Physiologic roles of soluble pyridine nucleotide transhydrogenase inEscherichia coli as determined by homologous recombination

2008 ◽  
Vol 58 (2) ◽  
pp. 275-280 ◽  
Author(s):  
Hanjun Zhao ◽  
Peng Wang ◽  
Enqi Huang ◽  
Yadong Ge ◽  
Guoping Zhu
Keyword(s):  
Homologous Recombination ◽  
Pyridine Nucleotide ◽  
Inescherichia Coli ◽  
Pyridine Nucleotide Transhydrogenase

scholarly journals PYRIDINE NUCLEOTIDE TRANSHYDROGENASE

1953 ◽  
Vol 205 (1) ◽  
pp. 1-15 ◽  
Author(s):  
Nathan O. Kaplan ◽  
Sidney P. Colowick ◽  
Elizabeth F. Neufeld
Keyword(s):  
Pyridine Nucleotide ◽  
Pyridine Nucleotide Transhydrogenase

scholarly journals PYRIDINE NUCLEOTIDE TRANSHYDROGENASE

1952 ◽  
Vol 195 (1) ◽  
pp. 107-119 ◽  
Author(s):  
Nathan O. Kaplan ◽  
Sidney P. Colowick ◽  
Elizabeth F. Neufeld
Keyword(s):  
Pyridine Nucleotide ◽  
Pyridine Nucleotide Transhydrogenase

Pyridine–Adenine Dinucleotide Transhydrogenase Activity in Cells Cultured from Rat Hepatoma

1972 ◽  
Vol 50 (5) ◽  
pp. 447-456 ◽  
Author(s):  
C. De Luca ◽  
R. P. Gioeli
Keyword(s):  
Phosphate Buffer ◽  
Pyridine Nucleotide ◽  
Maximum Activity ◽  
Ph Optimum ◽  
Apparent Lack ◽  
Minimal Deviation ◽  
Ph Range ◽  
Pyridine Nucleotide Transhydrogenase ◽  
Rat Hepatoma ◽  
Cells Cultured

Preparations from cells cultured from a minimal-deviation hepatoma in the rat exhibit pyridine nucleotide transhydrogenase (NAD(P)H: NAD(P) oxidoreductase, EC 1.6.1.1) activity. The pH optimum, its release by digitonin, and its apparent lack of dependence on steroids for activity tentatively classify it as a transhydrogenase of the type first described for animal tissue.Enzyme preparations from digitonin-treated homogenates were very unstable. The time necessary for the loss of one-half the activity was 16–18 h when the enzyme was stored at 5 °C; this was reduced to 4 h when storage was in polycarbonate tubes.The enzyme apparently transferred hydrogen directly and with equal ease from NADH to both the 3-acetyl-pyridine and thionicotinamide analogues of NAD. Half-saturation values for NAD and its acetylpyridine analogue were 0.99 × 10−5 M and 3.55 × 10−4 M, respectively. The enzyme exhibited its maximum activity in phosphate buffer at pH 5.8. It was inhibited by 50–60% over the pH range 7.0–8.5 in Tris buffer. This could be reversed by dithiothreitol; reversal was complete between pH 8.0 and 8.5.

scholarly journals Localization and Targeting of an Unusual Pyridine Nucleotide Transhydrogenase in Entamoeba histolytica

2010 ◽  
Vol 9 (6) ◽  
pp. 926-933 ◽  
Author(s):  
Mohammad Abu Yousuf ◽  
Fumika Mi-ichi ◽  
Kumiko Nakada-Tsukui ◽  
Tomoyoshi Nozaki
Keyword(s):  
Entamoeba Histolytica ◽  
Fluorescent Protein ◽  
Physiological Role ◽  
Protozoan Parasite ◽  
Pyridine Nucleotide ◽  
Immunofluorescence Assay ◽  
Chemical Degradation ◽  
Content Type ◽  
Targeting Signal ◽  
Pyridine Nucleotide Transhydrogenase

ABSTRACT Pyridine nucleotide transhydrogenase (PNT) catalyzes the direct transfer of a hydride-ion equivalent between NAD(H) and NADP(H) in bacteria and the mitochondria of eukaryotes. PNT was previously postulated to be localized to the highly divergent mitochondrion-related organelle, the mitosome, in the anaerobic/microaerophilic protozoan parasite Entamoeba histolytica based on the potential mitochondrion-targeting signal. However, our previous proteomic study of isolated phagosomes suggested that PNT is localized to organelles other than mitosomes. An immunofluorescence assay using anti-E. histolytica PNT (EhPNT) antibody raised against the NADH-binding domain showed a distribution to the membrane of numerous vesicles/vacuoles, including lysosomes and phagosomes. The domain(s) required for the trafficking of PNT to vesicles/vacuoles was examined by using amoeba transformants expressing a series of carboxyl-terminally truncated PNTs fused with green fluorescent protein or a hemagglutinin tag. All truncated PNTs failed to reach vesicles/vacuoles and were retained in the endoplasmic reticulum. These data indicate that the putative targeting signal is not sufficient for the trafficking of PNT to the vesicular/vacuolar compartments and that full-length PNT is necessary for correct transport. PNT displayed a smear of >120 kDa on SDS-PAGE gels. PNGase F and tunicamycin treatment, chemical degradation of carbohydrates, and heat treatment of PNT suggested that the apparent aberrant mobility of PNT is likely attributable to its hydrophobic nature. PNT that is compartmentalized to the acidic compartments is unprecedented in eukaryotes and may possess a unique physiological role in E. histolytica.

scholarly journals Dissociation and Assembly of Pyridine Nucleotide Transhydrogenase from Azotobacter vinelandii

1982 ◽  
Vol 127 (2) ◽  
pp. 267-274 ◽  
Author(s):  
Gerrit VOORDOUW ◽  
Hans HAARD ◽  
Johannus A. M. TIMMERMANS ◽  
Cees VEEGER ◽  
Pim ZABEL
Keyword(s):  
Azotobacter Vinelandii ◽  
Pyridine Nucleotide ◽  
Pyridine Nucleotide Transhydrogenase
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