Literature summary for 5.4.99.5 extracted from

Zhang, S.; Kongaeree, P.; Clardy, J.; Wilson, D.B.; Ganem, B.
Site-directed mutagenesis of monofunctional chorismate mutase engineered from the E. coli P-protein (1996), Bioorg. Med. Chem., 4, 1015-1020.

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Protein Variants

Protein Variants	Comment	Organism
K39N	the mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu show similar structures to the wild-type enzyme, as indicated by circular dichroism spectra, with Lys39Gln showing small deviation. The turnover numbers for the mutant enzymes Lys39Arg, Lys39Asn and Lys39Gln are 335fold, 820fold and 4090fold lower than the turnover number of the wild-type enzyme, no significant differences in Km-value for chorismate between Lys39Arg, Lys39Asn, and the wild-type enzyme	Escherichia coli
K39Q	the mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu show similar structures to the wild-type enzyme, as indicated by circular dichroism spectra, with Lys39Gln showing small deviation. The turnover numbers for the mutant enzymes Lys39Arg, Lys39Asn and Lys39Gln are 335fold, 820fold and 4090fold lower than the turnover number of the wild-type enzyme, no significant differences in Km-value for chorismate between Lys39Arg, Lys39Asn, and the wild-type enzyme	Escherichia coli
K39R	the mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu show similar structures to the wild-type enzyme, as indicated by circular dichroism spectra, with Lys39Gln showing small deviation. The turnover numbers for the mutant enzymes Lys39Arg, Lys39Asn and Lys39Gln are 335fold, 820fold and 4090fold lower than the turnover number of the wild-type enzyme, no significant differences in Km-value for chorismate between Lys39Arg, Lys39Asn, and the wild-type enzyme	Escherichia coli
Q88E	the mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu show similar structures to the wild-type enzyme, as indicated by circular dichroism spectra, with Lys39Gln showing small deviation. The turnover numbers for the mutant enzymes Lys39Arg, Lys39Asn and Lys39Gln are 335fold, 820fold and 4090fold lower than the turnover number of the wild-type enzyme, no significant differences in Km-value for chorismate between Lys39Arg, Lys39Asn, and the wild-type enzyme	Escherichia coli
Q88E	mutation of Gln88 to Glu in the monofunctional chorismate mutase results in an enzyme with a pH profile of activity significantly different from that of the wild-type protein	Escherichia coli
Q88R	the mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu show similar structures to the wild-type enzyme, as indicated by circular dichroism spectra, with Lys39Gln showing small deviation. The turnover numbers for the mutant enzymes Lys39Arg, Lys39Asn and Lys39Gln are 335fold, 820fold and 4090fold lower than the turnover number of the wild-type enzyme, no significant differences in Km-value for chorismate between Lys39Arg, Lys39Asn, and the wild-type enzyme	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.3	-	chorismate	wild-type enzyme	Escherichia coli
0.45	-	chorismate	mutant enzyme Lys39Asn	Escherichia coli
0.59	-	chorismate	mutant enzyme Lys39Arg	Escherichia coli
1.16	-	chorismate	mutant enzyme Lys39Gln	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	mutant enzymes Lys39Arg, Lys39Asn, Lys39Gln, Gln88Arg, and Gln88Glu	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Chorismate	-	Escherichia coli	Prephenate	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.00983	-	chorismate	mutant enzyme Lys39Arg	Escherichia coli
0.0492	-	chorismate	mutant enzyme Lys39Asn	Escherichia coli
0.123	-	chorismate	mutant enzyme Lys39Arg	Escherichia coli
41.4	-	chorismate	wild-type enzyme	Escherichia coli

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Release 2023.1 (January 2023)