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Gene Review:

GULO - gulonolactone (L-) oxidase

Sus scrofa

Inai, Y. et al., Nishikimi, M. et al., Koshizaka, T. et al., Hasan, L. et al., Ching, S. et al., et al.

Mahan, Ching, Dabrowski,

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High impact information on GULO

L-Gulono-gamma-lactone oxidase (L-gulono-gamma-lactone:oxygen 2-oxidoreductase, EC 1.1.3.8) is the enzyme that catalyzes the terminal step of L-ascorbic acid biosynthesis in mammalian liver [1].
On the other hand, extracts of all 10 other mammalian (4 orders) liver microsomes tested were shown to contain L-gulono-gamma-lactone oxidase activity that did crossreact with antibodies to the rat and goat enzymes [1].
Ascorbic acid synthesis in the pig occurs at mid-pregnancy, but activity of the enzyme l-gulono-gamma-lactone oxidase (GLO) declines thereafter during gestation and remains low when the pig nurses the sow [2].
Our results demonstrated that 10 mM of substrate added to the reaction media maximized L-gulono-gamma-lactone oxidase enzyme activity, whereas increasing levels of glutathione did not greatly affect enzyme activity [3].
We isolated part of the GULO gene of the pig by screening a porcine genomic library using a pig GULO cDNA as a probe, and mapped it to SSC14q14 by fluorescence in situ hybridization (FISH) [4].

Biological context of GULO

The L-gulono-gamma-lactone oxidase gene (GULO) which is a candidate for vitamin C deficiency in pigs maps to chromosome 14 [4].
Only five exons, as compared to 12 exons constituting the functional rat GULO gene, remain in the human genome [5].
From analyses of the molecular evolution of Alu sequences in the human GULO gene homologue, it is thought that two Alu sequences were inserted in the vicinity of a presumed position of lost exon 11 during the same period as GULO lost its function [5].
The whole structure of the human nonfunctional L-gulono-gamma-lactone oxidase gene--the gene responsible for scurvy--and the evolution of repetitive sequences thereon [5].

Anatomical context of GULO

In vitro synthesis of L-gulono-gamma-lactone oxidase by rabbit reticulocyte lysate [6].

Associations of GULO with chemical compounds

The absence of L-ascorbic acid (L-AA, or AA) synthesis in scurvy-prone organisms, including humans, other primates, guinea pigs, and flying mammals, was traced to the lack of L-gulonolactone oxidase (GULO) activity [7].
In vitro synthesis of L-gulono-gamma-lactone oxidase [L-gulono-gamma-lactone:oxygen 2-oxidoreductase, EC 1.1.3.8], one of the microsomal flavin enzymes, was performed with poly(A)+ RNA of rat liver using the rabbit reticulocyte lysate system in order to study the biosynthesis of the enzyme [6].

References

Immunologic evidence that the gene for L-gulono-gamma-lactone oxidase is not expressed in animals subject to scurvy. Nishikimi, M., Udenfriend, S. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
Developmental aspects and factors influencing the synthesis and status of ascorbic Acid in the pig. Mahan, D.C., Ching, S., Dabrowski, K. Annu. Rev. Nutr. (2004) [Pubmed]
Modification of analytical procedures for determining vitamin C enzyme (L-gulonolactone oxidase) activity in swine liver. Ching, S., Mahan, D.C., Moreau R, R., Dabrowski, K. J. Nutr. Biochem. (2003) [Pubmed]
The L-gulono-gamma-lactone oxidase gene (GULO) which is a candidate for vitamin C deficiency in pigs maps to chromosome 14. Hasan, L., Vögeli, P., Neuenschwander, S., Stoll, P., Meijerink, E., Stricker, C., Jörg, H., Stranzinger, G. Anim. Genet. (1999) [Pubmed]
The whole structure of the human nonfunctional L-gulono-gamma-lactone oxidase gene--the gene responsible for scurvy--and the evolution of repetitive sequences thereon. Inai, Y., Ohta, Y., Nishikimi, M. J. Nutr. Sci. Vitaminol. (2003) [Pubmed]
In vitro synthesis of L-gulono-gamma-lactone oxidase by rabbit reticulocyte lysate. Koshizaka, T., Nishikimi, M., Tanaka, M., Nakashima, K., Ozawa, T., Yagi, K. Biochem. Int. (1987) [Pubmed]
Intragenic deletion in the gene encoding L-gulonolactone oxidase causes vitamin C deficiency in pigs. Hasan, L., Vögeli, P., Stoll, P., Kramer, S.S., Stranzinger, G., Neuenschwander, S. Mamm. Genome (2004) [Pubmed]

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