Article ; Online: Structural basis of potassium activation in plant asparaginases.
2018 Volume 285, Issue 8, Page(s) 1528–1539
Abstract: l-asparaginases (EC 3.5.1.1) play an important role in nitrogen mobilization in plants. Here, we investigated the biochemical and biophysical properties of potassium-dependent (PvAspG1) and potassium-independent (PvAspG-T2) l-asparaginases from Phaseolus ...
Abstract | l-asparaginases (EC 3.5.1.1) play an important role in nitrogen mobilization in plants. Here, we investigated the biochemical and biophysical properties of potassium-dependent (PvAspG1) and potassium-independent (PvAspG-T2) l-asparaginases from Phaseolus vulgaris. Our previous studies revealed that PvAspG1 requires potassium for catalytic activation and its crystal structure suggested that Ser-118 in the activation loop plays a critical role in coordinating the metal cation. This amino acid residue is replaced by isoleucine in PvAspG-T2. Reciprocal mutants of the enzymes were produced and the effect of the amino acid substitution on the kinetic parameters, allosteric effector binding, secondary structure conformation, and pH profile were studied. Introduction of the serine residue conferred potassium activation in PvAspG-T2. Conversely, the PvAspG1-S118I mutant could no longer be activated by potassium. PvAspG1 and the PvAspG-T2-I117S mutant had a similar half-maximal effective concentration (EC |
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MeSH term(s) | Amino Acid Sequence ; Asparaginase/chemistry ; Asparaginase/genetics ; Asparaginase/metabolism ; Binding Sites/genetics ; Biocatalysis ; Circular Dichroism ; Kinetics ; Models, Molecular ; Mutation ; Phaseolus/enzymology ; Phaseolus/genetics ; Plant Proteins/chemistry ; Plant Proteins/genetics ; Plant Proteins/metabolism ; Potassium/metabolism ; Protein Conformation ; Sequence Homology, Amino Acid ; Serine/chemistry ; Serine/genetics ; Serine/metabolism ; Substrate Specificity |
Chemical Substances | Plant Proteins ; Serine (452VLY9402) ; Asparaginase (EC 3.5.1.1) ; Potassium (RWP5GA015D) |
Language | English |
Publishing date | 2018-03-14 |
Publishing country | England |
Document type | Journal Article ; Research Support, Non-U.S. Gov't |
ZDB-ID | 2173655-8 |
ISSN | 1742-4658 ; 1742-464X |
ISSN (online) | 1742-4658 |
ISSN | 1742-464X |
DOI | 10.1111/febs.14428 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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