@article{MTMT:30625253,
	title = {New type of interaction between the SARAH domain of the tumour suppressor RASSF1A and its mitotic kinase Aurora A},
	url = {https://m2.mtmt.hu/api/publication/30625253},
	author = {Szimler, Tamás and Gráczer, Éva Laura and Györffy, Dániel and Végh, Barbara and Szilágyi, András and Hajdú, István and Závodszky, Péter and Kazinczyné Vas, Mária},
	doi = {10.1038/s41598-019-41972-x},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {9},
	unique-id = {30625253},
	issn = {2045-2322},
	year = {2019},
	eissn = {2045-2322},
	orcid-numbers = {Végh, Barbara/0000-0002-1405-4136; Szilágyi, András/0000-0002-1773-6861}
}

@article{MTMT:3023735,
	title = {Dual Role of the Active Site Residues of Thermus thermophilus 3-Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure.},
	url = {https://m2.mtmt.hu/api/publication/3023735},
	author = {Gráczer, Éva Laura and Szimler, Tamás and Garamszegi, A and Konarev, PV and Krezinger, Anikó and Oláh, Julianna and Pallo, A and Svergun, DI and Merli, A and Závodszky, Péter and Weiss, MS and Kazinczyné Vas, Mária},
	doi = {10.1021/acs.biochem.5b00839},
	journal-iso = {BIOCHEMISTRY-US},
	journal = {BIOCHEMISTRY},
	volume = {55},
	unique-id = {3023735},
	issn = {0006-2960},
	abstract = {The key active site residues K185, Y139, D217, D241, D245, and N102 of Thermus thermophilus 3-isopropylmalate dehydrogenase (Tt-IPMDH) have been replaced, one by one, with Ala. A drastic decrease in the kcat value (0.06% compared to that of the wild-type enzyme) has been observed for the K185A and D241A mutants. Similarly, the catalytic interactions (Km values) of these two mutants with the substrate IPM are weakened by more than 1 order of magnitude. The other mutants retained some (1-13%) of the catalytic activity of the wild-type enzyme and do not exhibit appreciable changes in the substrate Km values. The pH dependence of the wild-type enzyme activity (pK = 7.4) is shifted toward higher values for mutants K185A and D241A (pK values of 8.4 and 8.5, respectively). For the other mutants, smaller changes have been observed. Consequently, K185 and D241 may constitute a proton relay system that can assist in the abstraction of a proton from the OH group of IPM during catalysis. Molecular dynamics simulations provide strong support for the neutral character of K185 in the resting state of the enzyme, which implies that K185 abstracts the proton from the substrate and D241 assists the process via electrostatic interactions with K185. Quantum mechanics/molecular mechanics calculations revealed a significant increase in the activation energy of the hydride transfer of the redox step for both D217A and D241A mutants. Crystal structure analysis of the molecular contacts of the investigated residues in the enzyme-substrate complex revealed their additional importance (in particular that of K185, D217, and D241) in stabilizing the domain-closed active conformation. In accordance with this, small-angle X-ray scattering measurements indicated the complete absence of domain closure in the cases of D217A and D241A mutants, while only partial domain closure could be detected for the other mutants. This suggests that the same residues that are important for catalysis are also essential for inducing domain closure.},
	year = {2016},
	eissn = {1520-4995},
	pages = {560-574}
}

@article{MTMT:2807961,
	title = {Glutamate 270 plays an essential role in K+-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase},
	url = {https://m2.mtmt.hu/api/publication/2807961},
	author = {Gráczer, Éva Laura and Palló, Anna and Oláh, Julianna and Szimler, Tamás and Konarev, Petr V and Svergun, Dmitri I and Merli, Angelo and Závodszky, Péter and Weiss, Manfred S and Kazinczyné Vas, Mária},
	doi = {10.1016/j.febslet.2014.12.005},
	journal-iso = {FEBS LETT},
	journal = {FEBS LETTERS},
	volume = {589},
	unique-id = {2807961},
	issn = {0014-5793},
	year = {2015},
	eissn = {1873-3468},
	pages = {240-245}
}

@article{MTMT:2785761,
	title = {Structural and energetic basis of isopropylmalate dehydrogenase enzyme catalysis},
	url = {https://m2.mtmt.hu/api/publication/2785761},
	author = {Palló, A and Oláh, Julianna and Gráczer, Éva Laura and Merli, A and Závodszky, Péter and Weiss, MS and Kazinczyné Vas, Mária},
	doi = {10.1111/febs.13044},
	journal-iso = {FEBS J},
	journal = {FEBS JOURNAL},
	volume = {281},
	unique-id = {2785761},
	issn = {1742-464X},
	abstract = {The three-dimensional structure of the enzyme 3-isopropylmalate dehydrogenase from the bacterium Thermus thermophilus in complex with Mn2+, its substrate isopropylmalate and its co-factor product NADH at 2.0 Å resolution features a fully closed conformation of the enzyme. Upon closure of the two domains, the substrate and the co-factor are brought into precise relative orientation and close proximity, with a distance between the C2 atom of the substrate and the C4N atom of the pyridine ring of the co-factor of approximately 3.0 Å. The structure further shows binding of a K+ ion close to the active site, and provides an explanation for its known activating effect. Hence, this structure is an excellent mimic for the enzymatically competent complex. Using high-level QM/MM calculations, it may be demonstrated that, in the observed arrangement of the reactants, transfer of a hydride from the C2 atom of 3-isopropylmalate to the C4N atom of the pyridine ring of NAD+ is easily possible, with an activation energy of approximately 15 kcal·mol-1. The activation energy increases by approximately 4-6 kcal·mol-1 when the K+ ion is omitted from the calculations. In the most plausible scenario, prior to hydride transfer the ε-amino group of Lys185 acts as a general base in the reaction, aiding the deprotonation reaction of 3-isopropylmalate prior to hydride transfer by employing a low-barrier proton shuttle mechanism involving a water molecule.},
	keywords = {ARTICLE; CATALYSIS; PYRIDINE; nonhuman; Manganese; calculation; X-RAY CRYSTALLOGRAPHY; carboxy terminal sequence; enzyme structure; reduced nicotinamide adenine dinucleotide; potassium ion; enzyme conformation; enzyme active site; enzyme binding; Thermus thermophilus; 3 isopropylmalate dehydrogenase; ISOPROPYLMALATE DEHYDROGENASE; Oxidative decarboxylation; QM/MM calculations; general base catalysis},
	year = {2014},
	eissn = {1742-4658},
	pages = {5063-5076}
}

@article{MTMT:2604041,
	title = {Drugs Against Mycobacterium Tuberculosis 3-Isopropylmalate Dehydrogenase Can be Developed using Homologous Enzymes as Surrogate Targets},
	url = {https://m2.mtmt.hu/api/publication/2604041},
	author = {Gráczer, Éva Laura and Bacsó, András and Kónya, Dénes and Kazi, A and Soós, Tibor and Molnár, Laura and Szimler, Tamás and Beinrohr, László and Szilágyi, András and Závodszky, Péter and Kazinczyné Vas, Mária},
	journal-iso = {PROTEIN PEPTIDE LETT},
	journal = {PROTEIN AND PEPTIDE LETTERS},
	volume = {21},
	unique-id = {2604041},
	issn = {0929-8665},
	abstract = {3-Isopropylmalate dehydrogenase (IPMDH) from Mycobacterium tuberculosis (Mtb) may be a target for specific drugs against this pathogenic bacterium. We have expressed and purified Mtb IPMDH and determined its physical-chemical and enzymological properties. Size-exclusion chromatography and dynamic light scattering measurements (DLS) suggest a tetrameric structure for Mtb IPMDH, in contrast to the dimeric structure of most IPMDHs. The kinetic properties (kcat and Km values) of Mtb IPMDH and the pH-dependence of kcat are very similar to both Escherichia coli (Ec) and Thermus thermophilus (Tt) IPMDHs. The stability of Mtb IPMDH in 8 M urea is close to that of the mesophilic counterpart, Ec IPMDH, both of them being much less stable than the thermophilic (Tt) enzyme. Two known IPMDH inhibitors, O-methyl oxalohydroxamate and 3-methylmercaptomalate, have been synthesised. Their inhibitory effects were found to be independent of the origin of IPMDHs. Thus, experiments with either Ec or Tt IPMDH would be equally relevant for designing specific inhibitory drugs against Mtb IPMDH.},
	year = {2014},
	eissn = {1875-5305},
	pages = {1295-1307},
	orcid-numbers = {Beinrohr, László/0000-0001-6237-871X; Szilágyi, András/0000-0002-1773-6861}
}

@{MTMT:2573753,
	title = {Structural-Temporal Description of the Reaction Cycle},
	url = {https://m2.mtmt.hu/api/publication/2573753},
	author = {Bowler, MW and Kazinczyné Vas, Mária},
	booktitle = {Phosphoglycerate Kinase: A Hinge-Bending Enzyme},
	unique-id = {2573753},
	year = {2014},
	pages = {223-229}
}

@{MTMT:2573745,
	title = {Architecture of the Active Site and the Importance of Charge Balance in Catalysis},
	url = {https://m2.mtmt.hu/api/publication/2573745},
	author = {JP, Waltho and M W, Bowler and M J, Cliff and Kazinczyné Vas, Mária},
	booktitle = {Phosphoglycerate Kinase: A Hinge-Bending Enzyme},
	unique-id = {2573745},
	year = {2014},
	pages = {203-210}
}

@{MTMT:2573725,
	title = {Physiological and Non-Physiological Functions of PGK and Its Abundance},
	url = {https://m2.mtmt.hu/api/publication/2573725},
	author = {Matkovicsné Varga, Andrea and Kazinczyné Vas, Mária},
	booktitle = {Phosphoglycerate Kinase: A Hinge-Bending Enzyme},
	unique-id = {2573725},
	year = {2014},
	pages = {143-153},
	orcid-numbers = {Matkovicsné Varga, Andrea/0000-0001-9165-5368}
}

@{MTMT:2573721,
	title = {Substrate-Assisted Cooperative Interaction of the Two Domains: Mechanism of Domain Closure at the Level of Atomic Interactions},
	url = {https://m2.mtmt.hu/api/publication/2573721},
	author = {Kazinczyné Vas, Mária},
	booktitle = {Phosphoglycerate Kinase: A Hinge-Bending Enzyme},
	unique-id = {2573721},
	year = {2014},
	pages = {211-221}
}

@{MTMT:2573696,
	title = {Role of the Metal-Ion in Nucleotide Binding and in the Catalysis},
	url = {https://m2.mtmt.hu/api/publication/2573696},
	author = {Kazinczyné Vas, Mária},
	booktitle = {Phosphoglycerate Kinase: A Hinge-Bending Enzyme},
	unique-id = {2573696},
	year = {2014},
	pages = {195-200}
}