 2002 |
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Volume | 277 |
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Pages | 10642-6 |
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Authors | Ryttersgaard C, Griffith SC, Sawaya MR, MacLaren DC, Clarke S, Yeates TO |
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Title | Crystal structure of human L-isoaspartyl methyltransferase. |
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Related PDB | 1kr5 |
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Related UniProtKB | P22061 |
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[6] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS). |
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PubMed ID | 11847284 |
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Journal | Protein Sci |
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Year | 2002 |
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Volume | 11 |
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Pages | 625-35 |
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Authors | Smith CD, Carson M, Friedman AM, Skinner MM, Delucas L, Chantalat L, Weise L, Shirasawa T, Chattopadhyay D |
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Title | Crystal structure of human L-isoaspartyl-O-methyl-transferase with S-adenosyl homocysteine at 1.6-A resolution and modeling of an isoaspartyl-containing peptide at the active site. |
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Related PDB | 1i1n |
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Related UniProtKB | P22061 |
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[7] |
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Comments | X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-221, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-60. |
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PubMed ID | 14596598 |
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Journal | Biochemistry |
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Year | 2003 |
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Volume | 42 |
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Pages | 12844-53 |
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Authors | Bennett EJ, Bjerregaard J, Knapp JE, Chavous DA, Friedman AM, Royer WE Jr, O'Connor CM |
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Title | Catalytic implications from the Drosophila protein L-isoaspartyl methyltransferase structure and site-directed mutagenesis. |
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Related PDB | 1r18 |
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Related UniProtKB | Q27869 |
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comments | This enzyme catalyzes the repair of proteins, which are age-damaged by isomerized and racemized aspartyl residue leading to the isoaspartyl formation (L-isoAsp), by methylation of the alpha-carboxylate of isoAsp in the damaged peptide. The methyl ester product is unstable and rapidly converted to succinimide, which can form either the normal L-Asp residue or the L-isoAsp residue spontaneously. This enzyme has homologous enzymes with a single domain (see S00639 in EzCatDB). According to the literature [2] and [7], the reaction of this enzyme occurs as follows: (1) Ser59 modulates the nucleophilicity of the alpha-carboxylate of the substrate, by orienting the oxygen atom of the acceptor carboxylate group, and by creating aprotic environment that is favorable for an SN2 reaction. (2) The acceptor carboxylate group makes a nucleophilic attack on the methyl group on AdoMet. This is an SN2 reaction.
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created | updated |
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2009-10-28 | 2010-08-19 |
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