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1.29
-
mutant S140A, pH 8.1, 30°C
1.37
-
mutant S43A, pH 8.1, 30°C
1.62
-
mutant D141A, pH 8.1, 30°C
1.67
-
mutant D141E, pH 8.1, 30°C
1.76
-
mutant H44A, pH 8.1, 30°C
1.92
-
mutant Y52F, pH 8.1, 30°C
1.97
-
mutant D141N, pH 8.1, 30°C
11.98
-
mutant R259A, pH 8.1, 30°C
45.98
-
mutant M251A, pH 8.1, 30°C
57
-
wild-type, pH 8.1, 30°C
1.29
-
mutant enzyme S140A, pH and temperature not specified in the publication
1.37
-
mutant enzyme S43A, pH and temperature not specified in the publication
1.62
-
mutant enzyme D141A, pH and temperature not specified in the publication
1.67
-
mutant enzyme D141E, pH and temperature not specified in the publication
1.76
-
mutant enzyme H44A, pH and temperature not specified in the publication
1.92
-
mutant enzyme Y52F, pH and temperature not specified in the publication
1.97
-
mutant enzyme D141N, pH and temperature not specified in the publication
11.98
-
mutant enzyme R259A, pH and temperature not specified in the publication
45.98
-
mutant enzyme M251A, pH and temperature not specified in the publication
57.06
-
wild type enzyme, pH and temperature not specified in the publication
0.05
-
mutant Q257N, pH 8.5, 30°C
0.23
-
mutant H424N, pH 8.5, 30°C
0.37
-
mutant H290Q, pH 8.5, 30°C
0.59
-
mutant Y423F, pH 8.5, 30°C
1.43
-
wild-type enzyme, pH 8.5, 30°C
493
-
pH 7.4, 30°C, K291R
761
-
pH 7.4, 30°C, wild-type enzyme
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1.06
-
wild-type, pH 8.1, 30°C
5.27
-
mutant D141A, pH 8.1, 30°C
5.87
-
mutant D141N, pH 8.1, 30°C
10.75
-
mutant S43A, pH 8.1, 30°C
11.47
-
mutant R259A, pH 8.1, 30°C
12.38
-
mutant S140A, pH 8.1, 30°C
13.15
-
mutant M251A, pH 8.1, 30°C
14.13
-
mutant D141E, pH 8.1, 30°C
16.82
-
mutant Y52F, pH 8.1, 30°C
16.94
-
mutant H44A, pH 8.1, 30°C
1.06
-
wild type enzyme, pH and temperature not specified in the publication
5.27
-
mutant enzyme D141A, pH and temperature not specified in the publication
5.84
-
mutant enzyme D141N, pH and temperature not specified in the publication
10.75
-
mutant enzyme S43A, pH and temperature not specified in the publication
11.47
-
mutant enzyme R259A, pH and temperature not specified in the publication
12.38
-
mutant enzyme S140A, pH and temperature not specified in the publication
13.15
-
mutant enzyme M251A, pH and temperature not specified in the publication
14.13
-
mutant enzyme D141E, pH and temperature not specified in the publication
16.82
-
mutant enzyme Y52F, pH and temperature not specified in the publication
16.94
-
mutant enzyme H44A, pH and temperature not specified in the publication
0.0113
-
wild-type enzyme, pH 8.5, 30°C
0.021
-
mutant Y423F, pH 8.5, 30°C
0.033
-
mutant H424N, pH 8.5, 30°C
0.04
-
at pH 7.0 and 37°C
0.188
-
at pH 7.0 and 37°C
1.77
-
pH 7.4, 30°C, wild-type enzyme
2.3
-
pH 7.4, 30°C, Y252F
3.46
-
pH 7.4, 30°C, K291R
700
-
mutant Q257N, pH 8.5, 30°C
840
-
mutant H290Q, pH 8.5, 30°C
0.006
-
30°C, pH 7.8, in the presence of 0.5 mM Mn2+
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-
Oxidative degradation of purines by the facultative phototrophic bacterium Rhodopseudomonas capsulata
1986
Kaspari, H.; Busse, W.
Arch. Microbiol.
144
67-70
-
Aerobic degradation of purines by Enterobacter cloacae
1982
Machida, Y.; Nakanishi, T.
Agric. Biol. Chem.
46
2135-2136
Allantoate and ureidoglycolate degradation by Pseudomonas aeruginosa
1967
Trijbels, F.; Vogels, G.D.
Biochim. Biophys. Acta
132
115-126
Allantoicase and ureidoglycolase in Pseudomonas and Penicillium species
1966
Tribjels, F.; Vogels, G.D.
Biochim. Biophys. Acta
118
387-395
Conformation of allantoicase in aqueous solution
1971
S-Gravenmade, E.J.; van der Drift, C.; Vogels, G.D.
Biochim. Biophys. Acta
251
393-406
Allantoinase and allantoicase synthesis in Pseudomonas aerguinosa
1977
Rijnierse, V.F.M.; van der Drift, C.; Vogels, G.D.
Can. J. Microbiol.
23
633-637
Degradation of uric acid to urea and glyoxylate in peroxisomes
1979
Nogucchi, T.; Takada, Y.; Fujiwara, S.
J. Biol. Chem.
254
5272-5275
Metabolite compartmentation in Saccharomyces cerevisiae
1978
Zacharski, C.A.; Cooper, T.G.
J. Bacteriol.
135
490-497
-
Some properties of allantoate amidinohydrolase of Streptomyces viridiviolaceus
1980
Elzainy, T.A.; El-Awamry, Z.A.
Egypt. J. Bot.
23
137-144
-
Nature of allantoate hydrolysing enzyme of Streptomyces viridiviolacetus
1980
Zeinab, A.E.; Elzainy, T.A.
Egypt. J. Bot.
23
131-136
Uric acid utilization by Mycobacterium intracellulare and Mycobacterium scrofulaceum isolates
1983
Falkinham, J.O.; George, K.L.; Parker, B.C.; Gruft, H.
J. Bacteriol.
155
36-39
Fibrin mambrane endowed with biological functions. V. Multienzyme complex of uricase, catalase, allantoinase and allantoicase
1980
Okamotot, H.; Tipayang, P.; Inada, Y.
Biochim. Biophys. Acta
611
35-39
Xenopus allantoicase: Molecular cloning, enzymatic activity and developmental expression
2000
Vigetti, D.; Monetti, C.; Pollegioni, L.; Taramelli, R.; Bernardini, G.
Arch. Biochem. Biophys.
379
90-96
Allantoate amidinohydrolase (allantoicase) from Chlamydomonas reinhardtii: Its Purification and catalytic and molecular characterization
2000
Piedras, P.; Munoz, A.; Aguilar, M.; Pineda, M.
Arch. Biochem. Biophys.
378
340-348
Molecular cloning and characterization of alc the gene encoding allantoicase of Neurospora crassa
1990
Lee, H.; Fu, Y.H.; Marzluf, G.A.
Mol. Gen. Genet.
222
140-144
Nucleotide sequence and DNA recognition elements of alc, the structural gene which encodes allantoicase, a purine catabolic enzyme of Neurospora crassa
1990
Lee, H.; Fu, Y.H.; Marzluf, G.A.
Biochemistry
29
8779-8787
-
Solubilization and extraction of allantoinase and allantoicase from the green alga Chlamydomonas reinhardtii
1995
Piedras, P.; Cardenas, J.; Pineda, M.
Phytochem. Anal.
6
239-243
The degradation of urate in liver peroxisomes. Association of allantoinase with allantoicase in amphibian liver but not in fish and invertebrate liver
1983
Takada, Y.; Noguchi, T.
J. Biol. Chem.
258
4762-4764
S-ureidoglycolate dehydrogenase: Purification and properties
1971
Van der Drift, C.; van Helvoort, P.E.M.; Vogels, G.D.
Arch. Biochem. Biophys.
145
465-469
Catalysis, stereochemistry, and inhibition of ureidoglycolate lyase
2003
McIninch, J.K.; McIninch, J.D.; May, S.W.
J. Biol. Chem.
278
50091-50100
Urea is a product of ureidoglycolate degradation in chickpea. Purification and characterization of the ureidoglycolate urea-lyase
2001
Munoz, A.; Piedras, P.; Aguilar, M.; Pineda, M.
Plant Physiol.
125
828-834
Purification of allantoicase from Pseudomonas aeruginosa
1969
S-Gravenmade, E.J.; Vogels, G.D.
Antonie van Leeuwenhoek
35
463-466
Crystal structure of an allantoicase (YIR029W) from Saccharomyces cerevisiae at 2.4 A resolution
2004
Xu, Q.; Schwarzenbacher, R.; Page, R.; Sims, E.; Abdubek, P.; Ambing, E.; Biorac, T.; Brinen, L.S.; Cambell, J.; Canaves, J.M.; Chiu, H.; Dai, X.; Deacon, A.M.; DiDonato, M.; Elsliger, M.; Floyd, R.; Godzik, A.; Grittini, C.; Grzechnik, S.K.; Hampton, E.;
Proteins
56
619-624
Crystal structure of ureidoglycolate hydrolase (AllA) from Escherichia coli O157:H7
2005
Raymond, S.; Tocilj, A.; Ajamian, E.; Li, Y.; Hung, M.; Matte, A.; Cygler, M.
Proteins
61
454-459
Role for an essential tyrosine in peptide amidation
2006
De, M.; Bell, J.; Blackburn, N.J.; Mains, R.E.; Eipper, B.A.
J. Biol. Chem.
281
20873-20882
An alternative pathway for ureide usage in legumes: enzymatic formation of a ureidoglycolate adduct in Cicer arietinum and Phaseolus vulgaris
2011
Munoz, A.; Bannenberg, G.L.; Montero, O.; Cabello-Diaz, J.M.; Piedras, P.; Pineda, M.
J. Exp. Bot.
62
307-318
Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli
1999
Cusa, E.; Obradors, N.; Baldoma, L.; Badia, J.; Aguilar, J.
J. Bacteriol.
181
7479-7484
Structural and functional insights into (S)-ureidoglycolate dehydrogenase, a metabolic branch point enzyme in nitrogen utilization
2012
Kim, M.I.; Shin, I.; Cho, S.; Lee, J.; Rhee, S.
PLoS ONE
7
e52066
Novel insights into E. colis hexuronate metabolism: KduI facilitates the conversion of galacturonate and glucuronate under osmotic stress conditions
2013
Rothe, M.; Alpert, C.; Loh, G.; Blaut, M.
PLoS ONE
8
e56906
The ureide-degrading reactions of purine ring catabolism employ three amidohydrolases and one aminohydrolase in Arabidopsis, soybean, and rice
2013
Werner, A.K.; Medina-Escobar, N.; Zulawski, M.; Sparkes, I.A.; Cao, F.Q.; Witte, C.P.
Plant Physiol.
163
672-681
Ureidoglycolate hydrolase, amidohydrolase, lyase: how errors in biological databases are incorporated in scientific papers and vice versa
2013
Percudani, R.; Carnevali, D.; Puggioni, V.
Database (Oxford)
2013
bat071
Structural and functional insights into (S)-ureidoglycine aminohydrolase, key enzyme of purine catabolism in Arabidopsis thaliana
2012
Shin, I.; Percudani, R.; Rhee, S.
J. Biol. Chem.
287
18796-18805
Structural insights into the substrate specificity of (S)-ureidoglycolate amidohydrolase and its comparison with allantoate amidohydrolase
2014
Shin, I.; Han, K.; Rhee, S.
J. Mol. Biol.
426
3028-3040
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