EC |
2.3.2.19 |
Accepted name: |
ribostamycin:4-(γ-L-glutamylamino)-(S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] 4-(γ-L-glutamylamino)-(S)-2-hydroxybutanoate transferase |
Reaction: |
4-(γ-L-glutamylamino)-(S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] + ribostamycin = γ-L-glutamyl-butirosin B + BtrI acyl-carrier protein |
Other name(s): |
btrH (gene name) |
Systematic name: |
ribostamycin:4-(γ-L-glutamylamino)-(S)-2-hydroxybutanoyl-[BtrI acyl-carrier protein] 4-(γ-L-glutamylamino)-(S)-2-hydroxybutanoate transferase |
Comments: |
The enzyme attaches the side chain of the aminoglycoside antibiotics of the butirosin family. The side chain confers resistance against several aminoglycoside-modifying enzymes. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Llewellyn, N.M., Li, Y. and Spencer, J.B. Biosynthesis of butirosin: transfer and deprotection of the unique amino acid side chain. Chem. Biol. 14 (2007) 379–386. [DOI] [PMID: 17462573] |
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[EC 2.3.2.19 created 2012] |
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EC |
4.3.2.6 |
Accepted name: |
γ-L-glutamyl-butirosin B γ-glutamyl cyclotransferase |
Reaction: |
γ-L-glutamyl-butirosin B = butirosin B + 5-oxo-L-proline |
Glossary: |
γ-L-glutamyl-butirosin B = (1R,2R,3S,4R,6S)-6-amino-4-{[(2R)-4-(γ-L-glutamylamino)-2-hydroxybutanoyl]amino}-3-hydroxy-2-(α-D-ribofuranosyloxy)cyclohexyl |
Other name(s): |
btrG (gene name); γ-L-glutamyl-butirosin B γ-glutamyl cyclotransferase (5-oxoproline producing) |
Systematic name: |
γ-L-glutamyl-butirosin B γ-glutamyl cyclotransferase (5-oxo-L-proline producing) |
Comments: |
The enzyme catalyses the last step in the biosynthesis of the aminoglycoside antibiotic butirosin B. The enzyme acts as a cyclotransferase, cleaving the amide bond via transamidation using the α-amine of the terminal γ-L-glutamate of the side chain, releasing it as the cyclic 5-oxo-L-proline. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Llewellyn, N.M., Li, Y. and Spencer, J.B. Biosynthesis of butirosin: transfer and deprotection of the unique amino acid side chain. Chem. Biol. 14 (2007) 379–386. [DOI] [PMID: 17462573] |
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[EC 4.3.2.6 created 2012] |
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