Characterization of a regulatory mutant of fructose 1,6-bisphosphatase in Saccharomyces carlsbergensis

1977 ◽  
Vol 154 (1) ◽  
pp. 61-66 ◽  
Author(s):  
K. W. van de Poll ◽  
D. H. J. Schamhart
Keyword(s):  
Saccharomyces Carlsbergensis ◽  
Regulatory Mutant ◽  
Fructose 1,6 Bisphosphatase

scholarly journals Characterization of the human liver fructose-1,6-bisphosphatase gene promoter

2000 ◽  
Vol 351 (2) ◽  
pp. 385 ◽  
Author(s):  
Birger HERZOG ◽  
Mary WALTNER-LAW ◽  
Donald K. SCOTT ◽  
Klaus ESCHRICH ◽  
Daryl K. GRANNER
Keyword(s):  
Human Liver ◽  
Gene Promoter ◽  
Fructose 1,6 Bisphosphatase

Ostrich fructose-1,6-bisphosphatase: Kinetic characterization of the liver isoenzyme

1991 ◽  
Vol 23 (10) ◽  
pp. 991-995 ◽  
Author(s):  
André van Tonder ◽  
Ryno J. Naudé ◽  
Willem Oelofsen
Keyword(s):  
Kinetic Characterization ◽  
Fructose 1,6 Bisphosphatase

scholarly journals Molecular Cloning and Characterization of a cDNA Encoding Sedoheptulose-1,7-bisphosphatase from Mulberry (Morus alba var. multicaulis)

2008 ◽  
Vol 57 (1-6) ◽  
pp. 152-157 ◽  
Author(s):  
X. Ji ◽  
Y. Gai ◽  
J. Ma ◽  
C. Zheng ◽  
Z. Mu
Keyword(s):  
Morus Alba ◽  
Evolutionary Analysis ◽  
Comparison Analysis ◽  
Reading Frame ◽  
Acid Protein ◽  
Fructose 1,6 Bisphosphatase ◽  
Rapid Amplification ◽  
Molecular Evolutionary Analysis ◽  
Amino Acid Protein

Abstract A full-length cDNA encoding sedoheptulose-1,7-bisphosphatase (SBPase; EC 3.1.3.37) was cloned from mulberry (Morus alba var. multicaulis) by rapid amplification of cDNA ends (RACE). The cDNA consisted of 1,527 nucleotides with an open reading frame (ORF) of 1,179 nucleotides encoding a 393 amino acid protein of approximately 42.6 kDa. Sequence comparison analysis showed that mulberry SBPase (MSBPase) had high homology to other plant counterparts. Phylogenetic and molecular evolutionary analysis revealed that MSBPase fell into plant SBPase group. Moreover, SBPase and fructose-1,6-bisphosphatase (FBPase; EC 3.1.3.11) shared 28-32% identical residues, suggesting that the two enzymes originated from the same evolution branch. Molecular modeling indicated that each subunit of MSBPase was composed of α-helices and β-sheets joined by turns and loops, and folded into a structure of hexahedron shape which was very similar to FBPase.

Characterization of three rabbit liver lysosomal proteinases with fructose 1,6-bisphosphatase converting enzyme activity

1981 ◽  
Vol 208 (1) ◽  
pp. 175-183 ◽  
Author(s):  
E. Melloni ◽  
S. Pontremoli ◽  
F. Salamino ◽  
B. Sparatore ◽  
M. Michetti ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Rabbit Liver ◽  
Converting Enzyme ◽  
Lysosomal Proteinases ◽  
Fructose 1,6 Bisphosphatase

scholarly journals Structural and Biochemical Characterization of the Type II Fructose-1,6-bisphosphatase GlpX fromEscherichia coli

2008 ◽  
Vol 284 (6) ◽  
pp. 3784-3792 ◽  
Author(s):  
Greg Brown ◽  
Alexander Singer ◽  
Vladimir V. Lunin ◽  
Michael Proudfoot ◽  
Tatiana Skarina ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Type Ii ◽  
Fromescherichia Coli ◽  
Fructose 1,6 Bisphosphatase
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