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Literature summary for 2.3.1.142 extracted from

  • Singh, P.; Ponnan, P.; Priya, N.; Tyagi, T.K.; Gaspari, M.; Krishnan, S.; Cuda, G.; Joshi, P.; Gambhir, J.K.; Sharma, S.K.; Prasad, A.K.; Saso, L.; Rastogi, R.C.; Parmar, V.S.; Raj, H.G.
    Protein acyltransferase function of purified calreticulin: the exclusive role of P-domain in mediating protein acylation utilizing acyloxycoumarins and acetyl CoA as the acyl group donors (2011), Protein Pept. Lett., 18, 507-517.
    View publication on PubMed
Search for more literature for 2.3.1.142

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
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 Haemonchus contortus 5783
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Haemonchus contortus protein acyltransferase function of purified calreticulin. The rhCRTAase/P-domain also undergoes autoacylation by acyloxycoumarins. The isolated autoacylated rhCRTAase/P-domain in non-denatured form alone exhibits the ability to transfer acyl group to rGST indicating the stable intermediate nature of the acylated enzyme ?
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 ?

Organism

Organism UniProt Comment Textmining
Haemonchus contortus
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione-S-transferase + 7,8-diacetoxy-4-methylcoumarin
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 Haemonchus contortus ?
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 ?
glutathione-S-transferase + acetyl-CoA recombinant Schistosoma japonicum glutathione S-transferase Haemonchus contortus ?
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 ?
additional information protein acyltransferase function of purified calreticulin. The rhCRTAase/P-domain also undergoes autoacylation by acyloxycoumarins. The isolated autoacylated rhCRTAase/P-domain in non-denatured form alone exhibits the ability to transfer acyl group to rGST indicating the stable intermediate nature of the acylated enzyme Haemonchus contortus ?
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 ?
additional information P-domain catalyzed acetylation of rGST by 7,8-diacetoxy-4-methylcoumarin or acetyl-CoA results in the modification of several lysine residues, LC-MS/MS analysis. Residues Lys173 and Lys174 are present in the P-domain, and are responsible for binding of acyloxycoumarins and acetyl-CoA, they are probably part of the active site Haemonchus contortus ?
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 ?

Synonyms

Synonyms Comment Organism
CRTAase
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 Haemonchus contortus

General Information

General Information Comment Organism
additional information the P-domain of recombinant calreticulin, unlike its N- and C-domains, is endowed with CRTAase function Haemonchus contortus