Metabolic Engineering of the Tricarboxylic Acid Cycle for Improved Lysine Production by Corynebacterium glutamicum

被引：89

作者：

Becker, Judith ^{[1
]}

Klopprogge, Corinna ^{[2
]}

Schroeder, Hartwig ^{[2
]}

Wittmann, Christoph ^{[1
]}

机构：

[1] Tech Univ Carolo Wilhelmina Braunschweig, Inst Biochem Engn, D-38106 Braunschweig, Germany

[2] BASF SE, Res Fine Chem & Biotechnol, Ludwigshafen, Germany

来源：

APPLIED AND ENVIRONMENTAL MICROBIOLOGY | 2009年 / 75卷 / 24期

关键词：

IN-VIVO; STRAIN IMPROVEMENT; FLUX; EXPRESSION; ASPARTOKINASE; DEHYDROGENASE; BIOSYNTHESIS; FRUCTOSE; PATHWAY; LEADS;

D O I：

10.1128/AEM.01942-09

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

In the present work, lysine production by Corynebacterium glutamicum was improved by metabolic engineering of the tricarboxylic acid (TCA) cycle. The 70% decreased activity of isocitrate dehydrogenase, achieved by start codon exchange, resulted in a > 40% improved lysine production. By flux analysis, this could be correlated to a flux shift from the TCA cycle toward anaplerotic carboxylation.

引用

页码：7866 / 7869

页数：4

共 22 条

[1] Amplified expression of fructose 1,6-bisphosphatase in Corynebacterium glutamicum increases in vivo flux through the pentose phosphate pathway and lysine production on different carbon sources [J].

Becker, J ;

Klopprogge, C ;

Zelder, O ;

Heinzle, E ;

Wittmann, C .

APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2005, 71 (12) :8587-8596

[2] Metabolic flux engineering of L-lysine production in Corynebacterium glutamicum -: over expression and modification of G6P dehydrogenase [J].

Becker, Judith ;

Klopprogge, Corinna ;

Herold, Andrea ;

Zelder, Oskar ;

Bolten, Christoph J. ;

Wittmann, Christoph .

JOURNAL OF BIOTECHNOLOGY, 2007, 132 (02) :99-109

[3] Metabolic responses to pyruvate kinase deletion in lysine producing Corynebacterium glutamicum [J].

Becker, Judith ;

Klopprogge, Corinna ;

Wittmann, Christoph .

MICROBIAL CELL FACTORIES, 2008, 7 (1)

[4]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[5] Improved L-lysine yield with Corynebacterium glutamicum:: use of dapA resulting in increased flux combined with growth limitation [J].

Eggeling, L ;

Oberle, S ;

Sahm, H .

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 1998, 49 (01) :24-30

[6]

Eikmanns B. J., 2005, Handbook of Corynebacterium glutamicum, P241

[7] CLONING, SEQUENCE-ANALYSIS, EXPRESSION, AND INACTIVATION OF THE CORYNEBACTERIUM-GLUTAMICUM-ICD GENE ENCODING ISOCITRATE DEHYDROGENASE AND BIOCHEMICAL-CHARACTERIZATION OF THE ENZYME [J].

EIKMANNS, BJ ;

RITTMANN, D ;

SAHM, H .

JOURNAL OF BACTERIOLOGY, 1995, 177 (03) :774-782

[8] Identification and characterization of the last two unknown genes, dapC and dapF, in the succinylase branch of the L-lysine biosynthesis of Corynebacterium glutamicum [J].

Hartmann, M ;

Tauch, A ;

Eggeling, L ;

Bathe, B ;

Möckel, B ;

Pühler, A ;

Kalinowski, J .

JOURNAL OF BIOTECHNOLOGY, 2003, 104 (1-3) :199-211

[9]

JAGER W, 1992, J BACTERIOL, V174, P5462

[10] GENETIC AND BIOCHEMICAL-ANALYSIS OF THE ASPARTOKINASE FROM CORYNEBACTERIUM-GLUTAMICUM [J].

KALINOWSKI, J ;

CREMER, J ;

BACHMANN, B ;

EGGELING, L ;

SAHM, H ;

PUHLER, A .

MOLECULAR MICROBIOLOGY, 1991, 5 (05) :1197-1204

← 1 2 3 →