Mitochondrial Phosphate Transport Protein. Replacements of Glutamic, Aspartic, and Histidine Residues Affect Transport and Protein Conformation and Point to a Coupled Proton Transport Path†

Biochemistry ◽  
1996 ◽  
Vol 35 (33) ◽  
pp. 10757-10762 ◽  
Author(s):  
Anne Phelps ◽  
Christine Briggs ◽  
Leesa Mincone ◽  
Hartmut Wohlrab
Keyword(s):  
Protein Conformation ◽  
Proton Transport ◽  
Phosphate Transport ◽  
Transport Protein ◽  
Histidine Residues ◽  
Transport Path

High specificity of a phosphate transport protein determined by hydrogen bonds

Nature ◽  
1990 ◽  
Vol 347 (6291) ◽  
pp. 402-406 ◽  
Author(s):  
Hartmut Luecke ◽  
Florante A. Quiocho
Keyword(s):  
Hydrogen Bonds ◽  
High Specificity ◽  
Phosphate Transport ◽  
Transport Protein

scholarly journals Analysis of human hepatic microsomal glucose-6-phosphatase in clinical conditions where the T2 pyrophosphate/phosphate transport protein is absent

1992 ◽  
Vol 281 (3) ◽  
pp. 859-863 ◽  
Author(s):  
R C Nordlie ◽  
H M Scott ◽  
I D Waddell ◽  
R Hume ◽  
A Burchell
Keyword(s):  
Endoplasmic Reticulum ◽  
Transport System ◽  
Phosphate Transport ◽  
Transport Protein ◽  
Hepatic Microsomes ◽  
Phosphatase System ◽  
Pyrophosphatase Activity ◽  
Protein Components ◽  
Clinical Conditions

The availability of a rare set of human hepatic microsomes in which T2, a pyrophosphate/phosphate transport protein of the glucose-6-phosphatase system, has been shown immunologically to be completely absent, has permitted further characterization of multicomponent glucose-6-phosphatase (EC 3.1.3.9). Pyrophosphatase activity in intact microsomes was found to be totally absent, but was normal in disrupted microsomes. However, Pi did not accumulate within the lumen of the microsomes when glucose 6-phosphate was the substrate. This was not as predicted if there is only one transport protein in the endoplasmic reticulum capable of transporting Pi, produced by glucose-6-phosphatase, out of the lumen. The results suggest that the pyrophosphate/phosphate transport system of human hepatic endoplasmic reticulum must be more complex than previously thought, as it must comprise at least two protein components.

Molecular Cloning of the cDNA Encoding a Human Renal Sodium Phosphate Transport Protein and Its Assignment to Chromosome 6p21.3-p23

Genomics ◽  
1993 ◽  
Vol 18 (2) ◽  
pp. 355-359 ◽  
Author(s):  
Samuel S. Chong ◽  
Kristleifur Kristjansson ◽  
Huda Y. Zoghbi ◽  
Mark R. Hughes
Keyword(s):  
Molecular Cloning ◽  
Sodium Phosphate ◽  
Phosphate Transport ◽  
Transport Protein ◽  
Chromosome 6P21.3

Purified mitochondrial phosphate-transport protein. Improved proteoliposomes and some properties of the transport protein sulfhydryl group(s)

Biochemistry ◽  
1984 ◽  
Vol 23 (6) ◽  
pp. 1057-1064 ◽  
Author(s):  
Hartmut Wohlrab ◽  
Anne Collins ◽  
Diane Costello ◽  
Kinichi Tsunoda
Keyword(s):  
Sulfhydryl Group ◽  
Phosphate Transport ◽  
Transport Protein ◽  
Protein Sulfhydryl
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