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.


1ewd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ewd.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ewd.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ewd| PDB=1ewd | SCENE= }}
{{STRUCTURE_1ewd| PDB=1ewd | SCENE= }}
-
'''FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE'''
+
===FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE===
-
==Overview==
+
<!--
-
The aldolase catalytic cycle consists of a number of proton transfers that interconvert covalent enzyme intermediates. Glu-187 is a conserved amino acid that is located in the mammalian fructose-1,6-bisphosphate aldolase active site. Its central location, within hydrogen bonding distance of three other conserved active site residues: Lys-146, Glu-189, and Schiff base-forming Lys-229, makes it an ideal candidate for mediating proton transfers. Point mutations, Glu-187--&gt; Gln, Ala, which would inhibit proton transfers significantly, compromise activity. Trapping of enzymatic intermediates in Glu-187 mutants defines a proton transfer role for Glu-187 in substrate cleavage and Schiff base formation. Structural data show that loss of Glu-187 negative charge results in hydrogen bond formation between Lys-146 and Lys-229 consistent with a basic pK(a) for Lys-229 in native enzyme and supporting nucleophilic activation of Lys-229 by Glu-187 during Schiff base formation. The crystal structures also substantiate Glu-187 and Glu-189 as present in ionized form in native enzyme, compatible with their role of catalyzing proton exchange with solvent as indicated from solvent isotope effects. The proton exchange mechanism ensures Glu-187 basicity throughout the catalytic cycle requisite for mediating proton transfer and electrostatic stabilization of ketamine intermediates. Glutamate general base catalysis is a recurrent evolutionary feature of Schiff base0forming aldolases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11779856}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11779856 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11779856}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Lyase]]
[[Category: Lyase]]
[[Category: Schiff base]]
[[Category: Schiff base]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:35:49 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:07:19 2008''

Revision as of 23:07, 30 June 2008

Image:1ewd.png

Template:STRUCTURE 1ewd

FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE

Template:ABSTRACT PUBMED 11779856

About this Structure

1EWD is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

A conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases., Maurady A, Zdanov A, de Moissac D, Beaudry D, Sygusch J, J Biol Chem. 2002 Mar 15;277(11):9474-83. Epub 2002 Jan 4. PMID:11779856

Page seeded by OCA on Tue Jul 1 02:07:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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