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.


1kck

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kck.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1kck.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kck| PDB=1kck | SCENE= }}
{{STRUCTURE_1kck| PDB=1kck | SCENE= }}
-
'''Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant N193G'''
+
===Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant N193G===
-
==Overview==
+
<!--
-
Cyclodextrin-glycosyltransferase (CGTase) catalyzes the formation of alpha-, beta-, and gamma-cyclodextrins (cyclic alpha-(1,4)-linked oligosaccharides of 6, 7, or 8 glucose residues, respectively) from starch. Nine substrate binding subsites were observed in an x-ray structure of the CGTase from Bacillus circulans strain 251 complexed with a maltononaose substrate. Subsite -6 is conserved in CGTases, suggesting its importance for the reactions catalyzed by the enzyme. To investigate this in detail, we made six mutant CGTases (Y167F, G179L, G180L, N193G, N193L, and G179L/G180L). All subsite -6 mutants had decreased k(cat) values for beta-cyclodextrin formation, as well as for the disproportionation and coupling reactions, but not for hydrolysis. Especially G179L, G180L, and G179L/G180L affected the transglycosylation activities, most prominently for the coupling reactions. The results demonstrate that (i) subsite -6 is important for all three CGTase-catalyzed transglycosylation reactions, (ii) Gly-180 is conserved because of its importance for the circularization of the linear substrates, (iii) it is possible to independently change cyclization and coupling activities, and (iv) substrate interactions at subsite -6 activate the enzyme in catalysis via an induced-fit mechanism. This article provides for the first time definite biochemical evidence for such an induced-fit mechanism in the alpha-amylase family.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11696539}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11696539 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11696539}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Glycosyl transferase]]
[[Category: Glycosyl transferase]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:34:29 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:07:49 2008''

Revision as of 07:07, 2 July 2008

Image:1kck.png

Template:STRUCTURE 1kck

Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant N193G

Template:ABSTRACT PUBMED 11696539

About this Structure

1KCK is a Single protein structure of sequence from Bacillus circulans. Full crystallographic information is available from OCA.

Reference

The remote substrate binding subsite -6 in cyclodextrin-glycosyltransferase controls the transferase activity of the enzyme via an induced-fit mechanism., Leemhuis H, Uitdehaag JC, Rozeboom HJ, Dijkstra BW, Dijkhuizen L, J Biol Chem. 2002 Jan 11;277(2):1113-9. Epub 2001 Nov 5. PMID:11696539

Page seeded by OCA on Wed Jul 2 10:07:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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