Biochemical and structural characterization of the Arabidopsis bifunctional enzyme dethiobiotin synthetase-diaminopelargonic acid aminotransferase: evidence for substrate channeling in biotin synthesis.
Cobessi, David
Biochemical and structural characterization of the Arabidopsis bifunctional enzyme dethiobiotin synthetase-diaminopelargonic acid aminotransferase: evidence for substrate channeling in biotin synthesis. [electronic resource] - The Plant cell Apr 2012 - 1608-25 p. digital
Publication Type: Journal Article
1532-298X
10.1105/tpc.112.097675 doi
Amino Acid Sequence
Amino Acids--chemistry
Arabidopsis--enzymology
Arabidopsis Proteins--chemistry
Biocatalysis
Biosynthetic Pathways
Biotin--analogs & derivatives
Carbon-Nitrogen Ligases--chemistry
Catalytic Domain
Holoenzymes--chemistry
Kinetics
Ligands
Models, Molecular
Molecular Sequence Data
Mutation--genetics
Protein Binding
Protein Multimerization
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins--biosynthesis
Subcellular Fractions--enzymology
Substrate Specificity
Transaminases--chemistry
Biochemical and structural characterization of the Arabidopsis bifunctional enzyme dethiobiotin synthetase-diaminopelargonic acid aminotransferase: evidence for substrate channeling in biotin synthesis. [electronic resource] - The Plant cell Apr 2012 - 1608-25 p. digital
Publication Type: Journal Article
1532-298X
10.1105/tpc.112.097675 doi
Amino Acid Sequence
Amino Acids--chemistry
Arabidopsis--enzymology
Arabidopsis Proteins--chemistry
Biocatalysis
Biosynthetic Pathways
Biotin--analogs & derivatives
Carbon-Nitrogen Ligases--chemistry
Catalytic Domain
Holoenzymes--chemistry
Kinetics
Ligands
Models, Molecular
Molecular Sequence Data
Mutation--genetics
Protein Binding
Protein Multimerization
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins--biosynthesis
Subcellular Fractions--enzymology
Substrate Specificity
Transaminases--chemistry