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PMID:16338958
| Citation |
Ishiyama, K, Inoue, E, Yamaya, T and Takahashi, H (2006) Gln49 and Ser174 residues play critical roles in determining the catalytic efficiencies of plant glutamine synthetase. Plant Cell Physiol. 47:299-303 |
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| Abstract |
Two essential residues playing critical roles in determining the substrate specificities of cytosolic glutamine synthetase (GS1) have been identified from the alignment of high-affinity (GLN1;1 and GLN1;4) and low-affinity (GLN1;2 and GLN1;3) GS1 isoenzymes in Arabidopsis, and confirmed by site-directed mutagenesis. The results indicated that either K49Q or A174S mutation is sufficient to increase the catalytic efficiencies of GLN1;3 by decreasing its Km values for ammonium. In contrast, replacement of Gln49 and Ser174 by lysine and alanine, respectively, was detrimental to glutamine synthetic activities in GLN1;4. The results suggested that Gln49 and Ser174 in the high-affinity GS1 isoenzymes are interchangeable with Lys49 and Ala174 in the low-affinity variants at the corresponding positions. |
| Links |
PubMed Online version:10.1093/pcp/pci238 |
| Keywords |
Alanine/analysis; Amino Acid Sequence; Arabidopsis/enzymology; Catalysis; Glutamate-Ammonia Ligase/chemistry; Glutamate-Ammonia Ligase/metabolism; Glutamine/analysis; Glutamine/physiology; Isoenzymes/chemistry; Isoenzymes/metabolism; Lysine/analysis; Molecular Sequence Data; Mutation; Quaternary Ammonium Compounds/metabolism; Serine/analysis; Serine/physiology; Substrate Specificity |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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