Literature summary for 6.2.1.46 extracted from

  • Strieter, E.R.; Vaillancourt, F.H.; Walsh, C.T.
    CmaE: a transferase shuttling aminoacyl groups between carrier protein domains in the coronamic acid biosynthetic pathway (2007), Biochemistry, 46, 7549-7557.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Pseudomonas syringae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] Pseudomonas syringae during the biosynthesis of the cyclopropyl amino acid coronamic acid from L-allo-Ile by the phytotoxic Pseudomonas syringae, the aminoacyl group covalently attached to the pantetheinyl arm of CmaA is shuttled to the HS-pantetheinyl arm of the protein CmaD by the aminoacyltransferase CmaE, reversible shuttling process AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein]
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r

Organism

Organism UniProt Comment Textmining
Pseudomonas syringae
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information aminoacylated-S-CmaE will transfer the L-Val moiety to the HS-pantetheinyl arm of other T domains, including CytC2, BarA, and ArfA C2-A2-T2 but not to free HS-pantetheine. CmaD can be loaded with other amino acids, for example, L-Leu and L-Thr, by the action of heterologous donor T domains containing alternative aminoacyl groups. Additionally, CmaE is able to accept L-Phe as a substrate when presented on CmaD and is able to load this aminoacyl moiety onto heterologous T domains Pseudomonas syringae ?
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ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] during the biosynthesis of the cyclopropyl amino acid coronamic acid from L-allo-Ile by the phytotoxic Pseudomonas syringae, the aminoacyl group covalently attached to the pantetheinyl arm of CmaA is shuttled to the HS-pantetheinyl arm of the protein CmaD by the aminoacyltransferase CmaE, reversible shuttling process Pseudomonas syringae AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein]
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r
ATP + L-allo-isoleucine + holo-[CmaA peptidyl-carrier protein] CmaE will only recognize deacylated CmaA for initial complexation. The aminoacyl group becomes covalently attached to the active site Cys of CmaE and can then be transferred out to the holo pantetheinylated form of CmaD, reversible shuttling process Pseudomonas syringae AMP + diphosphate + L-allo-isoleucyl-S-[CmaA peptidyl-carrier protein]
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r

Synonyms

Synonyms Comment Organism
CmaE
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Pseudomonas syringae

Cofactor

Cofactor Comment Organism Structure
ATP
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Pseudomonas syringae

General Information

General Information Comment Organism
physiological function the transferase shuttles aminoacyl groups between carrier protein domains in the coronamic acid biosynthetic pathway, overview Pseudomonas syringae