2vsu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px <!-- The line below this paragraph, containing "STRUCTURE_2vsu", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...)
Line 1: Line 1:
-
[[Image:2vsu.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2vsu.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2vsu| PDB=2vsu | SCENE= }}
{{STRUCTURE_2vsu| PDB=2vsu | SCENE= }}
-
'''A TERNARY COMPLEX OF HYDROXYCINNAMOYL-COA HYDRATASE-LYASE (HCHL) WITH ACETYL-COENZYME A AND VANILLIN GIVES INSIGHTS INTO SUBSTRATE SPECIFICITY AND MECHANISM.'''
+
===A TERNARY COMPLEX OF HYDROXYCINNAMOYL-COA HYDRATASE-LYASE (HCHL) WITH ACETYL-COENZYME A AND VANILLIN GIVES INSIGHTS INTO SUBSTRATE SPECIFICITY AND MECHANISM.===
-
==Overview==
+
<!--
-
Hydroxycinnamoyl-CoA Hydratase-Lyase (HCHL) catalyses the biotransformation of feruloyl-CoA to acetyl-CoA and the important flavour-fragrance compound vanillin (4-hydroxy 3-methoxybenzaldehyde) and is exploited in whole-cell systems for the bioconversion of ferulic acid to natural-equivalent vanillin. The reaction catalysed by HCHL has been thought to proceed by a two-step process involving first the hydration of the double bond of feruloyl-CoA, then the cleavage of the resultant beta-hydroxy thioester by retro-aldol reaction to yield the products. Kinetic analysis of active site residues identified using the crystal structure of HCHL revealed that whilst Glu-143 was essential for activity, Ser-123 played no major role in catalysis. However, mutation of Tyr-239 to Phe greatly increased the KM for the substrate ferulic acid, fulfilling its anticipated role as a factor in substrate binding. Structures of wild-type HCHL and of the Ser123Ala mutant, each of which had been co-crystallised with feruloyl-CoA, reveal a subtle helix movement upon ligand binding, the consequence of which is to bring the phenolic hydroxyl of Tyr-239 into close proximity with Tyr-75 from a neighbouring subunit in order to bind the phenolic hydroxyl of the product vanillin, for which electron density was observed. The active site residues of ligand-bound HCHL display a remarkable three-dimensional overlap with those of a structurally unrelated enzyme, vanillyl alcohol oxidase, that also recognises para-hydroxylated aromatic substrates related to vanillin. The data both explain the observed substrate specificity of HCHL for para-hydroxylated cinnamate derivatives and illustrate a remarkable convergence of the molecular determinants of ligand recognition between two otherwise unrelated enzymes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18479250}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18479250 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18479250}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Hydratase]]
[[Category: Hydratase]]
[[Category: Lyase]]
[[Category: Lyase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:17:01 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:24:44 2008''

Revision as of 21:24, 28 July 2008

Image:2vsu.png

Template:STRUCTURE 2vsu

A TERNARY COMPLEX OF HYDROXYCINNAMOYL-COA HYDRATASE-LYASE (HCHL) WITH ACETYL-COENZYME A AND VANILLIN GIVES INSIGHTS INTO SUBSTRATE SPECIFICITY AND MECHANISM.

Template:ABSTRACT PUBMED 18479250

About this Structure

2VSU is a Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA.

Reference

A ternary complex of Hydroxycinnamoyl-CoA Hydratase-Lyase (HCHL) with acetyl-Coenzyme A and vanillin gives insights into substrate specificity and mechanism., Bennett JP, Bertin L, Moulton B, Fairlamb IJ, Brzozowski AM, Walton NJ, Grogan G, Biochem J. 2008 May 14;. PMID:18479250

Page seeded by OCA on Tue Jul 29 00:24:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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