ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
The 1.9 A structure of the branched-chain amino-acid transaminase (IlvE) from Mycobacterium tuberculosis.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- Characterization of an aminotransferase TlBCAT from Trichoderma longibrachiatum UN32 involved in dendrobine-type total alkaloids biosynthesis.World journal of microbiology & biotechnology · 2024Article
- Research progress on branched-chain amino acid aminotransferases.Frontiers in genetics · 2023Review
- Key Enzymes Involved in the Synthesis of Hops Phytochemical Compounds: From Structure, Functions to Applications.International journal of molecular sciences · 2021Review
- Intracellular Mycobacterium tuberculosis Exploits Multiple Host Nitrogen Sources during Growth in Human Macrophages.Cell reports · 2019Article
- Bacterial Branched-Chain Amino Acid Biosynthesis: Structures, Mechanisms, and Drugability.Biochemistry · 2017Review
- Mechanism-Based Inhibition of the Mycobacterium tuberculosis Branched-Chain Aminotransferase by d- and l-Cycloserine.ACS chemical biology · 2017Article
- Discovery and structural characterisation of new fold type IV-transaminases exemplify the diversity of this enzyme fold.Scientific reports · 2016Article
- Chemical Mechanism of the Branched-Chain Aminotransferase IlvE from Mycobacterium tuberculosis.Biochemistry · 2016Article
- Role of Wax Ester Synthase/Acyl Coenzyme A:Diacylglycerol Acyltransferase in Oleaginous Streptomyces sp. Strain G25.Applied and environmental microbiology · 2016Article
- First structure of archaeal branched-chain amino acid aminotransferase from Thermoproteus uzoniensis specific for L-amino acids and R-amines.Extremophiles : life under extreme conditions · 2016Article
- Characterization of the branched-chain amino acid aminotransferase enzyme family in tomato.Plant physiology · 2010Article
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2 authors at 1 institution in 1 country.
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Abstract
Unlike mammals, bacteria encode enzymes that synthesize branched-chain amino acids. The pyridoxal 50-phosphate-dependent transaminase performs the final biosynthetic step in these pathways, converting keto acid precursors into -amino acids. The branched-chain amino-acid transaminase from Mycobacterium tuberculosis (MtIlvE) has been crystallized and its structure has been solved at 1.9 angstrom resolution. The MtIlvE monomer is composed of two domains that interact to form the active site. The biologically active form of IlvE is a homodimer in which each monomer contributes a substrate-specificity loop to the partner molecule. Additional substrate selectivity may be imparted by a conserved N-terminal Phe30 residue, which has previously been observed to shield the active site in the type IV fold homodimer. The active site of MtIlvE contains density corresponding to bound PMP, which is likely to be a consequence of the presence of tryptone in the crystallization medium. Additionally, two cysteine residues are positioned at the dimer interface for disulfide-bond formation under oxidative conditions. It is unknown whether they are involved in any regulatory activities analogous to those of the human mitochondrial branched-chain amino-acid transaminase.
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