1997 Fiscal Year Final Research Report Summary
Evolution of peroxisomal enzymes-Lost organization of uric acid degrading enzymes during animal development-
| Project/Area Number |
08680700
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | Kyushu Dental College |
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Principal Investigator |
NOGUCHI Tomoo Kyushu Dental College, Dept.of dentistry Professor, 歯学部, 教授 (30073688)
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| Co-Investigator(Kenkyū-buntansha) |
HAYASHI Sueko Kyushu Dental College, Dept.of dentistry Assistant Professor, 歯学部, 講師 (30047807)
FUJIWARA Satoko Kyushu Dental College, Dept.of dentistry Associate Professor, 歯学部, 助教授 (20047806)
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| Project Period (FY) |
1996 – 1997
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| Keywords | Animal evolution / Purine degradation / Urate degradation / Allantoinase / Allantoicase / Ureidoglyocollate lyase / Frog allantoinase gt 11 cDNA / Peroxisome |
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| Research Abstract |
End products of purine degradation vary from species to species. The end product of purine degradation is urate in humans, hominoid primates and new would monkeys, allantoin by uricase in mammals other than primates and old world monkeys, allantoate by allantoinase in some teleosts, urea by allantoicase in fish and amphibians and ammonia in many invertebrates.
The degradation of purines to urate is common to all animal species, while the degradation of urate is much less complete in higher animals. We have reported that in marine fish, the degrading enzymes of purines to urate are located in the cytosol, while the degrading enzymes of urate to urea are located in the peroxisomes. This shows that in purine degradation, peroxisomal enzymes have been lost during evolution. Allantoinase and allantoicase are different proteins in fish liver, whereas the two enzymes from a complex in amphibian liver. We examined the mechanism to form amphibian allantoinase-allantoicase complex and lose in hig
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her animals during animal evolution.
(1).The cDNA encoding bullfrog (Rana Catesbeiana) allantoinase is 2112 base pairs in length containing a 1449-base pair open reading frame which corresponds to a 483-residue protein.(53,296 Da) (2).We did the cloning of lambda gt 11 cDNA endoding zebra fish allantoinase. The cDNA was applified with PCR and sequenced with DNA sequencer. (3).In saltwater fish liver, the end products of purine degradation are urea and glyoxylate. Glyoxylate may be converted to glycine by alanine : glyoxylate aminotransferase for the reutilization of purine carbons. (4).It is generally accepted that all of the allantoin-degrading enzymes were lost during mammalian evolution. Surprisingly, ureidoglycollate lyase has been found in a mammalian tissue. The apparent Km (17 mM) of the rat enzyme for ureidoglycollate was much higher than (0.33 mM) of fish-liver ureidoglycollate lyase. Mammals have lost the function in vivo by elevating the km for ureidoglycollate during evolution. (5).cDNA encoding bullfrog catalase is 1636 base pairs in length containing a 1584 bases of an open reading frame that encoded 528 amino acids. (59871) Less
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Research Products
(14 results)
