| Title | Date | PubMed ID |
|---|
| A common catalytic mechanism for proteins of the HutI family. | 2008 May 20 | 18442260 |
| Local structure investigation of the active site of the imidazolonepropionase from Bacillus subtilis by XANES spectroscopy and ab initio calculations. | 2008 Mar | 18296777 |
| X-ray structure of imidazolonepropionase from Agrobacterium tumefaciens at 1.87 A resolution. | 2007 Nov 15 | 17640072 |
| A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis. | 2006 Dec 1 | 16990261 |
| Protein preparation, crystallization and preliminary X-ray analysis of imidazolonepropionase from Bacillus subtilis. | 2006 Jan | 16198643 |
| An evolutionary treasure: unification of a broad set of amidohydrolases related to urease. | 1997 May | 9144792 |
| Cloning and expression in Escherichia coli of histidine utilization genes from Pseudomonas putida. | 1985 Apr | 2858467 |
| Histidine dissimilation in Streptomyces coelicolor. | 1982 Sep | 6129283 |
| Genetic and metabolic control of enzymes responsible for histidine degradation in Salmonella typhimurium. 4-imidazolone-5-propionate amidohydrolase and N-formimino-L-glutamate formiminohydrolase. | 1971 May 25 | 4930059 |
| The mammalian metabolism of L-histidine. IV. Purification and properties of imidazolone propionic acid hydrolase. | 1961 Nov | 13914653 |