This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2olq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2olq.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2olq.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2olq| PDB=2olq | SCENE= }}
{{STRUCTURE_2olq| PDB=2olq | SCENE= }}
-
'''How Does an Enzyme Recognize CO2?'''
+
===How Does an Enzyme Recognize CO2?===
-
==Overview==
+
<!--
-
Phosphoenolpyruvate carboxykinase (PCK) reversibly catalyzes the carboxylation of phosphoenolpyruvate to oxaloacetate. Carbon dioxide, and not bicarbonate ion, is the substrate utilized. Assays of the carboxylation reaction show that initial velocities are 7.6-fold higher when CO(2) is used instead of HCO(3)(-). Two Escherichia coli PCK-CO(2) crystal structures are presented here. The location of CO(2) is the same for both structures; however the orientation of CO(2) is significantly different, likely from the presence of a manganese ion in one of the structures. PCK and the other three known protein-CO(2) crystal structure complexes have been compared; all have CO(2) hydrogen bonding with a basic amino acid side chain (Arg65 or Lys213 in PCK), likely to polarize CO(2) to make the central carbon atom more electrophilic and thus more reactive. Kinetic studies found that the PCK mutant Arg65Gln increased the K(M) for substrates PEP and oxaloacetate but not for CO(2). The unchanged K(M) for CO(2) can be explained since the Arg65Gln mutant likely maintains a hydrogen bond to one of the oxygen atoms of carbon dioxide.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17475535}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17475535 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17475535}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Co2]]
[[Category: Co2]]
[[Category: Phosphoenolpyruvate carboxykinase]]
[[Category: Phosphoenolpyruvate carboxykinase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:10:31 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:32:48 2008''

Revision as of 02:32, 28 July 2008

Image:2olq.png

Template:STRUCTURE 2olq

How Does an Enzyme Recognize CO2?

Template:ABSTRACT PUBMED 17475535

About this Structure

2OLQ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

How does an enzyme recognize CO2?, Cotelesage JJ, Puttick J, Goldie H, Rajabi B, Novakovski B, Delbaere LT, Int J Biochem Cell Biol. 2007;39(6):1204-10. Epub 2007 Mar 30. PMID:17475535

Page seeded by OCA on Mon Jul 28 05:32:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2olq"
Personal tools