Urease

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=General Information=
=General Information=
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Urease catalyzes the hydrolysis of urea to ammonia and carbon dioxide, thus allowing organisms to use exogenous and internally generated urea as a nitrogen source. <ref name="gp">PMID: PMC2443974 </ref>.
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Urease catalyzes the hydrolysis of urea to ammonia and carbon dioxide, thus allowing organisms to use exogenous and internally generated urea as a nitrogen source. <ref name="urease">PMID: PMC2443974 </ref>.
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The reaction occurs as follows:
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(NH<sub>2</sub>)<sub>2</sub>CO + H<sub>2</sub>O → CO<sub>2</sub> + 2NH<sub>3</sub>
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Urease is a nickel-dependent metalloenzyme, is synthesized by plants, some bacteria, and fungi. <ref name="urease">PMID: PMC2443974 </ref>.
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Jack bean urease was the first enzyme to be crystallized, accomplished by James. B. Sumner in 1926, one for which he was awarded Nobel Prize in chemistry in 1946. <ref name="jb">http://www.jbc.org/content/277/35/e23.full?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&searchid=1130442887043_7599&stored_search=&FIRSTINDEX=60&tocsectionid=Classics&sortspec=PUBDATE_SORTDATE+desc </ref>. Like urease, its substrate urea is also of major historical significance since it was the first organic compound to be synthesized in 1828. Urea is a major nitrogenous waste product of biological actions. In general, urea is short-lived and rapidly metabolized by microbial activities. Urease (urea amidohydrolase EC 3.3.1.5) catalyzes the hydrolysis of urea to form ammonia and carbamate. The later compound spontaneously hydrolyzes at physiological pH to form carbonic acid and a second molecule of ammonia.<ref name="urea">Andrews, R. K., Blakeley, R. L. & Zerner, B. (1984). Urea and urease. Adv. Inorg. Biochem. 6, 245–283.</ref>.
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=Characteristics=
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Molecular weight: 480 kDa or 545 kDa for Jack Bean Urease
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Optimum pH: 7.4
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Optimum Temperature: 60 degrees Celsius
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Enzymatic specificity: urea and hydroxyurea
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Inhibitors: heavy metals (Pb<sup>-</sup> & Pb<sup>2</sup><sup>+</sup>)
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=Structural Properties=
=Structural Properties=

Revision as of 02:23, 1 April 2011

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Contents

General Information

Urease catalyzes the hydrolysis of urea to ammonia and carbon dioxide, thus allowing organisms to use exogenous and internally generated urea as a nitrogen source. [1]. The reaction occurs as follows:

(NH2)2CO + H2O → CO2 + 2NH3

Urease is a nickel-dependent metalloenzyme, is synthesized by plants, some bacteria, and fungi. [1]. Jack bean urease was the first enzyme to be crystallized, accomplished by James. B. Sumner in 1926, one for which he was awarded Nobel Prize in chemistry in 1946. [2]. Like urease, its substrate urea is also of major historical significance since it was the first organic compound to be synthesized in 1828. Urea is a major nitrogenous waste product of biological actions. In general, urea is short-lived and rapidly metabolized by microbial activities. Urease (urea amidohydrolase EC 3.3.1.5) catalyzes the hydrolysis of urea to form ammonia and carbamate. The later compound spontaneously hydrolyzes at physiological pH to form carbonic acid and a second molecule of ammonia.[3].

Characteristics

Molecular weight: 480 kDa or 545 kDa for Jack Bean Urease

Optimum pH: 7.4

Optimum Temperature: 60 degrees Celsius

Enzymatic specificity: urea and hydroxyurea

Inhibitors: heavy metals (Pb- & Pb2+)


Structural Properties

Urease Active Site

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Function

References

  1. ↑ 1.0 1.1 PMID: PMC2443974
  2. ↑ http://www.jbc.org/content/277/35/e23.full?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&searchid=1130442887043_7599&stored_search=&FIRSTINDEX=60&tocsectionid=Classics&sortspec=PUBDATE_SORTDATE+desc
  3. ↑ Andrews, R. K., Blakeley, R. L. & Zerner, B. (1984). Urea and urease. Adv. Inorg. Biochem. 6, 245–283.

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Andrea Graydon, Alexander Berchansky, David Canner, OCA

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