The enzyme, isolated from the bacterium Streptomyces sp. NCIMB40513, catalyses the N-aminoacyl transfer of L-isoleucine from a charged isoleucine tRNA onto the primary sulfonamide group of the monoterpene alkaloid altemicidin.
The enzyme appears in viruses and cellular organisms
The enzyme, isolated from the bacterium Streptomyces sp. NCIMB40513, catalyses the N-aminoacyl transfer of L-isoleucine from a charged isoleucine tRNA onto the primary sulfonamide group of the monoterpene alkaloid altemicidin.
Substrates: altemicidin, i.e. (4aR,6S,7R,7aS)-4-carbamoyl-6-hydroxy-2-methyl-7-[(2-sulamoylacetyl)amino]-4a,5,6,7a-tetrahydro-1H-cyclopenta[c]pyridine-7-carboxylate. SB-203207, i.e. (sulfonamide-N)(L-isoleucyl)altemidicin Products: -
the enzyme catalyses the N-aminoacyl transfer of L-isoleucine from a charged isoleucine tRNA onto the primary sulfonamide group of the monoterpene alkaloid altemicidin
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