Sequence of URE2_SPOPA
EC Number:3.5.1.5
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
urea + H2O = CO2 + 2 NH3
Other sequences found for EC No. 3.5.1.5
General information:
Sequence
0 MSNNNYIVPG EYRVAEGEIE INAGREKTTI RVSNTGDRPI QVGSHIHFVE VNKELLFDRA
60 EGIGRRLNIP SGTAARFEPG EEMEVELTEL GGNREVFGIS DLTNGSVDNK ELILQRAKEL
120 GYKGVE
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
881087
Benini S.,Ciurli S.,Nolting H.F.,Mangani S.
X-ray absorption spectroscopy study of native and phenylphosphorodiamidate-inhibited Bacillus pasteurii urease.
Eur. J. Biochem.
239
61-66
1996
881088
Benini S.,Ciurli S.,Rypniewski W.R.,Wilson K.S.,Mangani S.
Crystallization and preliminary high-resolution X-ray diffraction analysis of native and beta-mercaptoethanol-inhibited urease from Bacillus pasteurii.
Acta Crystallogr. D
54
409-412
1998
881089
Benini S.,Rypniewski W.R.,Wilson K.S.,Miletti S.,Ciurli S.,Mangani S.
A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels.
Structure
7
205-216
1999
881090
Benini S.,Rypniewski W.R.,Wilson K.S.,Miletti S.,Ciurli S.,Mangani S.
The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 A resolution.
J. Biol. Inorg. Chem.
5
110-118
2000
881091
Benini S.,Rypniewski W.R.,Wilson K.S.,Ciurli S.,Mangani S.
Structure-based rationalization of urease inhibition by phosphate: novel insights into the enzyme mechanism.
J. Biol. Inorg. Chem.
6
778-790
2001
881092
Benini S.,Rypniewski W.R.,Wilson K.S.,Mangani S.,Ciurli S.
Molecular details of urease inhibition by boric acid: insights into the catalytic mechanism.
J. Am. Chem. Soc.
126
3714-3715
2004
