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Structural studies of three NAD(P)H-...

Kavanagh, Kathryn Louise.

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Structural studies of three NAD(P)H-dependent enzymes involved in sugar metabolism: Mannitol dehydrogenase, xylose reductase, and lactate dehydrogenase.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Structural studies of three NAD(P)H-dependent enzymes involved in sugar metabolism: Mannitol dehydrogenase, xylose reductase, and lactate dehydrogenase./
Author:	Kavanagh, Kathryn Louise.
Description:	138 p.
Notes:	Source: Dissertation Abstracts International, Volume: 64-07, Section: B, page: 3259.
Contained By:	Dissertation Abstracts International64-07B.
Subject:	Chemistry, Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3097439

Structural studies of three NAD(P)H-dependent enzymes involved in sugar metabolism: Mannitol dehydrogenase, xylose reductase, and lactate dehydrogenase.
Kavanagh, Kathryn Louise.

Structural studies of three NAD(P)H-dependent enzymes involved in sugar metabolism: Mannitol dehydrogenase, xylose reductase, and lactate dehydrogenase. - 138 p.

Source: Dissertation Abstracts International, Volume: 64-07, Section: B, page: 3259.

Thesis (Ph.D.)--University of California, Davis, 2003.

NAD(P)H-dependent oxidoreductases are important in all forms of metabolism. Sugar- and polyalcohol-specific dehydrogenase/reductases present good systems to study since their roles are well established. Despite the wealth of knowledge concerning NAD(P)H-dependent oxidoreductases, significant gaps exist in many areas. This work investigates catalytic mechanisms, features that confer specificity for cofactors and substrates, and molecular evolution in three enzymes. These enzymes have applications in medical diagnostics, chiral synthesis, biotechnology, and structure-assisted drug design.Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Structural studies of three NAD(P)H-dependent enzymes involved in sugar metabolism: Mannitol dehydrogenase, xylose reductase, and lactate dehydrogenase.
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035 $a (UnM)AAI3097439
035 $a AAI3097439
040 $a UnM $c UnM
100 1 $a Kavanagh, Kathryn Louise. $3 1946061
245 1 0 $a Structural studies of three NAD(P)H-dependent enzymes involved in sugar metabolism: Mannitol dehydrogenase, xylose reductase, and lactate dehydrogenase.
300 $a 138 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-07, Section: B, page: 3259.
500 $a Adviser: David K. Wilson.
502 $a Thesis (Ph.D.)--University of California, Davis, 2003.
520 $a NAD(P)H-dependent oxidoreductases are important in all forms of metabolism. Sugar- and polyalcohol-specific dehydrogenase/reductases present good systems to study since their roles are well established. Despite the wealth of knowledge concerning NAD(P)H-dependent oxidoreductases, significant gaps exist in many areas. This work investigates catalytic mechanisms, features that confer specificity for cofactors and substrates, and molecular evolution in three enzymes. These enzymes have applications in medical diagnostics, chiral synthesis, biotechnology, and structure-assisted drug design.
520 $a <italic>Pseudomonas fluorescens</italic> mannitol 2-dehydrogenase (pfMDH), a secondary alcohol dehydrogenase, is the first member of the long-chain mannitol dehydrogenase family to be structurally characterized. pfMDH provides remarkable examples of both convergent and divergent evolution. The N-terminal domain includes a Rossmann fold and is involved in NAD<super>+</super> binding while the C-terminal domain is primarily α-helical and promotes mannitol binding and catalysis. The reaction likely proceeds through an alkoxide intermediate whereby a lysine general base is assisted by two asparagines which precisely An unusual proton-transfer mechanism may return the lysine to its uncharged state.
520 $a The crystallographic study of <italic>Candida tenuis</italic> xylose reductase (ctXR) describes the structure of a family 2 aldo-keto reductase (AKR). Family 2 members are unusual in that many are homodimeric and efficiently utilize NADH in addition to NADPH. The (β/α)<sub>8</sub>-barrel monomers associate side-to-side via a highly-hydrated dimeric interface that may be required for protein stability. Apparently crucial for efficient NADH utilization is ctXR's ability to change the conformation of two loops as well as the presence of Glu227 on one of these loops. Residues that may be changed to improve biotechnological applications for the conversion of biomass into ethanol are delineated.
520 $a X-ray crystal structures of <italic>Toxoplasma gondii</italic> tachyzoite stage lactate dehydrogenase (LDH1) reveal active-site differences between parasitic and human isozymes. These amino-acid substitutions increase the hydrophobicity of LDH1's active site. As lactate dehydrogenase is necessary for growth of the parasite within human hosts, it presents an attractive target for drug design. The Met163 side chain displaces a conserved water molecule providing a structural explanation for the reduced substrate inhibition and increased catalytic efficiency with APAD<super>+</super> observed in LDH1.
590 $a School code: 0029.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biophysics, General. $3 1019105
690 $a 0487
690 $a 0307
690 $a 0786
710 2 0 $a University of California, Davis. $3 1018682
773 0 $t Dissertation Abstracts International $g 64-07B.
790 1 0 $a Wilson, David K., $e advisor
790 $a 0029
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3097439