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New metal containing enzymes and fun...

Kish, Michelle Marie.

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New metal containing enzymes and fundamental studies in biological mass spectrometry.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	New metal containing enzymes and fundamental studies in biological mass spectrometry./
作者:	Kish, Michelle Marie.
面頁冊數:	110 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1224.
Contained By:	Dissertation Abstracts International64-03B.
標題:	Chemistry, Analytical. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3083399

New metal containing enzymes and fundamental studies in biological mass spectrometry.
Kish, Michelle Marie.

New metal containing enzymes and fundamental studies in biological mass spectrometry. - 110 p.

Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1224.

Thesis (Ph.D.)--The University of Akron, 2003.

This dissertation explores protein engineering, a method used to create a new metal ion-binding site into the existing enzyme malate dehydrogenase, thus altering its native catalytic activity. This enzyme does not require a metal ion to catalyze the oxidation of malate to oxaloacetate. The metal ion was introduced to provide a new catalytic activity, the decarboxylation of malate to pyruvate and carbon dioxide. Mutations were made to incorporate a metal binding site that consisted of two histidines and one glutamic acid. Both the native and new catalytic activities were measured.Subjects--Topical Terms:

586156
Chemistry, Analytical.

New metal containing enzymes and fundamental studies in biological mass spectrometry.
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245 1 0 $a New metal containing enzymes and fundamental studies in biological mass spectrometry.
300 $a 110 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-03, Section: B, page: 1224.
500 $a Adviser: Chrys Wesdemiotis.
502 $a Thesis (Ph.D.)--The University of Akron, 2003.
520 $a This dissertation explores protein engineering, a method used to create a new metal ion-binding site into the existing enzyme malate dehydrogenase, thus altering its native catalytic activity. This enzyme does not require a metal ion to catalyze the oxidation of malate to oxaloacetate. The metal ion was introduced to provide a new catalytic activity, the decarboxylation of malate to pyruvate and carbon dioxide. Mutations were made to incorporate a metal binding site that consisted of two histidines and one glutamic acid. Both the native and new catalytic activities were measured.
520 $a Tandem mass spectrometry techniques were applied to study the intrinsic chemistry of a variety of biomolecules in this dissertation. Sodium bound dimers of amino acids and GlyGly with amino acids were produced in the gas phase by electrospray ionization (ESI). The dissociation kinetics of these AA<sub>1</sub>-Na<super>+</super>-AA<sub>2</sub> and GlyGly-Na<super>+</super>-AA ions were determined by collisionally activated dissociation (CAD) and converted to relative Na<super>+</super> affinities via the kinetic method. The Na<super> +</super> binding energies of the reference bases and of representative aliphatic and side-chain functionalized amino acids were determined by ab initio theory. The data showed that functional side chains increased the AA-Na<super>+</super> bond strength by providing an extra ligand to the metal ion. Ab initio calculations were also performed to determine the types of bonding present in the complex GlyGly-Na<super>+</super>.
520 $a The proton, lithium, sodium, potassium and silver ion (Cat<super>+</super>) adducts of the peptides GGKAA and SIKVAV were formed by ESI and the unimolecular chemistry of these ions was examined by low-energy CAD in the mass spectrometer. Comparing the fragmentation of [GGKAA+Cat]<super>+</super> and [SIKVAV+Cat]<super></super>+ to [YGGFL+Cat]<super>+</super> revealed that an internal lysine enhanced the cleavage of the amide bond in C-terminal position (i.e. Lys-Xxx) because of involvement of the amine group of the lysine side chain in this reaction. [PTHIKWGD+Cat]<super>+</super> further showed that, when both His and Lys residues are present internally, Lys-Xxx bonds were cleaved more selectively than His-Xxx bonds if Cat = Na (or Li), whereas both these bonds break with competitive rates if Cat = Ag. The enhanced dissociation of Lys-Xxx bonds should be useful in the sequence analysis of non-tryptic as well as incomplete tryptic digests.
590 $a School code: 0003.
650 4 $a Chemistry, Analytical. $3 586156
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0486
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710 2 0 $a The University of Akron. $3 1018399
773 0 $t Dissertation Abstracts International $g 64-03B.
790 1 0 $a Wesdemiotis, Chrys, $e advisor
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791 $a Ph.D.
792 $a 2003
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