We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1f2w

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1f2w.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1f2w.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1f2w| PDB=1f2w | SCENE= }}
{{STRUCTURE_1f2w| PDB=1f2w | SCENE= }}
-
'''THE MECHANISM OF CYANAMIDE HYDRATION CATALYZED BY CARBONIC ANHYDRASE II REVEALED BY CRYOGENIC X-RAY DIFFRACTION'''
+
===THE MECHANISM OF CYANAMIDE HYDRATION CATALYZED BY CARBONIC ANHYDRASE II REVEALED BY CRYOGENIC X-RAY DIFFRACTION===
-
==Overview==
+
<!--
-
The three-dimensional structure of a possible intermediate in the hydration reaction of cyanamide to urea catalyzed by human carbonic anhydrase II (hCAII) has been determined by cryocrystallographic techniques. The crystal structure shows that two different adducts are formed under the experimental conditions and that they have different occupancy in the crystal. The high occupancy form consists of a binary hCAII-cyanamide complex where the substrate has replaced the zinc-bound hydroxide anion present in the native enzyme, maintaining the tetrahedral geometry around the metal ion. The second, low-occupancy form consists of a hCAII-cyanamide-water ternary complex where the catalytic zinc ion, still being bound to cyanamide, is approached by a water molecule in a five-coordinate adduct. While the first form can be considered a nonproductive complex, the second form may represent an intermediate state of the catalyzed reaction where the water molecule is about to perform a nucleophilic attack on the zinc-activated cyanamide substrate. The structural evidence is consistent with the kinetic data previously reported about this recently described hydrolytic reaction catalyzed by hCAII, and indicates that a different mechanism with respect to that generally accepted for the physiologic carbon dioxide hydration reaction may be adopted by the enzyme, depending on the substrate chemical properties.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11015219}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11015219 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11015219}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Supuran, C T.]]
[[Category: Supuran, C T.]]
[[Category: Protein-inhibitor complex]]
[[Category: Protein-inhibitor complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:49:38 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:28:48 2008''

Revision as of 23:29, 30 June 2008

Image:1f2w.png

Template:STRUCTURE 1f2w

THE MECHANISM OF CYANAMIDE HYDRATION CATALYZED BY CARBONIC ANHYDRASE II REVEALED BY CRYOGENIC X-RAY DIFFRACTION

Template:ABSTRACT PUBMED 11015219

About this Structure

1F2W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Mechanism of cyanamide hydration catalyzed by carbonic anhydrase II suggested by cryogenic X-ray diffraction., Guerri A, Briganti F, Scozzafava A, Supuran CT, Mangani S, Biochemistry. 2000 Oct 10;39(40):12391-7. PMID:11015219

Page seeded by OCA on Tue Jul 1 02:28:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1f2w"
Personal tools