Molecular and physiological analysis of Arabidopsis mutants defective in cytosolic or chloroplastic aspartate aminotransferase

Plant Physiology

Volumn 129, Issue 2, 2002, Pages 650-660

  Miesak, Barbara H ^a   Coruzzi, Gloria M ^a  

^a NEW YORK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOASSAY; DNA SEQUENCES; GENES; METABOLISM; NITROGEN; PHYSIOLOGY;

MUTANT DEFICIENT;

PLANTS (BOTANY);

ARABIDOPSIS; EMBRYOPHYTA; INSERTION SEQUENCES;

ASPARTATE AMINOTRANSFERASE; ASPARTATE AMINOTRANSFERASE ISOENZYME 1; ASPARTIC ACID; BACTERIAL DNA; T DNA; T-DNA;

AMINO ACID SUBSTITUTION; ARABIDOPSIS; ARTICLE; CHLOROPLAST; ENZYMOLOGY; GENETICS; GROWTH, DEVELOPMENT AND AGING; ISOLATION AND PURIFICATION; METABOLISM; MISSENSE MUTATION; MUTATION; PLANT ROOT; POLYMERASE CHAIN REACTION;

AMINO ACID SUBSTITUTION; ARABIDOPSIS; ASPARTATE AMINOTRANSFERASE, CYTOPLASMIC; ASPARTATE AMINOTRANSFERASES; ASPARTIC ACID; CHLOROPLASTS; DNA, BACTERIAL; MUTATION; MUTATION, MISSENSE; PLANT ROOTS; POLYMERASE CHAIN REACTION;

EID: 0035983639     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.005090     Document Type: Article

References (35)

1. 5-Fluoroindole resistance identifies tryptophan synthase beta subunit mutants in Arabidopsis thaliana
2. Metabolic significance of transamination
3. Aminotransferases in higher plants
4. m
5. Ammonia assimilation
6. Spatial organization of enzymes in plant metabolic pathways
7. Plant enzyme structure. Explaining substrate specificity and the evolution of function
8. Channeling of substrates and intermediates in enzyme-catalyzed reactions
9. Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: Role of Tyr70 in the catalytic processes
10. Influence of ionic strength, pH, and chelation of divalent metals on isolation of polyribosomes from tobacco leaves
11. Three-dimensional structures of aspartate aminotransferase from Escherichia coli and its mutant enzyme at 2.5 A resolution
12. Crystalline aspartate aminotransferase: Lattice-induced functional asymmetry of the two subunits
13. Significant improvement to the catalytic properties of aspartate aminotransferase: Role of hydrophobic and charged residues in the substrate binding pocket
14. T-DNA as an insertional mutagen in Arabidopsis
15. Use of Arabidopsis mutants and genes to study amide amino acid biosynthesis
16. Reciprocal regulation of distinct asparagine synthetase genes by light and metabolites in Arabidopsis thaliana
17. Metabolic regulation of the gene encoding glutamine-dependent asparagine synthetase in Arabidopsis thaliana
18. Domain closure in mitochondrial aspartate aminotransferase
19. Evolutionary relationships among homologous proteins
20. A revised medium for rapid growth and bio assays with tobacco tissue cultures
21. X-ray crystallographic study of pyridoxal 5′-phosphate-type aspartate aminotransferases from E. coli in open and closed form
22. Functional roles of valine 37 and glycine 38 in the mobile loop of porcine cytosolic aspartate aminotransferase
23. Transaminases
24. The aspartate aminotransferase gene Family of Arabidopsis encodes isoenzymes localized to three distinct subcellular compartments
25. Arabidopsis mutants define an in vivo role for isoenzymes of aspartate aminotransferase in plant nitrogen assimilation
26. 2.8-A-Resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli
27. Nitrate regulation of metabolism and growth
28. Isolation and analysis of a cDNA clone that encodes an alfalfa (Medicago sativa) aspartate aminotransferase
29. Use of phloem exudate technique in the study of amino acid transport in pea plants
30. Isozymes in plant biology
31. Chloroplastic aspartate aminotransferase from Arabidopsis thaliana: An examination of the relationship between the structure of the gene and the spatial structure of the protein
32. Isolation, characterization, and expression of a cDNA clone encoding aspartate aminotransferase from Arabidopsis thaliana
33. Mutant aspartate aminotransferase (K258H) without pyridoxal-5′-phosphate-binding lysine residue structural and catalytic properties