Purine and Pyrimidine Metabolism in Man X
DOI: 10.1007/0-306-46843-3_22
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Human Guanine Deaminase: Cloning, Expression and Characterisation

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Cited by 7 publications
(3 citation statements)
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“…In this pathway, seven DEGs were detected and annotated to seven proteins, including guanylyl cyclases, 3 -phosphoadenosine 5 -prime-phosphosulfate, TWISTNB protein, ectonucleoside triphosphate diphosphohydrolase, NTPDase 3, NTPDase 8, cGMP-specific-3 ,5 -cyclic phosphodiesterase, and guanine deaminase. They are mainly involved in the regulation of the nervous system (Snyder et al, 2000;Xu et al, 2000;Belcher et al, 2006). In this study, most of the DEGs in this pathway were downregulated, suggesting that the function of the nervous system is damaged, which may lead to uncoordinated movements in animals.…”
Section: Discussionmentioning
confidence: 60%
“…In this pathway, seven DEGs were detected and annotated to seven proteins, including guanylyl cyclases, 3 -phosphoadenosine 5 -prime-phosphosulfate, TWISTNB protein, ectonucleoside triphosphate diphosphohydrolase, NTPDase 3, NTPDase 8, cGMP-specific-3 ,5 -cyclic phosphodiesterase, and guanine deaminase. They are mainly involved in the regulation of the nervous system (Snyder et al, 2000;Xu et al, 2000;Belcher et al, 2006). In this study, most of the DEGs in this pathway were downregulated, suggesting that the function of the nervous system is damaged, which may lead to uncoordinated movements in animals.…”
Section: Discussionmentioning
confidence: 60%
“…Fernández et al [2009]. This sequence is common in the amidohydrolases family [Kim and Kim, 1998] and has been described in guanine deaminases of E. coli , S. cerevisiae and humans [Maynes et al, 2000;Saint-Marc and DaignanFornier, 2004;Snyder et al, 2000]. The amino acid sequence of A. adeninivorans LS3 did not, however, contain signal sequences for intracellular localisation or for secretion.…”
Section: Discussionmentioning
confidence: 99%
“…This often leads to the formation of specific chemical motifs that are unique and determinant for the protein function . The enzyme guanine deaminase is one of these cases with a zinc ion surrounded by a cluster of histidine residues in its active site . The X‐ray structure with the bound product (pdb code: 2UZ9) also reveals that the metal ion interacts very closely with the substrate, and therefore, it participates directly in the catalytic process.…”
Section: Software Validationmentioning
confidence: 99%