User:Tommie Hata/2010 Pingry S.M.A.R.T. Team

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== 2010 Pingry S.M.A.R.T. Team-AKR's for Biofuel Cells ==
== 2010 Pingry S.M.A.R.T. Team-AKR's for Biofuel Cells ==
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[[Image:2010PingrySMARTTeam.jpg|right]]The 2010 Pingry School S.M.A.R.T. Team (Students Modeling A Research Topic) is working with Scott Banta at Columbia University to learn about enzymes being engineered for use in a biofuel cell. Features being engineered into these enzymes include (1) self-assembly into hydrogels, (2) alternate cofactor use, and (3) broader substrate specificity. The Banta Lab is engineering these features into AdhD alcohol dehydrogenase from the thermophile ''Pyrococcus furiosus''. AdhD is a member of the aldo-keto reductase (AKR) family of oxidoreductases. Taking advantage of its innate thermostable properties, the Banta Lab is engineering AdhD for use in biofuel cells.
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[[Image:2010PingrySMARTTeam.jpg|right]]The 2010 Pingry School S.M.A.R.T. Team (Students Modeling A Research Topic) is working with Scott Banta at Columbia University to learn about enzymes being engineered for use in biofuel cells. Features being engineered into these enzymes include (1) self-assembly into hydrogels, (2) alternate cofactor use, and (3) broader substrate specificity. AdhD alcohol dehydrogenase from the thermophile ''Pyrococcus furiosus'' is one of the enzymes being engineered with these features by the Banta Lab. AdhD is a member of the aldo-keto reductase (AKR) family of oxidoreductases. Taking advantage of its innate thermostable properties, the Banta Lab is engineering AdhD for use in biofuel cells.
The logical design and engineering of AdhD is based partially on the solved structures of other enzymes belonging to the AKR family of enzymes. Structures of mutants that bind alternate cofactors and those bound to its substrate provide insight into how to engineer AdhD and other enzymes of use in a biofuel cell. The 2010 Pingry S.M.A.R.T. Team is producing physical models of various AKR's that highlight the enzymes' structural and functional characteristics that are relevant to the Banta Lab's work.
The logical design and engineering of AdhD is based partially on the solved structures of other enzymes belonging to the AKR family of enzymes. Structures of mutants that bind alternate cofactors and those bound to its substrate provide insight into how to engineer AdhD and other enzymes of use in a biofuel cell. The 2010 Pingry S.M.A.R.T. Team is producing physical models of various AKR's that highlight the enzymes' structural and functional characteristics that are relevant to the Banta Lab's work.
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== What are S.M.A.R.T. Teams? ==
== What are S.M.A.R.T. Teams? ==
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This project was supported by Grant Number 1 R25 RR022749-01 from the National Center for Research Resources (NCRR), a component of the National Institutes of Health (NIH).
This project was supported by Grant Number 1 R25 RR022749-01 from the National Center for Research Resources (NCRR), a component of the National Institutes of Health (NIH).
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== AdhD and Self-assembly into hydrogels ==
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 +
== Modifying cofactor specificity ==
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 +
== Substrate specificity ==
=='''Reference'''==
=='''Reference'''==
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Biofuel cells
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'''Biofuel cells'''
<ref group="xtra">PMID:15669171</ref><references group="xtra"/>
<ref group="xtra">PMID:15669171</ref><references group="xtra"/>
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Aldo-keto reductases
+
<ref group="xtra">PMID:17399977</ref><references group="xtra"/>
 +
<ref group="xtra">PMID:16781864</ref><references group="xtra"/>
 +
'''Aldo-keto reductases'''
<ref group="xtra">PMID:12663943</ref><references group="xtra"/>
<ref group="xtra">PMID:12663943</ref><references group="xtra"/>
 +
'''AdhD and hydrogels'''
 +
<ref group="xtra">PMID:19577577</ref><references group="xtra"/>
 +
'''Modifying cofactor specificity, 2,5-diketo-d-gluconic acid reductase'''
 +
<ref group="xtra">PMID:9618487</ref><references group="xtra"/>
 +
<ref group="xtra">PMID:12733986</ref><references group="xtra"/>
 +
'''Innate dual-cofactor use, Rat liver 3 alpha-hydroxysteroid hidydrodiol dehydrogenase'''
 +
<ref group="xtra">PMID:9618487</ref><references group="xtra"/>
 +
<ref group="xtra">PMID:14718658</ref><references group="xtra"/>
 +
<ref group="xtra">PMID:14718658</ref><references group="xtra"/>

Revision as of 17:35, 24 December 2009

Contents

2010 Pingry S.M.A.R.T. Team-AKR's for Biofuel Cells

The 2010 Pingry School S.M.A.R.T. Team (Students Modeling A Research Topic) is working with Scott Banta at Columbia University to learn about enzymes being engineered for use in biofuel cells. Features being engineered into these enzymes include (1) self-assembly into hydrogels, (2) alternate cofactor use, and (3) broader substrate specificity. AdhD alcohol dehydrogenase from the thermophile Pyrococcus furiosus is one of the enzymes being engineered with these features by the Banta Lab. AdhD is a member of the aldo-keto reductase (AKR) family of oxidoreductases. Taking advantage of its innate thermostable properties, the Banta Lab is engineering AdhD for use in biofuel cells.

The logical design and engineering of AdhD is based partially on the solved structures of other enzymes belonging to the AKR family of enzymes. Structures of mutants that bind alternate cofactors and those bound to its substrate provide insight into how to engineer AdhD and other enzymes of use in a biofuel cell. The 2010 Pingry S.M.A.R.T. Team is producing physical models of various AKR's that highlight the enzymes' structural and functional characteristics that are relevant to the Banta Lab's work.

What are S.M.A.R.T. Teams?

"SMART Teams (Students Modeling A Research Topic) are teams of high school students and their teachers who are working with research scientists to design and construct physical models of the proteins or other molecular structures that are being investigated in their laboratories. SMART Teams use state-of-the-art molecular design software and rapid prototyping technologies to produce these unique models." -from the Center of BioMolecular Modeling Website.

This project was supported by Grant Number 1 R25 RR022749-01 from the National Center for Research Resources (NCRR), a component of the National Institutes of Health (NIH).

AdhD and Self-assembly into hydrogels

Modifying cofactor specificity

Substrate specificity

Reference

Biofuel cells

  • Barton SC, Gallaway J, Atanassov P. Enzymatic biofuel cells for implantable and microscale devices. Chem Rev. 2004 Oct;104(10):4867-86. PMID:15669171
  • Davis F, Higson SP. Biofuel cells--recent advances and applications. Biosens Bioelectron. 2007 Feb 15;22(7):1224-35. Epub 2006 Jun 16. PMID:16781864 doi:10.1016/j.bios.2006.04.029

Aldo-keto reductases

  • Sanli G, Dudley JI, Blaber M. Structural biology of the aldo-keto reductase family of enzymes: catalysis and cofactor binding. Cell Biochem Biophys. 2003;38(1):79-101. PMID:12663943 doi:10.1385/CBB:38:1:79

AdhD and hydrogels

  • Wheeldon IR, Campbell E, Banta S. A chimeric fusion protein engineered with disparate functionalities-enzymatic activity and self-assembly. J Mol Biol. 2009 Sep 11;392(1):129-42. Epub 2009 Jul 3. PMID:19577577 doi:10.1016/j.jmb.2009.06.075

Modifying cofactor specificity, 2,5-diketo-d-gluconic acid reductase

  • Khurana S, Powers DB, Anderson S, Blaber M. Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-A resolution. Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6768-73. PMID:9618487
  • Kavanagh KL, Klimacek M, Nidetzky B, Wilson DK. Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases. Biochem J. 2003 Jul 15;373(Pt 2):319-26. PMID:12733986 doi:10.1042/BJ20030286

Innate dual-cofactor use, Rat liver 3 alpha-hydroxysteroid hidydrodiol dehydrogenase

  • Khurana S, Powers DB, Anderson S, Blaber M. Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-A resolution. Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6768-73. PMID:9618487
  • Sanli G, Banta S, Anderson S, Blaber M. Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase. Protein Sci. 2004 Feb;13(2):504-12. Epub 2004 Jan 10. PMID:14718658 doi:10.1110/ps.03450704
  • Sanli G, Banta S, Anderson S, Blaber M. Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase. Protein Sci. 2004 Feb;13(2):504-12. Epub 2004 Jan 10. PMID:14718658 doi:10.1110/ps.03450704

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Tommie Hata

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