Literature summary for 1.14.20.1 extracted from

Lipscomb, S.J.; Lee, H.J.; Mukherji, M.; Baldwin, J.E.; Schofield, C.J.; Lloyd, M.D.
The role of arginine residues in substrate binding and catalysis by deacetoxycephalosporin C synthase (2002), Eur. J. Biochem., 269, 2735-2739.

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Protein Variants

Protein Variants	Comment	Organism
R160Q	more than 95% loss of activity	Streptomyces clavuligerus
R266L	2-oxoglutarate conversion is very low and the same whether penicillin N, penicillin G or no penicillin substrate is present	Streptomyces clavuligerus
R266Q	2-oxoglutarate conversion is very low and the same whether penicillin N, penicillin G or no penicillin substrate is present	Streptomyces clavuligerus
R306L	mutation enhances penicillin N conversion compared to the level of wild-type enzyme, turnover number for penicillin N is increased, no enhancement in activity with penicillin G as substrate, little effect on kinetic values using penicillin G as substrate	Streptomyces clavuligerus
R307Q	mutation enhances penicillin N conversion compared to the level of wild-type enzyme, turnover number for penicillin N is increased, no enhancement in activity with penicillin G as substrate. Mutation increase the Km-value by 10fold, but has little effect on the turnover number for penicillin G	Streptomyces clavuligerus
R74I	turnover number and Km-values are similar to that for wild-type enzyme. 2-Oxoglutarate conversion is significantly stimulated in presence of penicillin N and penicillin G compared to wild type enzyme. Penicillin oxidation is reduced relative to the wild type enzyme	Streptomyces clavuligerus
R74Q	turnover number and Km-values are similar to that for wild-type enzyme. 2-Oxoglutarate conversion is significantly stimulated in presence of penicillin N and penicillin G compared to wild type enzyme. Penicillin oxidation is reduced relative to the wild type enzyme	Streptomyces clavuligerus
R74Q/R266I	2-oxoglutarate conversion is not stimulated by penicillin substrates	Streptomyces clavuligerus
R74Q/R266Q	2-oxoglutarate conversion is not stimulated by penicillin substrates	Streptomyces clavuligerus
R75I/D270G	2-oxoglutarate conversion is not stimulated by penicillin substrates	Streptomyces clavuligerus
R75Q	turnover number and Km-values are similar to that for wild-type enzyme. 2-Oxoglutarate conversion is significantly stimulated in presence of penicillin N compared to wild type enzyme	Streptomyces clavuligerus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Km-values for mutant enzymes with penicillin N and penicillin G as substrate	Streptomyces clavuligerus
0.033	-	Penicillin N	wild-type enzyme	Streptomyces clavuligerus
0.7	-	penicillin G	wild-type enzyme	Streptomyces clavuligerus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
penicillin N + 2-oxoglutarate + O2	Streptomyces clavuligerus	committed step in biosynthesis of cephamycin C	deacetoxycephalosporin C + succinate + CO2 + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Streptomyces clavuligerus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
wild-type and mutant enzymes R74I, R74Q, R75I/D270G, R75Q, R306L and R307Q	Streptomyces clavuligerus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
penicillin G + 2-oxoglutarate + O2	-	Streptomyces clavuligerus	phenylacetyl-7-aminodeacetoxy cephalosporanic acid + succinate + CO2 + H2O	-	?
penicillin N + 2-oxoglutarate + O2	-	Streptomyces clavuligerus	deacetoxycephalosporin C + succinate + CO2 + H2O	-	?
penicillin N + 2-oxoglutarate + O2	committed step in biosynthesis of cephamycin C	Streptomyces clavuligerus	deacetoxycephalosporin C + succinate + CO2 + H2O	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.02	-	Penicillin N	wild-type enzyme	Streptomyces clavuligerus
0.05	-	penicillin G	wild-type enzyme	Streptomyces clavuligerus

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Release 2023.1 (January 2023)