Metabolism of urea and glyoxylate, degradative products of purines in marine animals

Tomoo Noguchi, Satoko Fujiwara, Yoshikazu Takada, Toshio Mori, Miyota Nagano

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

In marine fish and crustacean liver, degradative enzymes able to convert purines to urate have been shown to be located only in the cytosol, and degradative enzymes able to convert urate to urea and glyoxylate, only in the peroxisomes (Noguchi, T., Takada, Y., & Fujiwara, S. (1979) J. Biol. Chem. 254, 5272-5275). The subcellular distribution of these two enzymes involved in further metabolism of urea and glyoxylate in marine animal species was examined by centrifugation in a sucrose density gradient.Urease was located only in the cytosol of crustacean and mollusc liver; no activity was detected with fish liver.In fish, crustacean and mollusc liver, the conversion of glyoxylate to glycine may be mainly catalyzed by alanine: glyoxylate aminotransferase. Hepatic alanine: glyoxylate aminotransferase was located both in the mitochondrial matrix and in the cytosol in each species studied.These findings suggest that peroxisomal urea is transported to the cytosol then degraded to NH3 for the excretion of purine nitrogens, while peroxisomal glyoxylate is transported to the cytosol or mitochondria then converted to glycine for the reutilization of purine carbons.

Original languageEnglish
Pages (from-to)525-529
Number of pages5
JournalJournal of Biochemistry
Volume92
Issue number2
Publication statusPublished - 1982
Externally publishedYes

Fingerprint

Purines
Metabolism
Urea
Liver
Cytosol
Animals
Fish
Molluscs
Enzymes
Uric Acid
Fishes
Glycine
Mollusca
Convert
Amino acids
Mitochondria
Centrifugation
Urease
Sugar (sucrose)
Sucrose

ASJC Scopus subject areas

  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Physiology (medical)
  • Radiology Nuclear Medicine and imaging
  • Molecular Biology
  • Biochemistry

Cite this

Noguchi, T., Fujiwara, S., Takada, Y., Mori, T., & Nagano, M. (1982). Metabolism of urea and glyoxylate, degradative products of purines in marine animals. Journal of Biochemistry, 92(2), 525-529.

Metabolism of urea and glyoxylate, degradative products of purines in marine animals. / Noguchi, Tomoo; Fujiwara, Satoko; Takada, Yoshikazu; Mori, Toshio; Nagano, Miyota.

In: Journal of Biochemistry, Vol. 92, No. 2, 1982, p. 525-529.

Research output: Contribution to journalArticle

Noguchi, T, Fujiwara, S, Takada, Y, Mori, T & Nagano, M 1982, 'Metabolism of urea and glyoxylate, degradative products of purines in marine animals', Journal of Biochemistry, vol. 92, no. 2, pp. 525-529.
Noguchi T, Fujiwara S, Takada Y, Mori T, Nagano M. Metabolism of urea and glyoxylate, degradative products of purines in marine animals. Journal of Biochemistry. 1982;92(2):525-529.
Noguchi, Tomoo ; Fujiwara, Satoko ; Takada, Yoshikazu ; Mori, Toshio ; Nagano, Miyota. / Metabolism of urea and glyoxylate, degradative products of purines in marine animals. In: Journal of Biochemistry. 1982 ; Vol. 92, No. 2. pp. 525-529.
@article{2da641129a5741fea9885404836f3f13,
title = "Metabolism of urea and glyoxylate, degradative products of purines in marine animals",
abstract = "In marine fish and crustacean liver, degradative enzymes able to convert purines to urate have been shown to be located only in the cytosol, and degradative enzymes able to convert urate to urea and glyoxylate, only in the peroxisomes (Noguchi, T., Takada, Y., & Fujiwara, S. (1979) J. Biol. Chem. 254, 5272-5275). The subcellular distribution of these two enzymes involved in further metabolism of urea and glyoxylate in marine animal species was examined by centrifugation in a sucrose density gradient.Urease was located only in the cytosol of crustacean and mollusc liver; no activity was detected with fish liver.In fish, crustacean and mollusc liver, the conversion of glyoxylate to glycine may be mainly catalyzed by alanine: glyoxylate aminotransferase. Hepatic alanine: glyoxylate aminotransferase was located both in the mitochondrial matrix and in the cytosol in each species studied.These findings suggest that peroxisomal urea is transported to the cytosol then degraded to NH3 for the excretion of purine nitrogens, while peroxisomal glyoxylate is transported to the cytosol or mitochondria then converted to glycine for the reutilization of purine carbons.",
author = "Tomoo Noguchi and Satoko Fujiwara and Yoshikazu Takada and Toshio Mori and Miyota Nagano",
year = "1982",
language = "English",
volume = "92",
pages = "525--529",
journal = "Journal of Biochemistry",
issn = "0021-924X",
publisher = "Oxford University Press",
number = "2",

}

TY - JOUR

T1 - Metabolism of urea and glyoxylate, degradative products of purines in marine animals

AU - Noguchi, Tomoo

AU - Fujiwara, Satoko

AU - Takada, Yoshikazu

AU - Mori, Toshio

AU - Nagano, Miyota

PY - 1982

Y1 - 1982

N2 - In marine fish and crustacean liver, degradative enzymes able to convert purines to urate have been shown to be located only in the cytosol, and degradative enzymes able to convert urate to urea and glyoxylate, only in the peroxisomes (Noguchi, T., Takada, Y., & Fujiwara, S. (1979) J. Biol. Chem. 254, 5272-5275). The subcellular distribution of these two enzymes involved in further metabolism of urea and glyoxylate in marine animal species was examined by centrifugation in a sucrose density gradient.Urease was located only in the cytosol of crustacean and mollusc liver; no activity was detected with fish liver.In fish, crustacean and mollusc liver, the conversion of glyoxylate to glycine may be mainly catalyzed by alanine: glyoxylate aminotransferase. Hepatic alanine: glyoxylate aminotransferase was located both in the mitochondrial matrix and in the cytosol in each species studied.These findings suggest that peroxisomal urea is transported to the cytosol then degraded to NH3 for the excretion of purine nitrogens, while peroxisomal glyoxylate is transported to the cytosol or mitochondria then converted to glycine for the reutilization of purine carbons.

AB - In marine fish and crustacean liver, degradative enzymes able to convert purines to urate have been shown to be located only in the cytosol, and degradative enzymes able to convert urate to urea and glyoxylate, only in the peroxisomes (Noguchi, T., Takada, Y., & Fujiwara, S. (1979) J. Biol. Chem. 254, 5272-5275). The subcellular distribution of these two enzymes involved in further metabolism of urea and glyoxylate in marine animal species was examined by centrifugation in a sucrose density gradient.Urease was located only in the cytosol of crustacean and mollusc liver; no activity was detected with fish liver.In fish, crustacean and mollusc liver, the conversion of glyoxylate to glycine may be mainly catalyzed by alanine: glyoxylate aminotransferase. Hepatic alanine: glyoxylate aminotransferase was located both in the mitochondrial matrix and in the cytosol in each species studied.These findings suggest that peroxisomal urea is transported to the cytosol then degraded to NH3 for the excretion of purine nitrogens, while peroxisomal glyoxylate is transported to the cytosol or mitochondria then converted to glycine for the reutilization of purine carbons.

UR - http://www.scopus.com/inward/record.url?scp=0020172710&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020172710&partnerID=8YFLogxK

M3 - Article

VL - 92

SP - 525

EP - 529

JO - Journal of Biochemistry

JF - Journal of Biochemistry

SN - 0021-924X

IS - 2

ER -