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Martínez-Rodríguez, S, Las Heras-Vázquez, FJ, Clemente-Jiménez, JM and Rodríguez-Vico, F (2004) Biochemical characterization of a novel hydantoin racemase from Agrobacterium tumefaciens C58. Biochimie 86:77-81
A novel hydantoin racemase gene of Agrobacterium tumefaciens C58 (AthyuA2) has been cloned and expressed in Escherichia coli BL21. The recombinant protein was purified in a one-step procedure and showed an apparent molecular mass of 27000 Da in SDS-gel electrophoresis. Size exclusion chromatography analysis determined a molecular mass of approximately 100000 Da, suggesting that the native enzyme is a tetramer. The optimum pH and temperature for hydantoin racemase activity were 7.5 and 55 degrees C, respectively, with L-5-ethylhydantoin as substrate. Enzyme activity was strongly inhibited by Cu(2+) and Hg(2+). No effect on enzyme activity was detected with any other divalent cations, EDTA or DTT, suggesting that it is not a metalloenzyme. Kinetic studies showed the preference of the enzyme for hydantoins with short rather than long aliphatic side chains or hydantoins with aromatic rings.
Agrobacterium tumefaciens/enzymology; Agrobacterium tumefaciens/genetics; Cloning, Molecular; Dithiothreitol/chemistry; Edetic Acid/chemistry; Gene Expression Regulation, Bacterial/genetics; Hydrogen-Ion Concentration; Kinetics; Metals/chemistry; Molecular Sequence Data; Molecular Weight; Racemases and Epimerases/chemistry; Racemases and Epimerases/genetics; Racemases and Epimerases/isolation & purification; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Sequence Analysis, DNA; Stereoisomerism; Temperature; Time Factors
|Gene product||Qualifier||GO Term||Evidence Code||with/from||Aspect||Extension||Notes||Status|
|GO:0036348: hydantoin racemase activity||
Figures show that Enzyme had no effect on metals. Enzyme Catalyzes hydantoin, aromatic rings with short side chains better than long side chains.
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