1999
DOI: 10.1074/jbc.274.12.8175
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Cloning and Characterization of Human Guanine Deaminase

Abstract: Mouse erythrocyte guanine deaminase has been purified to homogeneity. The native enzyme was dimeric, being comprised of two identical subunits of approximately 50,000 Da. The protein sequence was obtained from five cyanogen bromide cleavage products giving sequences ranging from 12 to 25 amino acids in length and corresponding to 99 residues. Basic Local Alignment Search Tool (BLAST) analysis of expressed sequence databases enabled the retrieval of a human expressed sequence tag cDNA clone highly homologous to… Show more

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Cited by 60 publications
(26 citation statements)
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“…The dihydro-orotase from hamster was suggested to contain two atoms of zinc per mol of enzyme (26), whereas recently the E. coli enzyme was revealed to have four atom of zinc per mol of enzyme by three-dimensional structure analysis (41). A recently purified and cloned human guanine deaminase (which also possesses the metal binding motif DXHXH) was determined to contain two atoms of zinc per mol of enzyme (42). The zinc-binding site of barbiturase is located at amino acids 320 -324 (DVHWH, Fig.…”
Section: Discussionmentioning
confidence: 99%
“…The dihydro-orotase from hamster was suggested to contain two atoms of zinc per mol of enzyme (26), whereas recently the E. coli enzyme was revealed to have four atom of zinc per mol of enzyme by three-dimensional structure analysis (41). A recently purified and cloned human guanine deaminase (which also possesses the metal binding motif DXHXH) was determined to contain two atoms of zinc per mol of enzyme (42). The zinc-binding site of barbiturase is located at amino acids 320 -324 (DVHWH, Fig.…”
Section: Discussionmentioning
confidence: 99%
“…These proteins have a histidine-aspartic acid signature which is required for metal binding (27) and are known to catalyze hydrolytic reactions with nitrogen heterocyclic ring substrates (29). During the preparation of this manu- script, cDNA encoding a human protein having guanine aminohydrolase (GAH) activity was reported (28), and its deduced amino acid sequence is identical to nedasin. GAH catalyzes the hydrolytic deamination of guanine, yielding xanthine and ammonium, and is considered to be involved in a major pathway for producing uric acid (30).…”
Section: Discussionmentioning
confidence: 99%
“…Notably, the N-terminal HXH motif of the signature pattern and the C-terminally conserved block of the amidohydrolase superfamily are highly conserved in nedasin. A recent report (28) shows that the protein that harbors a guanine aminohydrolase activity appears to have an identical sequence to nedasin, suggesting that nedasin may be involved in intracellular guanine metabolism.…”
Section: Purification Of Ne-dlg/sap102-associating Protein-tomentioning
confidence: 99%
“…1,2 Two families of GDs have evolved in nature, one with ∼160 amino residues such as Bacillus subtilis GD (bGD) 1 and the other with >400 residues such as Escherichia coli 3 and mammalian GDs. [4][5][6] In mammals, the GD gene expression is tissue-specific and development-dependent. 4,5,7,8 Because of its near absence in normal human serum, erythrocytes, and lymphoid cells, the GD activity is a specific and sensitive index for the diagnosis of liver diseases.…”
Section: Introductionmentioning
confidence: 99%
“…[4][5][6] In mammals, the GD gene expression is tissue-specific and development-dependent. 4,5,7,8 Because of its near absence in normal human serum, erythrocytes, and lymphoid cells, the GD activity is a specific and sensitive index for the diagnosis of liver diseases. 9,10 The crystal structure of bGD has been determined at 1.17 Å resolution.…”
Section: Introductionmentioning
confidence: 99%