Recognition of Arylsulfatase A and B by the UDP-N-acetylglucosamine:lysosomal Enzyme N-Acetylglucosamine-phosphotransferase
نویسندگان
چکیده
منابع مشابه
Bovine UDP-N-acetylglucosamine:lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase. II. Enzymatic characterization and identification of the catalytic subunit.
The kinetic properties of UDP-N-acetylglucosamine:lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase (GlcNAc-phosphotransferase) purified to homogeneity from lactating bovine mammary gland have been investigated. GlcNAc-phosphotransferase transferred GlcNAc 1-phosphate from UDP-GlcNAc to the synthetic acceptor alpha-methylmannoside, generating GlcNAc-1-phospho-6-mannose alpha-methyl, the...
متن کاملStructural requirements for efficient processing and activation of recombinant human UDP-N-acetylglucosamine:lysosomal-enzyme-N-acetylglucosamine-1-phosphotransferase.
Mannose 6-phosphate-modified N-glycans are the determinant for intracellular targeting of newly synthesized lysosomal hydrolases to the lysosome. The enzyme responsible for the initial step in the synthesis of mannose 6-phosphate is UDP-N-acetylglucosamine:lysosomal-enzyme-N-acetylglucosmine-1-phosphotransferase(GlcNAc-phosphotransferase). GlcNAc-phosphotransferase is a multisubunit enzyme with...
متن کاملLysosomal enzyme phosphorylation. I. Protein recognition determinants in both lobes of procathepsin D mediate its interaction with UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase.
We have investigated the nature of a protein domain that is shared among lysosomal hydrolases and is recognized by UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase, the initial enzyme in the biosynthesis of mannose 6-phosphate residues. Previously, elements of this recognition domain were identified using a chimeric protein approach. The combined substitution of two regions ...
متن کاملHydrocarbon rulers in UDP-N-acetylglucosamine acyltransferases.
UDP-GlcNAc acyltransferase (LpxA), the first enzyme of lipid A biosynthesis, catalyzes the transfer of an acyl chain activated on acyl carrier protein (ACP) to UDP-GlcNAc. LpxAs are very selective for the lengths of their acyl donor substrates. Escherichia coli LpxA prefers R-3-hydroxymyristoyl-ACP to R-3-hydroxydecanoyl-ACP by a factor of approximately 1000, whereas Pseudomonas aeruginosa LpxA...
متن کاملDiazobenzenesulphonate selectively abolishes stimulation of glucuronidation by UDP-N-acetylglucosamine.
1. Basal rates of glucuronidation of oestrone (guinea pig) or of 4-nitrophenol (rat or guinea pig) were not significantly altered in sealed liver microsomal vesicles, treated with the membrane-impermeant protein-modifying agent diazobenzenesulphonate at 0.5-1.0 mM. 2. Contrarily, diazobenzenesulphonate abolished the normal stimulation of glucuronidation by UDP-N-acetylglucosamine. 3. Ultrasonic...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2003
ISSN: 0021-9258
DOI: 10.1074/jbc.m304865200