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Title		Authors	PubMed ID
1	Enzymatic Synthesis of a Fluorogenic Reporter Substrate and the Development of a High-Throughput Assay for Fucosyltransferase VIII Provide a Toolkit to Probe and Inhibit Core Fucosylation.	Soroko M, Kwan DH	32441090 CHEMBIOCHEM
2	Identification of active site residues of chorismate mutase-prephenate dehydrogenase from Escherichia coli.	Christendat D, Turnbull J	8605196 CHEMBIOCHEM
3	Characterization of active and inactive forms of the phenol hydroxylase stimulatory protein DmpM.	Cadieux E, Powlowski J	10451366 CHEMBIOCHEM
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5	Mechanism of S-nitrosation of recombinant human brain calbindin D28K.	Tao L, English AM	12641465 CHEMBIOCHEM
6	Protein S-glutathiolation triggered by decomposed S-nitrosoglutathione.	Tao L, English AM	15049710 CHEMBIOCHEM
7	Mass spectrometric analysis of nitroxyl-mediated protein modification: comparison of products formed with free and protein-based cysteines.	Shen B, English AM	16229492 CHEMBIOCHEM
8	A shared binding site for NAD+ and coenzyme A in an acetaldehyde dehydrogenase involved in bacterial degradation of aromatic compounds.	Lei Y, Pawelek PD, Powlowski J	18537268 CHEMBIOCHEM
9	Backbone Flexibility Influences Nucleotide Incorporation by Human Translesion DNA Polymerase η opposite Intrastrand Cross-Linked DNA.	O'Flaherty DK, Guengerich FP, Egli M, Wilds CJ	26624500 CHEMBIOCHEM
10	Proton release due to manganese binding and oxidation in modified bacterial reaction centers.	Kálmán L, Thielges MC, Williams JC, Allen JP	16201752 PHYSICS
11	Light-induced conformational changes in photosynthetic reaction centers: dielectric relaxation in the vicinity of the dimer.	Deshmukh SS, Williams JC, Allen JP, Kálmán L	21141811 PHYSICS
12	Light-induced conformational changes in photosynthetic reaction centers: redox-regulated proton pathway near the dimer.	Deshmukh SS, Williams JC, Allen JP, Kálmán L	21410139 PHYSICS
13	Light-induced conformational changes in photosynthetic reaction centers: impact of detergents and lipids on the electronic structure of the primary electron donor.	Deshmukh SS, Akhavein H, Williams JC, Allen JP, Kalman L	21561160 PHYSICS

Title:	Identification of active site residues of chorismate mutase-prephenate dehydrogenase from Escherichia coli.
Authors:	Christendat D, Turnbull J
Link:	www.ncbi.nlm.nih.gov/pubmed/8605196?dopt=Abstract
DOI:	10.1021/bi9525637
Publication:	Biochemistry
Keywords:
PMID:	8605196	Category:	Biochemistry	Date Added:	2019-06-20
Dept Affiliation:	CHEMBIOCHEM 1 Department of Chemistry and Biochemistry, Concordia University, Montreal, Quebec, Canada.

Description:

Identification of active site residues of chorismate mutase-prephenate dehydrogenase from Escherichia coli.

Biochemistry. 1996 Apr 09;35(14):4468-79

Authors: Christendat D, Turnbull J

Abstract

Chemical modification studies of the bifunctional enzyme chorismate mutase-prephenate dehydrogenase and mass spectral analysis of peptide fragments containing modified residues are presented. The reaction with diethyl pyrocarbonate (DEPC) results in the modification of several enzymic groups, including a single histidine group essential for dehydrogenase activity and a single lysine residue essential for mutase activity. This conclusion is based on the following evidence. (1) Hydroxylamine rapidly restores dehydrogenase activity to the DEPC-inactivated enzyme without restoring mutase activity. (2) Mutase activity is also lost upon treatment of the enzyme with trinitrobenzene sulfonate. (3) The reactivity of the dehydrogenase to DEPC increases with pH, suggesting the participation of a group with a pKa of 7.0 in the dehydrogenase reaction. (4) Two peptides identified by differential peptide mapping had mass values matching those calculated for peptides comprising residues 127-135 (containing His131) and residues 36-48 (containing Lys37). In support of the idea that the residues being modified are within the active sites, we show that the substrates prephenate and nicotinamide adenine dinucleotide (NAD+) offer protection against inactivation of dehydrogenase activity while inactivation of mutase activity can be prevented by prephenate and a transition state analogue (3-endo-8-exo)-8-hydroxy-2-oxabicyclo[3.3.1]-non-6-ene-3,5-dicarboxylic acid (endo-oxabicyclic diacid). Lys37 is conserved among several chorismate mutases and may participate in catalysis by interacting with an ether oxygen between C-5 and C-8 of chorismate in the transition state. His131 may be assisting in a hydride transfer from prephenate to NAD+ in the dehydrogenase reaction.

PMID: 8605196 [PubMed - indexed for MEDLINE]

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