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Investigations of substrate channeli...

Sanyal, Nikhilesh.

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Investigations of substrate channeling in the proline oxidative pathway.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Investigations of substrate channeling in the proline oxidative pathway./
作者:	Sanyal, Nikhilesh.
面頁冊數:	131 p.
附註:	Source: Dissertation Abstracts International, Volume: 74-08(E), Section: B.
Contained By:	Dissertation Abstracts International74-08B(E).
標題:	Chemistry, Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3559518
ISBN:	9781303046353

Investigations of substrate channeling in the proline oxidative pathway.
Sanyal, Nikhilesh.

Investigations of substrate channeling in the proline oxidative pathway. - 131 p.

Source: Dissertation Abstracts International, Volume: 74-08(E), Section: B.

Thesis (Ph.D.)--The University of Nebraska - Lincoln, 2013.

In cell metabolism, substrate channeling is a phenomenon where the product of one reaction is transported to a second enzyme active site without equilibrating into bulk solvent. Chapter 1 reviews the rationale and evidence for substrate channeling with the specific example of proline metabolism. Oxidation of proline to glutamate is catalyzed in consecutive reactions by proline dehydrogenase (PRODH) and pyrroline-5-carboxylate dehydrogenase (P5CDH). The intermediate Delta1-pyrroline-5-carboxylate reportedly tends to be labile and inhibitory towards several metabolic pathways.

ISBN: 9781303046353Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Investigations of substrate channeling in the proline oxidative pathway.
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100 1 $a Sanyal, Nikhilesh. $3 2100427
245 1 0 $a Investigations of substrate channeling in the proline oxidative pathway.
300 $a 131 p.
500 $a Source: Dissertation Abstracts International, Volume: 74-08(E), Section: B.
500 $a Adviser: Donald F. Becker.
502 $a Thesis (Ph.D.)--The University of Nebraska - Lincoln, 2013.
520 $a In cell metabolism, substrate channeling is a phenomenon where the product of one reaction is transported to a second enzyme active site without equilibrating into bulk solvent. Chapter 1 reviews the rationale and evidence for substrate channeling with the specific example of proline metabolism. Oxidation of proline to glutamate is catalyzed in consecutive reactions by proline dehydrogenase (PRODH) and pyrroline-5-carboxylate dehydrogenase (P5CDH). The intermediate Delta1-pyrroline-5-carboxylate reportedly tends to be labile and inhibitory towards several metabolic pathways.
520 $a One of the main objectives of this dissertation was to investigate substrate channeling between independent proline oxidative enzymes from Thermus thermophilus-TtPRODH and TtP5CDH. Chapter 2 establishes that TtPRODH and TtP5CDH are capable of interacting with a dissociation constant ( KD) of 3.03 muM as demonstrated using Surface Plasmon Resonance (SPR). As observed in the present study, this interaction is possible only with a specific orientation of TtPRODH relative to TtP5CDH. A docking model of the two enzymes predicts an orientation of the active sites which is supportive of substrate channeling. Corroborating observations are made with kinetic studies. We observe that interference of TtPRODH-TtP5CDH complex by catalytically inactive mutants TtPRODH R288M/R289M and TtP5CDH C322A lead to significant decrease in glutamate formation. The results pave the way for testing substrate channeling in eukaryotic enzymes. In chapter 3, two novel eukaryotic enzymes from Saccharomyces cerevisiae, Put1p (PRODH) and Put2p (P5CDH), have been characterized. Particular attention was focused on the oxidative half-reaction of Put1p for gaining insight into possible redox functions of human PRODH.
520 $a Previous studies show that bifunctional enzyme from Gram-negative Bradyrhizobium japonicum (BjPutA) containing PRODH and P5CDH domains, exhibits substrate channeling via an elegant internal tunnel. BjPutA and its channeling variants were used to test the role of substrate channel in hydrolysis of P5C, an essential step in proline oxidation. These aspects of substrate channeling are discussed in chapter 4.
520 $a Overall, this study provides an improved understanding of: (1) Substrate channeling in proline oxidation; and (2) a model for investigating substrate channeling between other individual enzymes that catalyze consecutive reactions.
590 $a School code: 0138.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biophysics, General. $3 1019105
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710 2 $a The University of Nebraska - Lincoln. $b Biochemistry. $3 1282272
773 0 $t Dissertation Abstracts International $g 74-08B(E).
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791 $a Ph.D.
792 $a 2013
793 $a English
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