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| | {{STRUCTURE_1lue| PDB=1lue | SCENE= }} | | {{STRUCTURE_1lue| PDB=1lue | SCENE= }} |
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| - | '''RECOMBINANT SPERM WHALE MYOGLOBIN H64D/V68A/D122N MUTANT (MET)'''
| + | ===RECOMBINANT SPERM WHALE MYOGLOBIN H64D/V68A/D122N MUTANT (MET)=== |
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| - | ==Overview==
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| - | In the elucidation of structural requirements of heme vicinity for hydrogen peroxide activation, we found that the replacement of His-64 of myoglobin (Mb) with a negatively charged aspartate residue enhanced peroxidase and peroxygenase activities by 78- and 580-fold, respectively. Since residue 68 is known to influence the ligation of small molecules to the heme iron, we constructed H64D/V68X Mb bearing Ala, Ser, Leu, Ile, and Phe at position 68 to improve the oxidation activity. The Val-68 to Leu mutation of H64D Mb accelerates the reaction with H(2)O(2) to form a catalytic species, called compound I, and improves the one-electron oxidation of 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) (i.e., peroxidase activity) approximately 2-fold. On the other hand, H64D/V68I Mb oxygenates thioanisole 2.7- and 1600-fold faster than H64D and wild-type Mb, respectively. In terms of the enantioselectivity, H64D/V68A and H64D/V68S Mb were good chiral catalysts for thioanisole oxidation and produced the (R)-sulfoxide dominantly with 84% and 88% ee, respectively [Kato, S., et al. (2002) J. Am. Chem. Soc. 124, 8506-8507]. On the contrary, the substitution of Val-68 in H64D Mb with an isoleucine residue alters the dominant sulfoxide product from the (R)- to the (S)-isomer. The crystal structures of H64D/V68A and H64D/V68S Mb elucidated in this study do not clearly indicate residues interacting with thioanisole. However, comparison of the active site structures provides the basis to interpret the changes in oxidation activity: (1) direct steric interactions between residue 68 and substrates (i.e., H(2)O(2), ABTS, thioanisole) and (2) the polar interactions between tightly hydrogen-bonded water molecules and substrates.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12939145}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12939145 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12939145}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Myoglobin]] | | [[Category: Myoglobin]] |
| | [[Category: Sulfoxidation]] | | [[Category: Sulfoxidation]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:18:03 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:17:09 2008'' |
Revision as of 19:17, 2 July 2008
Template:STRUCTURE 1lue
RECOMBINANT SPERM WHALE MYOGLOBIN H64D/V68A/D122N MUTANT (MET)
Template:ABSTRACT PUBMED 12939145
About this Structure
1LUE is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.
Reference
Molecular engineering of myoglobin: influence of residue 68 on the rate and the enantioselectivity of oxidation reactions catalyzed by H64D/V68X myoglobin., Yang HJ, Matsui T, Ozaki S, Kato S, Ueno T, Phillips GN Jr, Fukuzumi S, Watanabe Y, Biochemistry. 2003 Sep 2;42(34):10174-81. PMID:12939145
Page seeded by OCA on Wed Jul 2 22:17:09 2008
