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Reference on EC 3.5.2.7 - imidazolonepropionase

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Consevage, M.W.; Porter, R.D.; Phillips, A.T.
Cloning and expression in Escherichia coli of histidine utilization genes from Pseudomonas putida
J. Bacteriol.
162
138-146
1985
Pseudomonas putida
Manually annotated by BRENDA team
Kendrick, K.E.; Wheelis, M.L.
Histidine dissimilation in Streptomyces coelicolor
J. Gen. Microbiol.
128
2029-2040
1982
Streptomyces coelicolor
Manually annotated by BRENDA team
Snyder, S.H.
Imidazolonepropionic acid hydrolase (Rat liver)
Methods Enzymol.
17B
92-95
1971
Rattus norvegicus
-
Manually annotated by BRENDA team
Magasanik, B.; Kaminskas, E.; Kimhi, Y.
Imidazolonepropionic acid hydrolase (Bacillus subtilis)
Methods Enzymol.
17B
55-57
1971
Bacillus subtilis
-
Manually annotated by BRENDA team
Holm, L.; Sander, C.
An evolutionary treasure: Unification of a broad set of amidohydrolases related to urease
Proteins Struct. Funct. Genet.
28
72-82
1997
Caenorhabditis elegans
Manually annotated by BRENDA team
Smith, G.R.; Halpern, Y.S.; Magasanik, B.
Genetic and metabolic control of enzymes responsible for histidine degradation in Salmonella typhimurium. 4-imidazolone-5-propionate amidohydrolase and N-formimino-L-glutamate formiminohydrolase
J. Biol. Chem.
246
3320-3329
1971
Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Snyder, S.H.; Silva, O.L.; Kies, M.W.
The mammalian metabolism of L-histidine: IV. Purification and properties of imidazolone propionic acid hydrolase
J. Biol. Chem.
236
2996-2998
1961
Rattus norvegicus
Manually annotated by BRENDA team
Rao, D.R.; Greenberg, D.M.
Studies on the enzymic decomposition of urocanic acid
J. Biol. Chem.
236
1758-1763
1961
Klebsiella aerogenes, Bos taurus, Cavia porcellus, Clostridium tetanomorphum, Ovis aries, Pseudomonas fluorescens, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Yu, Y.; Li, L.; Zheng, X.; Liang, Y.; Su, X.
Protein preparation, crystallization and preliminary x-ray analysis of imidazolonepropionase from Bacillus subtilis
Biochim. Biophys. Acta
1764
153-156
2006
Bacillus subtilis (P42084), Bacillus subtilis
Manually annotated by BRENDA team
Tyagi, R.; Eswaramoorthy, S.; Burley, S.K.; Raushel, F.M.; Swaminathan, S.
A common catalytic mechanism for proteins of the HutI family
Biochemistry
47
5608-5615
2008
Agrobacterium tumefaciens (Q8U8Z6), Agrobacterium tumefaciens
Manually annotated by BRENDA team
Yu, Y.; Liang, Y.H.; Brostromer, E.; Quan, J.M.; Panjikar, S.; Dong, Y.H.; Su, X.D.
A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis
J. Biol. Chem.
281
36929-36936
2006
Bacillus subtilis (P42084), Bacillus subtilis
Manually annotated by BRENDA team
Yang, F.; Chu, W.; Yu, M.; Wang, Y.; Ma, S.; Dong, Y.; Wu, Z.
Local structure investigation of the active site of the imidazolonepropionase from Bacillus subtilis by XANES spectroscopy and ab initio calculations
J. Synchrotron Radiat.
15
129-133
2008
Bacillus subtilis (P42084), Bacillus subtilis
Manually annotated by BRENDA team
Tyagi, R.; Kumaran, D.; Burley, S.K.; Swaminathan, S.
X-ray structure of imidazolonepropionase from Agrobacterium tumefaciens at 1.87 A resolution
Proteins Struct. Funct. Bioinform.
69
652-658
2007
Agrobacterium tumefaciens (Q8U8Z6), Agrobacterium tumefaciens
Manually annotated by BRENDA team
Su, H.; Sheng, X.; Liu, Y.
Exploring the substrate specificity and catalytic mechanism of imidazolonepropionase (HutI) from Bacillus subtilis
Phys. Chem. Chem. Phys.
18
27928-27938
2016
Bacillus subtilis (P42084), Bacillus subtilis, Bacillus subtilis 168 (P42084)
Manually annotated by BRENDA team