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L-ALANINE BIOSYNTHESIS IN ESCHERICHI...

WHALEN, WILLIAM ANTHONY, III.

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L-ALANINE BIOSYNTHESIS IN ESCHERICHIA COLI AND SALMONELLA TYPHIMURIUM (TRANSAMINASES, AVTA, TRANSPOSON).

Record Type:	Electronic resources : Monograph/item
Title/Author:	L-ALANINE BIOSYNTHESIS IN ESCHERICHIA COLI AND SALMONELLA TYPHIMURIUM (TRANSAMINASES, AVTA, TRANSPOSON)./
Author:	WHALEN, WILLIAM ANTHONY, III.
Description:	117 p.
Notes:	Source: Dissertation Abstracts International, Volume: 45-12, Section: B, page: 3726.
Contained By:	Dissertation Abstracts International45-12B.
Subject:	Biology, Microbiology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=8503795

L-ALANINE BIOSYNTHESIS IN ESCHERICHIA COLI AND SALMONELLA TYPHIMURIUM (TRANSAMINASES, AVTA, TRANSPOSON).
WHALEN, WILLIAM ANTHONY, III.

L-ALANINE BIOSYNTHESIS IN ESCHERICHIA COLI AND SALMONELLA TYPHIMURIUM (TRANSAMINASES, AVTA, TRANSPOSON). - 117 p.

Source: Dissertation Abstracts International, Volume: 45-12, Section: B, page: 3726.

Thesis (Ph.D.)--The University of Connecticut, 1984.

Even though L-alanine is an important primary metabolite in bacteria, little is known about its biosynthesis in any microorganism. This thesis begins the study of the biosynthesis of L-alanine in Escherichia coli and Salmonella typhimurium.Subjects--Topical Terms:

1017734
Biology, Microbiology.

L-ALANINE BIOSYNTHESIS IN ESCHERICHIA COLI AND SALMONELLA TYPHIMURIUM (TRANSAMINASES, AVTA, TRANSPOSON).
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100 1 $a WHALEN, WILLIAM ANTHONY, III. $3 1939065
245 1 0 $a L-ALANINE BIOSYNTHESIS IN ESCHERICHIA COLI AND SALMONELLA TYPHIMURIUM (TRANSAMINASES, AVTA, TRANSPOSON).
300 $a 117 p.
500 $a Source: Dissertation Abstracts International, Volume: 45-12, Section: B, page: 3726.
502 $a Thesis (Ph.D.)--The University of Connecticut, 1984.
520 $a Even though L-alanine is an important primary metabolite in bacteria, little is known about its biosynthesis in any microorganism. This thesis begins the study of the biosynthesis of L-alanine in Escherichia coli and Salmonella typhimurium.
520 $a Mutations affecting L-alanine biosynthesis were obtained by isolating valine-requiring derivatives of L-isoleucine-requiring ilvE mutants, which lack the branched-chain amino acid transaminase, transaminase B. Two classes of transposon-induced mutants were isolated in E. coli and S. typhimurium: one class of mutants (avtA) lacked TrC and had a L-valine requirement which could not be satisfied by any other amino acid, and a second class (ala) retained TrC activity and could grow on L-alanine in place of L-valine.
520 $a Neither avtA or ala mutations alone confer a growth requirement in E. coli or S. typhimurium. It is only when they are combined with other mutations that avtA- and ala-dependent growth requirements are detected. avtA mutations confer: upon ilvE mutants an L-valine requirement, upon ilvGEDA mutants of E. coli an L-leucine and pantothenate requirement, upon ilvA mutants a reduced ability to use (alpha)-aminobutyrate in place L-isoleucine, and upon ala mutants a partial L-alanine requirement. ala mutations confer: upon ilvE mutants an L-alanine or L-valine requirement, and upon avtA mutants a partial L-alanine requirement.
520 $a The ala mutations were shown to reduce alanine-glutamate transaminase activity (ALAGT) in E. coli and S. typhimurium, suggesting that this enzyme is involved in L-alanine biosynthesis. However, no mutations abolished this activity in either genus, leaving assignment of its role in L-alanine synthesis tentative. These observation suggest the L-alanine is synthesized by at least two pathways: by TrC and by ALAGT.
520 $a The regulation of synthesis of these enzymes suggests that they are regulated by two distinct regulatory pathways: TrC synthesis was repressed by L-alanine, L-leucine, and a number of nonprotein amino acids whereas ALAGT synthesis was unaffected. Also, ALAGT synthesis increased as alanyl-tRNA charging decreased whereas TrC synthesis was unaffected. The control of the levels of TrC and ALAGT by L-alanine and alanyl-tRNA suggests that these enzymes are primarily L-alanine biosynthetic enzymes.
590 $a School code: 0056.
650 4 $a Biology, Microbiology. $3 1017734
690 $a 0410
710 2 0 $a The University of Connecticut. $3 1249323
773 0 $t Dissertation Abstracts International $g 45-12B.
790 $a 0056
791 $a Ph.D.
792 $a 1984
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=8503795