2008
DOI: 10.1107/s0907444908009438
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Insights into the structural basis of substrate recognition by histidinol-phosphate aminotransferase fromCorynebacterium glutamicum

Abstract: Histidinol-phosphate aminotransferase (HisC) is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes the reversible transamination reaction between histidinol phosphate (His-P) and 2-oxoglutarate (O-Glu). The crystal structures of apo histidinol-phosphate aminotransferase from Corynebacterium glutamicum, of the internal PLP aldimine adduct and of a pyridoxamine 5-phosphate-enzyme complex were determined at resolutions of 2.2, 2.1 and 1.8 A, respectively. Residues important for substrate specificity were id… Show more

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Cited by 8 publications
(23 citation statements)
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“…The enzyme exhibits a K m value for Hol‐P of 0.89 ± 0.1 mM, a k cat value of 1.18 ± 0.1 s −1 and a specific activity of 2.8 μmol min −1 mg −1 (Marienhagen et al ., ). Interestingly, HisC Cg shows also activity with the precursors of leucine and aromatic amino acids in in vitro assays, but the K m values are two orders of magnitude higher compared with those observed with the histidine precursor and HisC Cg does not contribute to aromatic amino acid synthesis in vivo (Marienhagen et al ., 2005; 2008). The crystal structure of HisC Cg has been solved revealing a three‐domain structure of the monomer, with a N‐terminal arm, a large PLP binding domain, and a small C‐terminal domain (Marienhagen et al ., ).…”
Section: Enzymes Involved In Histidine Biosynthesismentioning
confidence: 97%
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“…The enzyme exhibits a K m value for Hol‐P of 0.89 ± 0.1 mM, a k cat value of 1.18 ± 0.1 s −1 and a specific activity of 2.8 μmol min −1 mg −1 (Marienhagen et al ., ). Interestingly, HisC Cg shows also activity with the precursors of leucine and aromatic amino acids in in vitro assays, but the K m values are two orders of magnitude higher compared with those observed with the histidine precursor and HisC Cg does not contribute to aromatic amino acid synthesis in vivo (Marienhagen et al ., 2005; 2008). The crystal structure of HisC Cg has been solved revealing a three‐domain structure of the monomer, with a N‐terminal arm, a large PLP binding domain, and a small C‐terminal domain (Marienhagen et al ., ).…”
Section: Enzymes Involved In Histidine Biosynthesismentioning
confidence: 97%
“…Interestingly, HisC Cg shows also activity with the precursors of leucine and aromatic amino acids in in vitro assays, but the K m values are two orders of magnitude higher compared with those observed with the histidine precursor and HisC Cg does not contribute to aromatic amino acid synthesis in vivo (Marienhagen et al ., 2005; 2008). The crystal structure of HisC Cg has been solved revealing a three‐domain structure of the monomer, with a N‐terminal arm, a large PLP binding domain, and a small C‐terminal domain (Marienhagen et al ., ). HisC Cg dimerization occurs via extensive hydrophobic interactions and 24 intersubunit hydrogen bonds with the N‐terminal arm contributing significantly to the intersubunit interface (Marienhagen et al ., ).…”
Section: Enzymes Involved In Histidine Biosynthesismentioning
confidence: 99%
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“…Here, the in vivo function could be studied only when the other two genes were inactivated (8). Nonetheless, we succeeded in identifying the function of 11 ATs of 20 putative PLP-dependent proteins encoded in the Corynebacterium glutamicum genome, thus gaining a global view of the transamination activities in this bacterium (16,17). This bacterium is of particular interest due to its excellent amino acid production properties.…”
mentioning
confidence: 99%
“…2A-2D) the enzymes of class I, II, IV and V can be defined as -transaminases in that they transfer the amino group to and from the position to a carboxylic acid (or phosphate ester in the case of the class II enzyme L-histidinol-phosphate transaminase [44]). A recent addition to the class II enzymes (based on the protein amino acid sequence alignment) is from the bacterium Mezorhizobium sp.…”
Section: Alpha Transaminasesmentioning
confidence: 99%