From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1mgo.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1mgo.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1mgo| PDB=1mgo | SCENE= }} | | {{STRUCTURE_1mgo| PDB=1mgo | SCENE= }} |
| | | | |
| - | '''Horse Liver Alcohol Dehydrogenase Phe93Ala Mutant'''
| + | ===Horse Liver Alcohol Dehydrogenase Phe93Ala Mutant=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The relationship between substrate mobility and catalysis was studied with wild-type and Phe93Ala (F93A) horse liver alcohol dehydrogenase (ADH). Wild-type ADH binds 2,3,4,5,6-pentafluorobenzyl alcohol in one position as shown by X-ray results, and (19)F NMR shows five resonances for the fluorines of the bound alcohol. The two meta-fluorines exchange positions with a rate constant of about 4 s(-1), indicating that mobility (ring flipping) of the benzyl alcohol is relatively restricted. The wild-type enzyme binds 2,3-difluorobenzyl alcohol in two alternative conformations that are related by a ring flip and a small translation of the fluorinated benzene ring, and the (19)F NMR spectrum shows three resonances for the two bound fluorines, consistent with the two orientations. Phe-93 interacts with the bound benzyl alcohols, and the F93A substitution decreases the rate constants for hydride transfer for benzyl alcohol oxidation and benzaldehyde reduction by 7.4- and 130-fold, respectively. The structure of F93A ADH crystallized with NAD(+) and 2,3,4,5,6-pentafluorobenzyl alcohol is similar to the structure of the wild-type enzyme complex except that the pentafluorobenzyl alcohol is not found in one position. The (19)F NMR spectrum of the F93A ADH-NAD(+)-pentafluorobenzyl alcohol complex shows three resonances for the bound fluorines. Line shape analysis of the spectrum suggests the bound pentafluorobenzyl ring undergoes rapid ring-flipping at about 20 000 s(-1). The F93A substitution greatly increases the mobility of the benzyl alcohol but modestly and differentially decreases the probability that the substrate is preorganized for hydride transfer.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12501206}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12501206 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_12501206}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| | [[Category: Nicotinamide coenzyme]] | | [[Category: Nicotinamide coenzyme]] |
| | [[Category: Substrate binding site]] | | [[Category: Substrate binding site]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:59:54 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:55:03 2008'' |
Revision as of 20:55, 2 July 2008
Template:STRUCTURE 1mgo
Horse Liver Alcohol Dehydrogenase Phe93Ala Mutant
Template:ABSTRACT PUBMED 12501206
About this Structure
1MGO is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.
Reference
Mobility of fluorobenzyl alcohols bound to liver alcohol dehydrogenases as determined by NMR and X-ray crystallographic studies., Rubach JK, Plapp BV, Biochemistry. 2002 Dec 31;41(52):15770-9. PMID:12501206
Page seeded by OCA on Wed Jul 2 23:55:03 2008
