The semi-phosphorylative Entner-Doudoroff pathway in hyperthermophilic archaea: a re-evaluation

被引:102
作者
Ahmed, H
Ettema, TJG
Tjaden, B
Geerling, ACM
van der Oost, J
Siebers, B
机构
[1] Univ Duisburg Essen, Dept Microbiol, D-45117 Essen, Germany
[2] Univ Wageningen & Res Ctr, Microbiol Lab, NL-6703 CT Wageningen, Netherlands
关键词
carbohydrate metabolism; Entner-Doudoroff pathway; gluconate dehydratase; hyperthermophilic archaea; 2-keto-3-deoxygluconate (KDG); phosphorylation;
D O I
10.1042/BJ20041711
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Biochemical studies have suggested that, in hyperthermophilic archaea, the metabolic conversion of glucose via the ED (Entner-Doudoroff) pathway generally proceeds via a non-phosphorylative variant. A key enzyme of the non-phosphorylating ED pathway of Sulfolobus solfataricus, KDG (2-keto-3-deoxygluconate) aldolase, has been cloned and characterized previously. In the present study, a comparative genomics analysis is described that reveals conserved ED gene clusters in both Thermoproteus tenax and S. solfataricus. The corresponding ED proteins from both archaea, have been expressed in Escherichia coli and their specificity has been identified, revealing: (i) a novel type of gluconate dehydratase (gad gene), (ii) a bifunctional 2-keto-3-deoxy-(6phospho)-gluconate aldolase (kdgA gene), (iii) a 2-keto-3-deoxy-gluconate kinase (kdgK gene) and, in S. solfataricus, (iv) a GAPN (non-phosphorylating glyceral dehyde-3-phosphate dehydrogenarse; gapN gene). Extensive in vivo and in vitro enzymatic analyses indicate the operation of both the semi-phosphorylative and the non-phosphorylative ED pathway in T tenax and S. solfataricus. The existence of this branched ED pathway is yet another example of the versatility and flexibility of the central carbohydrate metabolic pathways in the archaeal domain.
引用
收藏
页码:529 / 540
页数:12
相关论文
共 52 条
[1]  
AHMED H, 2004, BIOCHEM SOC T, V32, P2
[2]   OCCURRENCE OF A MODIFIED ENTNER-DOUDOROFF PATHWAY IN CLOSTRIDIUM ACETICUM [J].
ANDREESEN, JR ;
GOTTSCHALK, G .
ARCHIV FUR MIKROBIOLOGIE, 1969, 69 (02) :160-+
[3]   The enolase superfamily: A general strategy for enzyme-catalyzed abstraction of the alpha-protons of carboxylic acids [J].
Babbitt, PC ;
Hasson, MS ;
Wedekind, JE ;
Palmer, DRJ ;
Barrett, WC ;
Reed, GH ;
Rayment, I ;
Ringe, D ;
Kenyon, GL ;
Gerlt, JA .
BIOCHEMISTRY, 1996, 35 (51) :16489-16501
[4]   Understanding enzyme superfamilies - Chemistry as the fundamental determinant in the evolution of new catalytic activities [J].
Babbitt, PC ;
Gerlt, JA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (49) :30591-30594
[5]   PURIFICATION AND PROPERTIES OF D-GLUCONATE DEHYDRATASE FROM CLOSTRIDIUM-PASTEURIANUM [J].
BENDER, R ;
GOTTSCHA.G .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1973, 40 (01) :309-321
[6]   ENZYMATIC-SYNTHESIS OF 2-KETO-3-DEOXY-D-GLUCONATE FROM D-GLUCONATE [J].
BENDER, R ;
GOTTSCHALK, G .
ANALYTICAL BIOCHEMISTRY, 1974, 61 (01) :275-279
[7]  
BORK P, 1993, PROTEIN SCI, V2, P31
[8]   The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine biosynthesis in response to lysine availability [J].
Brinkman, AB ;
Bell, SD ;
Lebbink, RJ ;
de Vos, WM ;
van der Oost, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (33) :29537-29549
[9]   NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax -: The first identified archaeal, member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties [J].
Brunner, NA ;
Brinkmann, H ;
Siebers, B ;
Hensel, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (11) :6149-6156
[10]   Role of two different glyceraldehyde-3-phosphate dehydrogenases in controlling the reversible Embden-Meyerhof-Parnas pathway in Thermoproteus tenax:: regulation on protein and transcript level [J].
Brunner, NA ;
Siebers, B ;
Hensel, R .
EXTREMOPHILES, 2001, 5 (02) :101-109