1hjf | pdb_00001hjf
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ALTERATION OF THE CO-SUBSTRATE SELECTIVITY OF DEACETOXYCEPHALOSPORIN C SYNTHASE: THE ROLE OF ARGININE-258
Overview
Deacetoxycephalosporin C synthase is an iron(II) 2-oxoglutaratedependent, oxygenase that catalyzes the oxidative ring-expansion of penicillin N to, deacetoxycephalosporin C. The wild-type enzyme is only able to efficiently, utilize 2-oxoglutarate and 2-oxoadipate as a 2-oxoacid co-substrate., Mutation of arginine 258, the side chain of which forms an electrostatic, interaction with the 5-carboxylate of the 2-oxoglutarate co-substrate, to, a glutamine residue reduced activity to about 5% of the wild-type enzyme, with 2-oxoglutarate. However, other aliphatic 2-oxoacids, which were not, co-substrates for the wild-type enzyme, were utilized by the R258Q mutant., These 2-oxoacids "rescued" catalytic activity to the level observed for, the wild-type enzyme as judged by penicillin N and G ... [(full description)]
About this Structure
1HJF is a [Single protein] structure of sequence from [Streptomyces clavuligerus] with FE2 and COI as [ligands]. Structure known Active Sites: COI and FE. Full crystallographic information is available from [OCA].
Reference
Alteration of the co-substrate selectivity of deacetoxycephalosporin C synthase. The role of arginine 258., Lee HJ, Lloyd MD, Clifton IJ, Harlos K, Dubus A, Baldwin JE, Frere JM, Schofield CJ, J Biol Chem. 2001 May 25;276(21):18290-5. Epub 2001 Feb 21. PMID:11279000
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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Single protein
- Streptomyces clavuligerus
- Baldwin, J.E.
- Clifton, I.J.
- Dubus, A.
- Frere, J.M.
- Harlos, K.
- Lee, H.J.
- Lloyd, M.D.
- Schofield, C.J.
- COI
- FE2
- 2-oxoglutarate-dependent oxygenase
- Alternative 2-oxoacids
- Cephem antibiotic biosynthesis
- Chemical cosubstrate rescue
- Co-substrate selectivity
