NDLI: Anaerobiospirillum succiniciproducens Phosphoenolpyruvate Carboxykinase: Mutagenesis at Metal Site 2

Content Provider	Springer Nature Link
Author	Jabalquinto, Ana María Laivenieks, Maris González Nilo, Fernando D. Encinas, María Victoria Zeikus, Gregory Cardemil, Emilio
Copyright Year	2003
Abstract	Phosphoenolpyruvate (PEP) carboxykinases harbor two divalent metal-binding sites. One cation interacts with the enzyme (metal binding site 1) to elicit activation, while a second cation (metal binding site 2) interacts with the nucleotide to serve as the metal nucleotide substrate. Mutants of Anaerobiospirillum succiniciproducens PEP carboxykinase have been constructed where Thr$^{249}$ and Asp$^{262}$, two residues of metal binding site 2 of the enzyme, were altered. Binding of the 3′(2′)-O- (N-methylantraniloyl) derivative of ADP provides a test of the structural integrity of these mutants. The conservative mutation (Asp262Glu) retains a significant proportion of the wild type enzymatic activity. Meanwhile, removal of the OH group of Thr$^{249}$ in the Thr249Ala mutant causes a decrease in V $_{max}$ by a factor of 1.1 × 10$^{4}$. Molecular modeling of wild type and mutant enzymes suggests that the lower catalytic efficiency of the Thr249Ala enzyme could be explained by a movement of the lateral chain of Lys$^{248}$, a critical catalytic residue, away from the reaction center.
Starting Page	515
Ending Page	519
Page Count	5
File Format	PDF
ISSN	02778033
Journal	The Protein Journal
Volume Number	22
Issue Number	6
e-ISSN	15734943
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	2003-01-01
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Organic Chemistry Bioorganic Chemistry Biochemistry Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Biochemistry

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