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.


1geb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1geb.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1geb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1geb| PDB=1geb | SCENE= }}
{{STRUCTURE_1geb| PDB=1geb | SCENE= }}
-
'''X-RAY CRYSTAL STRUCTURE AND CATALYTIC PROPERTIES OF THR252ILE MUTANT OF CYTOCHROME P450CAM'''
+
===X-RAY CRYSTAL STRUCTURE AND CATALYTIC PROPERTIES OF THR252ILE MUTANT OF CYTOCHROME P450CAM===
-
==Overview==
+
<!--
-
The structure-function relationship in cytochrome P450cam monooxygenase was studied by employing its active site mutant Thr252Ile. X-ray crystallographic analyses of the ferric d-camphor-bound form of the mutant revealed that the mutation caused a structural change in the active site giving an enlarged oxygen-binding pocket that did not contain any hydrophilic group such as the OH group of Thr and H(2)O. The enzyme showed a low monooxygenase activity of ca. 1/10 of the activity of the wild-type enzyme. Kinetic analyses of each catalytic step revealed that the rate of proton-coupled reduction of the oxygenated intermediate of the enzyme, a ternary complex of dioxygen and d-camphor with the ferrous enzyme, decreased to about 1/30 of that of the wild-type enzyme, while the rates of other catalytic steps including the reduction of the ferric d-camphor-bound form by reduced putidaredoxin did not change significantly. These results indicated that a hydrophilic group(s) such as water and/or hydroxyl group in the active site is prerequisite to a proton supply for the reduction of the oxygenated intermediate, thereby giving support for the operation of a proton transfer network composed of Thr252, Asp251, and two other amino acids and water proposed by previous investigators.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11098139}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11098139 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11098139}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Cytochrome p450cam]]
[[Category: Cytochrome p450cam]]
[[Category: Monooxygenase]]
[[Category: Monooxygenase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:27:56 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:09:45 2008''

Revision as of 02:09, 1 July 2008

Image:1geb.png

Template:STRUCTURE 1geb

X-RAY CRYSTAL STRUCTURE AND CATALYTIC PROPERTIES OF THR252ILE MUTANT OF CYTOCHROME P450CAM

Template:ABSTRACT PUBMED 11098139

About this Structure

1GEB is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.

Reference

X-ray crystal structure and catalytic properties of Thr252Ile mutant of cytochrome P450cam: roles of Thr252 and water in the active center., Hishiki T, Shimada H, Nagano S, Egawa T, Kanamori Y, Makino R, Park SY, Adachi S, Shiro Y, Ishimura Y, J Biochem. 2000 Dec;128(6):965-74. PMID:11098139

Page seeded by OCA on Tue Jul 1 05:09:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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