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IUBMB Comments The enzyme, characterized from the bacterium Nocardia uniformis, is involved in the biosynthesis of the beta-lactam antibiotic nocardicin A. The enzyme can act on nocardicin E, F, and G, producing isonocardicin A, B, and C, respectively. However, the in vivo substrate is believed to be nocardicin G .
The expected taxonomic range for this enzyme is: Nocardia uniformis
Synonyms
aminocarboxypropyltransferase, nocardicin, nocardicin aminocarboxypropyltransferase,
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aminocarboxypropyltransferase, nocardicin
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nocardicin aminocarboxypropyltransferase
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S-adenosyl-L-methionine + nocardicin G = S-methyl-5'-thioadenosine + isonocardicin C
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3-amino-3-carboxypropyl group transfer
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S-adenosyl-L-methionine:nocardicin-G 3-amino-3-carboxypropyltransferase
The enzyme, characterized from the bacterium Nocardia uniformis, is involved in the biosynthesis of the beta-lactam antibiotic nocardicin A. The enzyme can act on nocardicin E, F, and G, producing isonocardicin A, B, and C, respectively. However, the in vivo substrate is believed to be nocardicin G [3].
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S-adenosyl-L-methionine + nocardicin E
5'-methylthioadenosine + isonocardicin A
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S-adenosyl-L-methionine + nocardicin E
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enzyme is involved in the biosynthesis of the beta-lactam antibiotic nocardicin A
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S-adenosyl-L-methionine + nocardicin E
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enzyme is involved in the biosynthesis of the beta-lactam antibiotic nocardicin A
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ssp. tsuyamanensis, ATCC 21806
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brenda
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partially purified enzyme is stable after dialysis against 50 mM phosphate buffer, pH 7.5, containing 20% glycerol and 10 mM 2-mercaptoethanol
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ssp. tsuyamanensis, ATCC 21806, partial
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Wilson, B.A.; Bantia, S.; Salituro, G.M.; Reeve, A.M.; Townsend, C.A.
Cell-free biosynthesis of nocardicin A from nocardicin E and S-adenosylmethionine
J. Am. Chem. Soc.
110
8238-8239
1988
Nocardia uniformis
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brenda
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2.5.1.38 isonocardicin synthase
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