Metal Binding Asp-120 in Metallo-β-lactamase L1 from Stenotrophomonas maltophilia Plays a Crucial Role in Catalysis

Metallo-β-lactamase L1 from Stenotrophomonas maltophilia is a dinuclear Zn(II) enzyme that contains a metal-binding aspartic acid in a position to potentially play an important role in catalysis. The presence of this metal-binding aspartic acid appears to be common to most dinuclear, metal-containin...

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Veröffentlicht in:	The Journal of biological chemistry 2004-01, Vol.279 (2), p.920-927
Hauptverfasser:	Garrity, James D., Carenbauer, Anne L., Herron, Lissa R., Crowder, Michael W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Aspartic Acid - chemistry beta-Lactamases - chemistry Binding Sites Catalysis Circular Dichroism Escherichia coli - metabolism Hydrogen Bonding Hydrogen-Ion Concentration Kinetics Metals - metabolism Models, Molecular Mutagenesis, Site-Directed Mutation Protein Binding Protein Folding Protons Stenotrophomonas maltophilia Stenotrophomonas maltophilia - enzymology Zinc - chemistry
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