Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P50583 (asymmetrical)
 12,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The enzymatic transfer of the sugar portion from UDP-N-acetylgalactosamine to pyridylamino (PA) lacto-N-fucopentaose I (Fuc alpha 1-2Gal beta 1-3GlcNAc beta 1-4Glc-PA) was detected by high-performance liquid chromatography. Separation of the fluorescent product from the fluorescence-labeled acceptor was achieved within 10 min by reversed-phase high-performance liquid chromatography. Rat stomach enzyme activity was detected in the microsomal fraction from antrum but not corpus. Ohara et al. (1986, Comp. Biochem. Physiol. 83B, 273-275) reported that the N-acetylgalactosamine content in antrum mucin was greater than that in corpus mucin and antrum mucin had strong blood group A activity. The prominent asymmetrical distribution of the enzyme detected here well supports these findings. The elution position of the fluorescent product was the same as that of the product formed by the action of type A human serum toward the acceptor. Its hydrolysis by alpha-N-acetylgalactosaminidase yielded the acceptor. It is thus evident that the detected enzyme is the same as that producing the blood group A structure.
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PMID:Detection of UDP-N-acetylgalactosamine-oligosaccharide N-acetylgalactosaminyltransferase activity in rat stomach and human serum by high-performance liquid chromatography. 314 99

Nucleotide sugar transporters play an essential role in protein and lipid glycosylation, and mutations can result in developmental phenotypes. We have characterized a transporter of UDP-N-acetylglucosamine and UDP-N-acetylgalactosamine encoded by the Caenorhabditis elegans gene C03H5.2. Surprisingly, translocation of these substrates occurs in an independent and simultaneous manner that is neither a competitive nor a symport transport. Incubations of Golgi apparatus vesicles of Saccharomyces cerevisiae expressing C03H5.2 protein with these nucleotide sugars labeled with (3)H and (14)C in their sugars showed that both substrates enter the lumen to the same extent, whether or not they are incubated alone or in the presence of a 10-fold excess of the other nucleotide sugar. Vesicles containing a deletion mutant of the C03H5.2 protein transport UDP-N-acetylglucosamine at rates comparable with that of wild-type transporter, whereas transport of UDP-N-acetylgalactosamine was decreased by 85-90%, resulting in an asymmetrical loss of substrate transport.
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PMID:Independent and simultaneous translocation of two substrates by a nucleotide sugar transporter. 1706 Jun 6