scholarly journals From Suicide Enzyme to Catalyst: The Iron-Dependent Sulfide Transfer in Methanococcus jannaschii Thiamin Thiazole Biosynthesis

2016 ◽  
Vol 138 (11) ◽  
pp. 3639-3642 ◽  
Author(s):  
Bekir E. Eser ◽  
Xuan Zhang ◽  
Prem K. Chanani ◽  
Tadhg P. Begley ◽  
Steven E. Ealick
Keyword(s):  
Methanococcus Jannaschii

scholarly journals Identification of the Gene Encoding Sulfopyruvate Decarboxylase, an Enzyme Involved in Biosynthesis of Coenzyme M

2000 ◽  
Vol 182 (17) ◽  
pp. 4862-4867 ◽  
Author(s):  
Marion Graupner ◽  
Huimin Xu ◽  
Robert H. White
Keyword(s):  
Escherichia Coli ◽  
Second Step ◽  
Gene Products ◽  
Methanococcus Jannaschii ◽  
Coenzyme M ◽  
Gene Encoding ◽  
Fourth Step

ABSTRACT The products of two adjacent genes in the chromosome ofMethanococcus jannaschii are similar to the amino and carboxyl halves of phosphonopyruvate decarboxylase, the enzyme that catalyzes the second step of fosfomycin biosynthesis inStreptomyces wedmorensis. These two M. jannaschii genes were recombinantly expressed inEscherichia coli, and their gene products were tested for the ability to catalyze the decarboxylation of a series of α-ketoacids. Both subunits are required to form an α6β6 dodecamer that specifically catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde. This transformation is the fourth step in the biosynthesis of coenzyme M, a crucial cofactor in methanogenesis and aliphatic alkene metabolism. The M. jannaschiisulfopyruvate decarboxylase was found to be inactivated by oxygen and reactivated by reduction with dithionite. The two subunits, designated ComD and ComE, comprise the first enzyme for the biosynthesis of coenzyme M to be described.

scholarly journals Crystals of ribosomal protein L1 from a hyperthermophilic archaeon Methanococcus jannaschii

IUBMB Life ◽  
1998 ◽  
Vol 45 (2) ◽  
pp. 349-354
Author(s):  
Svetlana Tishchenko ◽  
Stanislav Nikonov ◽  
Maria Garber ◽  
Alex Kraft ◽  
Caroline Köhrer ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Methanococcus Jannaschii ◽  
Hyperthermophilic Archaeon ◽  
Ribosomal Protein L1

Isolation of a complete A1AO ATP synthase comprising nine subunits from the hyperthermophile Methanococcus jannaschii

Extremophiles ◽  
2003 ◽  
Vol 7 (3) ◽  
pp. 249-257 ◽  
Author(s):  
Astrid Lingl ◽  
Harald Huber ◽  
Karl O. Stetter ◽  
Frank Mayer ◽  
Josef Kellermann ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Methanococcus Jannaschii ◽  
A1ao Atp Synthase

scholarly journals Cation Selectivity of Cora Divalent Transporter from Methanococcus Jannaschii

2012 ◽  
Vol 102 (3) ◽  
pp. 522a
Author(s):  
Albert Guskov ◽  
Nurhuda Nordin ◽  
Aline Reynaud ◽  
Said Eshaghi
Keyword(s):  
Methanococcus Jannaschii ◽  
Cation Selectivity

scholarly journals Small heat shock protein of Methanococcus jannaschii, a hyperthermophile

1998 ◽  
Vol 95 (16) ◽  
pp. 9129-9133 ◽  
Author(s):  
Rosalind Kim ◽  
Kyeong Kyu Kim ◽  
Hisao Yokota ◽  
Sung-Hou Kim
Keyword(s):  
Heat Shock ◽  
Citrate Synthase ◽  
Thermal Protection ◽  
Small Heat Shock Protein ◽  
Methanococcus Jannaschii ◽  
Single Chain ◽  
Cell Extracts ◽  
Electron Microscopy Analysis ◽  
Shock Proteins

Small heat shock proteins (sHSPs) belong to a family of 12- to 43-kDa proteins that are ubiquitous and are conserved in amino acid sequence among all organisms. A sHSP homologue of Methanococcus jannaschii, a hyperthermophilic Archaeon, forms a homogeneous multimer comprised of 24 monomers with a molecular mass of 400 kDa in contrast to other sHSPs that show heterogeneous oligomeric complexes. Electron microscopy analysis revealed a spherically shaped oligomeric structure ≈15–20 nm in diameter. The protein confers thermal protection of other proteins in vitro as found in other sHSPs. Escherichia coli cell extracts containing the protein were protected from heat-denatured precipitation when heated up to 100°C, whereas extracts from cells not expressing the protein were heat-sensitive at 60°C. Similar results were obtained when purified sHSP protein was added to an E. coli cell lysate. The protein also prevented the aggregation of two purified proteins: single-chain monellin (SCM) at 80°C and citrate synthase at 40°C.

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