Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.2.1.13 (glyceraldehyde-3-phosphate dehydrogenase)
 6,511 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The system under development has a large counting rate capability; this is extremely important where the total background count exceeds the total counts in the signals of interest. Its spatial resolution is of the order of one mm, which is perfectly adequate for neutron work, while the screen size of 400 mm is reasonable. The main limitation of the system is its limited counting efficiency, and this is directly attributable to the optical self-absorption of the neutron phosphor. Any newly developed transparent phosphor with the same light output would immediately change the situation. The success of the electronics hardware in reducing random noise is demonstrated in Figure 3, which shows in the bottom trace the live video output when the input to the system is a grey-scale test chart. The top trace is the output after the image has been digitally integrated. Figures 4 and 5 show the monitor outputs of the see articles x-ray system with a "still" diffraction pattern of a crystal of GPD (glyceraldehyde-3-phosphate dehydrogenase). Figure 4 is a photograph of the "live" video display, and Figure 5 is the digitally summed image. All coherent noise in the system, i.e., all noise synchronized with the TV scans has to be kept lower than the first bit threshold. However, this requirement can be relaxed when dealing with diffraction patterns, such as those from single crystals, for which a local background is subtracted from the pattern.
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PMID:A neutron television camera detector. 96 82

Amino acid sequence of the 36 KD protein which is the active subunit of immunoglobulin production stimulating factor-II alpha (IPSF-II alpha) derived from Burkitt's lymphoma Namalwa cells was analyzed for the 20 amino acids from N-terminus. The N-terminal amino acid sequence of this protein coincided very closely with glyceraldehyde-3-phosphate dehydrogenase (GPD; EC 1.2.1.12) derived from various origins. Especially, it was completely homologous with that of human liver GPD. Several GPD's derived from human erythrocyte, rabbit muscle and Bacillus stearothermophilus also stimulated IgM production of hybridomas, as well as IPSF-II alpha. Conversely, IPSF-II alpha had GPD enzymic activity as strong as rabbit muscle and B. stearothermophilus, and stronger than human erythrocyte GPD. These results suggested that 36 KD subunit of IPSF-II alpha was a GPD, or GPD like protein. The level of mRNA for IgM was not enhanced by IPSF-II alpha in hybridoma cells, though the IgM productivity of the cell was remarkably stimulated by the protein, indicating that IPSF-II alpha does not stimulate immunoglobulin production by enhancement of transcription.
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PMID:Immunoglobulin production stimulating factor-II alpha (IPSF-II alpha) is glyceraldehyde-3-phosphate dehydrogenase like protein. 136 5

GPD genes encoding glyceraldehyde-3-phosphate dehydrogenase were isolated from the homobasidiomycetes Schizophyllum commune, Phanerochaete chrysosporium and Agaricus bisporus. All three species contain one transcriptionally active GPD gene, but A. bisporus also contains an inactive GPD gene (tandemly linked to the active gene). These genes contain 5-9 introns located at conserved positions, differing (except in one case) from intron positions in ascomycetous GPD genes. The predicted amino-acid sequences of the proteins encoded by the three active GPD genes are highly homologous. A comparison with protein sequences from filamentous ascomycetes shows a clear distinction, whereas the GPD genes from ascomycetous yeasts are quite distinct from both the filamentous ascomycetes and basidiomycetes. Promoter regions of ascomycetous GPD genes do not correspond to those of the GPD genes of basidiomycetes which may (partly) explain poor expression in basidiomycetes of introduced genes driven by an ascomycete GPD promoter.
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PMID:Sequence analysis of the glyceraldehyde-3-phosphate dehydrogenase genes from the basidiomycetes Schizophyllum commune, Phanerochaete chrysosporium and Agaricus bisporus. 147 76

The glyceraldehyde-3-phosphate dehydrogenase (gpd) gene of Podospora anserina has been isolated from a genomic library by heterologous hybridization with the corresponding gene of Curvularia lunata. The coding region consists of 1014 nucleotides and is interrupted by a single intron. The amino-acid sequence encoded by the gpd gene shows a high degree of sequence identity with the corresponding gene products of various fungi. Multiple alignments of all fungal GPD sequences so far available resulted in the construction of a phylogenetic tree. The evolutionary relationships of the various fungi belonging to different taxa will be discussed on the basis of these data. Sequence analysis of 1.9 kbp of the 5' non-coding region revealed the presence of typical fungal promoter elements. Utilizing different parts of the 5' regulatory sequence of the Podospora gpd gene, expression vectors containing a dominant selectable marker gene (hygromycin B phosphotransferase) have been constructed for the transformation of P. anserina protoplasts. The use of these homologous gpd regulatory sequences resulted in a significant increase in transformation efficiencies compared to those obtained with vectors in which the selectable marker gene is under the control of the corresponding heterologous promoter of Aspergillus nidulans.
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PMID:Sequence analysis of the gene coding for glyceraldehyde-3-phosphate dehydrogenase (gpd) of Podospora anserina: use of homologous regulatory sequences to improve transformation efficiency. 156 46

Three anaesthetics (halothane, CF3CHClBr; Ethrane, F2 HCOF2CCHClF; cyclopropane) and one other halogenated, short-chain hydrocarbon (F-12, Cl2F2C) were tested under various conditions to determine their effects on the viability of cells of Escherichia coli and the activities of some of its enzymes. When any of the test chemicals were applied for 60 min at concentrations slightly in excess of saturation, the number of surviving cells decreased substantially, with halothane being the most biocidal of the four chemicals and F-12 the least. Three enzymes (malate dehydrogenase, MD; NADH dehydrogenase; glyceraldehyde-3-phosphate dehydrogenase, GPD) were tested for activity after treatment of E. coli with the test chemicals. In all instances, GPD was least resistant to inactivation and MD was most resistant. Halothane was most inhibitory followed in order by Ethrane, cyclopropane and F-12. Treatment of E. coli with halothane for 60 min at 23 degrees C and a concentration slightly in excess of saturation, resulted in nearly complete inhibition of all three enzymes.
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PMID:Effect of anaesthetics and dichlorodifluoromethane on the viability of the cells of Escherichia coli and the activities of some of its enzymes. 391 44

The GPD 1 gene of Claviceps purpurea coding for glyceraldehyde-3-phosphate dehydrogenase was cloned and sequenced, including 1,800 bp of its 5' upstream region. This gene shows an identical structure to the gpd gene of Podospora anserina and Cryphonectria parasitica (one intron at an identical position) with high homology at both the DNA and amino-acid levels. Two fragments of the promoter spanning from the ATG to -500 bp and to -1,400 bp were fused to the phleomycin-resistance gene. Both constructs transformed C. purpurea at a high rate. The enhanced expression of the long vector construct indicates the presence of additional elements between -500 bp and -1,400 bp upstream of the initiation codon.
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PMID:The Claviceps purpurea glyceraldehyde-3-phosphate dehydrogenase gene: cloning, characterization, and use for the improvement of a dominant selection system. 808 77

Several bisphosphonates were examined as inhibitors of yeast GPD (glyceraldehyde-3-phosphate dehydrogenase, EC 1.2.1.12) and PGK (phosphoglycerate kinase, EC 2.7.2.3). The phosphonomethyl analog of 2-deoxy-1,3-bisphosphoglycerate (i.e., 2-oxo-1,5-bisphosphonopentane, 2-oxo-PC5P) is a good inhibitor of PGK (Ki = 0.2 +/- 0.08 mM at pH 8.5, 27 degrees C) and a poor inhibitor of GPD (Ki = 20 +/- 1 mM, pH 8.5). The shorter, butane, analog (2-oxo-PC4P) binds more tightly to PGK (Ki = 84 +/- 6 microM), and about equally well to GPD, as does 2-oxo-PC5P. The 2-oxo-bisphosphonates bind to PGK more tightly (by approx. 4 kJ/mol) than do the corresponding non-carbonyl analogues (1,4-bisphosphonobutane and 1,5-bisphosphonopentane).
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PMID:Phosphonate inhibitors of glyceraldehyde-3-phosphate dehydrogenase and phosphoglycerate kinase. 851 93

The glyceraldehyde-3-phosphate dehydrogenase (GPD; EC1.2.1.12)-encoding gene (gpd) was isolated from a genomic library of Phaffia rhodozyma CBS 6938. Unlike some other eukaryotic organisms the gpd gene is represented by a single copy in P. rhodozyma. The complete nucleotide sequence of the coding, as well as the flanking non-coding regions was determined. The nucleotide sequence of gpd predicted six introns and a polypeptide chain of 339 amino acids. The codon usage in the gpd gene of P. rhodozyma was highly biased and was significantly different from the codon usage in other yeasts. Phylogenetic analysis of different yeasts and filamentous asco- and basidiomycetes gpd sequences indicated that the gpd gene of P. rhodozyma forms a cluster with the corresponding genes of filamentous basidiomycetes.
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PMID:Molecular characterization of the glyceraldehyde-3-phosphate dehydrogenase gene of Phaffia rhodozyma. 936 47

The GPD gene encoding glyceraldehyde-3-phosphate dehydrogenase was isolated from Cryptococcus neoformans, a heterobasidiomycetous yeast that is pathogenic to humans. The gene contains 11 introns, differing from the conserved intron positions found in the GPD genes of Basidiomycetes. The predicted amino-acid sequence of this gene is extremely similar to that reported from GPD proteins of other basidiomycetes. The promoter region of the C. neoformans GPD gene was similar to those of other basidiomycetes. Plasmid constructs containing up to 1600 base pairs upstream of the native GPD open reading frame were used to express either the native URA5 gene in a ura5 mutant or the heterologous hphI gene (a bacterial gene that confers resistance to the aminoglycoside hygromycin) in a wild-type strain of C. neoformans. Transformation frequencies resulting from the plasmid-borne Gpdp::URA5 gene were at levels similar to those of the native URA5, which suggested that all the sequences necessary for proper expression were present. Transformation frequencies using the Gpdp::hphI gene constructs were poor. However, addition of DNA sequences flanking the 3'-end of an native C. neoformans gene significantly improved the transformation frequencies resulting from the expression of the heterologous hphI gene.
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PMID:Characterization of the glyceraldehyde-3-phosphate dehydrogenase gene [correction of glyceraldehyde-3-phosphate gene] and the use of its promoter for heterologous expression in Cryptococcus neoformans, a human pathogen. 1035 26

A genomic library of Mucor circinelloides ATCC 1216b has been constructed in Lambda Fix II vector. The library has an average insert site of 10 kb and covers the genome 12 times. The M. circinelloides gene encoding glyceraldehyde-3-phosphate dehydrogenase (gpd) was isolated from this library by hybridization of the recombinant phage clones with a gpd-specific gene probe generated by PCR reaction. The complete nucleotide sequence encodes a putative polypeptide chain of 339 amino acids interrupted by 3 introns. The predicted amino acid sequence of this gene shows a high degree of sequence similarity to the GPD proteins from other filamentous fungi. The promoter region, containing a consensus TATA and CAAT box and a 298 nucleotid long termination region were also determined.
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PMID:Cloning and sequence analysis of Mucor circinelloides glyceraldehyde-3-phosphate dehydrogenase gene. 1210 62


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