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ALLC  -  allantoicase

Homo sapiens

Synonyms: ALC, Allantoate amidinohydrolase
 
 
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Disease relevance of ALLC

 

High impact information on ALLC

  • Degradation of uric acid in fish liver peroxisomes. Intraperoxisomal localization of hepatic allantoicase and purification of its peroxisomal membrane-bound form [2].
  • Genomic organization and chromosome localization of the murine and human allantoicase gene [3].
  • The enzymes of this catabolic pathway (i.e. allantoinase, allantoicase, ureidoglycolate lyase and urease) were lost during vertebrate evolution and the causes for this loss are still unclear [3].
  • By comparison with available genomic sequences deposited in database, we have determined that the human allantoicase gene consists of five exons and spans 8kb [4].
  • Allantoicase cDNA is expressed in adult testis, prostate, kidney and fetal spleen [4].
 

Biological context of ALLC

 

Anatomical context of ALLC

  • Erwinia-like bacteria were found exclusively in the cecum of midgut, in which three uricolytic enzymes, i.e., uricase, allantoinase and allantoicase were detected [6].
  • The aim of this study was to detect an eventual allantoicase-like activity in the human gut and to elucidate the metabolism of glycosyl ureides by human intestinal brush border enzymes [7].
 

Associations of ALLC with chemical compounds

  • Urate-degrading enzymes such as uricase, allantoinase, and allantoicase are located in the peroxisomes of marine fish liver (Noguchi, T., Takada, Y., and Fujiwara, S. (1979) J. Biol. Chem. 254, 5272-5275) [2].
  • Allantoate amidinohydrolase was reported to be the pathway of degradation in studies using the cultivar Maple Arrow and allantoate amidohydrolase was the pathway that existed in the cultivar Williams [8].
  • Allantoin is broken down to glyoxylate and ammonia by the consecutive action of allantoinase, allantoicase, ureidoglycolase and urease [9].
  • Thus, the activity of allantoicase, a key inducible enzyme of this metabolism, was used as tool for assaying the activation of the purine degradation pathway [1].
 

Analytical, diagnostic and therapeutic context of ALLC

  • Increased mean serum concentrations and Cu/Zn ratios were found in the whole group (ALLC), and for the GIC and GYNC groups with local as well as metastasized (Meta) disease in comparison with the control group [10].

References

  1. The purine degradation pathway: possible role in paralytic shellfish toxin metabolism in the cyanobacterium Planktothrix sp. FP1. Pomati, F., Manarolla, G., Rossi, O., Vigetti, D., Rossetti, C. Environment international. (2001) [Pubmed]
  2. Degradation of uric acid in fish liver peroxisomes. Intraperoxisomal localization of hepatic allantoicase and purification of its peroxisomal membrane-bound form. Hayashi, S., Fujiwara, S., Noguchi, T. J. Biol. Chem. (1989) [Pubmed]
  3. Genomic organization and chromosome localization of the murine and human allantoicase gene. Vigetti, D., Monetti, C., Prati, M., Gornati, R., Bernardini, G. Gene (2002) [Pubmed]
  4. Human allantoicase gene: cDNA cloning, genomic organization and chromosome localization. Vigetti, D., Monetti, C., Acquati, F., Taramelli, R., Bernardini, G. Gene (2000) [Pubmed]
  5. Evolution of urate-degrading enzymes in animal peroxisomes. Hayashi, S., Fujiwara, S., Noguchi, T. Cell Biochem. Biophys. (2000) [Pubmed]
  6. Uric acid recycling in the shield bug, Parastrachia japonensis (Hemiptera: Parastrachiidae), during diapause. Kashima, T., Nakamura, T., Tojo, S. J. Insect Physiol. (2006) [Pubmed]
  7. Metabolism of glycosyl ureides by human intestinal brush border enzymes. Ruemmele, F.M., Heine, W.E., Keller, K.M., Lentze, M.J. Biochim. Biophys. Acta (1997) [Pubmed]
  8. Ureide degradation pathways in intact soybean leaves. Vadez, V., Sinclair, T.R. J. Exp. Bot. (2000) [Pubmed]
  9. Metabolism of allantoin in Hyphomicrobium species. van der Drift, C., de Windt, F.E., Doddema, H.J. Antonie Van Leeuwenhoek (1981) [Pubmed]
  10. Analysis of serum copper and zinc concentrations in cancer patients. Zowczak, M., Iskra, M., Torliński, L., Cofta, S. Biological trace element research. (2001) [Pubmed]
 
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