Exemplar Abstract for Sulfolobus solfataricus Zillig et al. 1980.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
Sulfolobus Solfataricus

scholarly journals A Redox-Neutral, Two-Enzyme Cascade for the Production of Malate and Gluconate from Pyruvate and Glucose

2021 ◽  
Vol 11 (11) ◽  
pp. 4877
Author(s):  
Ravneet Mandair ◽  
Pinar Karagoz ◽  
Roslyn M. Bill
Keyword(s):  
Malate Dehydrogenase ◽  
Closed System ◽  
Glucose Dehydrogenase ◽  
Sulfolobus Solfataricus ◽  
Cofactor Regeneration ◽  
Triple Mutant ◽  
Thermococcus Kodakarensis ◽  
Platform Chemicals ◽  
Enzyme Cascade

A triple mutant of NADP(H)-dependent malate dehydrogenase from thermotolerant Thermococcus kodakarensis has an altered cofactor preference for NAD+, as well as improved malate production compared to wildtype malate dehydrogenase. By combining mutant malate dehydrogenase with glucose dehydrogenase from Sulfolobus solfataricus and NAD+/NADH in a closed reaction environment, gluconate and malate could be produced from pyruvate and glucose. After 3 h, the yield of malate was 15.96 mM. These data demonstrate the feasibility of a closed system capable of cofactor regeneration in the production of platform chemicals.

scholarly journals Identification of a serine/threonine-specific protein phosphatase from the archaebacterium Sulfolobus solfataricus.

1993 ◽  
Vol 268 (9) ◽  
pp. 6505-6510
Author(s):  
P.J. Kennelly ◽  
K.A. Oxenrider ◽  
J. Leng ◽  
J.S. Cantwell ◽  
N. Zhao
Keyword(s):  
Protein Phosphatase ◽  
Sulfolobus Solfataricus ◽  
Specific Protein

scholarly journals Open Reading Frame sso2387 from the Archaeon Sulfolobus solfataricus Encodes a Polypeptide with Protein-Serine Kinase Activity

2003 ◽  
Vol 185 (11) ◽  
pp. 3436-3445 ◽  
Author(s):  
Brian H. Lower ◽  
Peter J. Kennelly
Keyword(s):  
Protein Kinases ◽  
Catalytic Domain ◽  
Sulfolobus Solfataricus ◽  
Open Reading Frame ◽  
Serine Kinase ◽  
Eukaryotic Protein Kinase ◽  
Reading Frame ◽  
Eukaryotic Protein ◽  
High Concentrations ◽  
Eukaryotic Protein Kinases

ABSTRACT The predicted polypeptide product of open reading frame sso2387 from the archaeon Sulfolobus solfataricus, SsoPK2, displayed several of the sequence features conserved among the members of the “eukaryotic” protein kinase superfamily. sso2387 was cloned, and its polypeptide product was expressed in Escherichia coli. The recombinant protein, rSsoPK2, was recovered in insoluble aggregates that could be dispersed by using high concentrations (5 M) of urea. The solubilized polypeptide displayed the ability to phosphorylate itself as well as several exogenous proteins, including mixed histones, casein, bovine serum albumin, and reduced carboxyamidomethylated and maleylated lysozyme, on serine residues. The source of this activity resided in that portion of the protein displaying homology to the catalytic domain of eukaryotic protein kinases. By use of mass spectrometry, the sites of autophosphorylation were found to be located in two areas, one immediately N terminal to the region corresponding to subdomain I of eukaryotic protein kinases, and the second N terminal to the presumed activation loop located between subdomains VII and VIII. Autophosphorylation of rSsoPK2 could be uncoupled from the phosphorylation of exogenous proteins by manipulation of the temperature or mutagenic alteration of the enzyme. Autophosphorylation was detected only at temperatures ≥60°C, whereas phosphorylation of exogenous proteins was detectable at 37°C. Similarly, replacement of one of the potential sites of autophosphorylation, Ser548, with alanine blocked autophosphorylation but not phosphorylation of an exogenous protein, casein.

scholarly journals Identification of a novel NADH-specific aldo-keto reductase using sequence and structural homologies

2006 ◽  
Vol 400 (1) ◽  
pp. 105-114 ◽  
Author(s):  
Eric Di Luccio ◽  
Robert A. Elling ◽  
David K. Wilson
Keyword(s):  
Escherichia Coli ◽  
Sinorhizobium Meliloti ◽  
Thermotoga Maritima ◽  
Xylose Reductase ◽  
Sulfolobus Solfataricus ◽  
Sequence Comparisons ◽  
E Coli ◽  
Fluorescence Measurements ◽  
Dual Specificity ◽  
Substrate Dependence

The AKRs (aldo-keto reductases) are a superfamily of enzymes which mainly rely on NADPH to reversibly reduce various carbonyl-containing compounds to the corresponding alcohols. A small number have been found with dual NADPH/NADH specificity, usually preferring NADPH, but none are exclusive for NADH. Crystal structures of the dual-specificity enzyme xylose reductase (AKR2B5) indicate that NAD+ is bound via a key interaction with a glutamate that is able to change conformations to accommodate the 2′-phosphate of NADP+. Sequence comparisons suggest that analogous glutamate or aspartate residues may function in other AKRs to allow NADH utilization. Based on this, nine putative enzymes with potential NADH specificity were identified and seven genes were successfully expressed and purified from Drosophila melanogaster, Escherichia coli, Schizosaccharomyces pombe, Sulfolobus solfataricus, Sinorhizobium meliloti and Thermotoga maritima. Each was assayed for co-substrate dependence with conventional AKR substrates. Three were exclusive for NADPH (AKR2E3, AKR3F2 and AKR3F3), two were dual-specific (AKR3C2 and AKR3F1) and one was specific for NADH (AKR11B2), the first such activity in an AKR. Fluorescence measurements of the seventh protein indicated that it bound both NADPH and NADH but had no activity. Mutation of the aspartate into an alanine residue or a more mobile glutamate in the NADH-specific E. coli protein converted it into an enzyme with dual specificity. These results show that the presence of this carboxylate is an indication of NADH dependence. This should allow improved prediction of co-substrate specificity and provide a basis for engineering enzymes with altered co-substrate utilization for this class of enzymes.

Two glycolytic enzymes from Sulfolobus solfataricus

1998 ◽  
Vol 26 (3) ◽  
pp. S275-S275 ◽  
Author(s):  
G. S. E. Crowhurst ◽  
M. N. Isupov ◽  
T. Fleming ◽  
J. A. Littlechild
Keyword(s):  
Sulfolobus Solfataricus ◽  
Glycolytic Enzymes
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