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Results 1 - 10 of 88 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157288685 Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis J. Bacteriol. 176 5788-5795 1994 Bacillus subtilis 8083170
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157288685 Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis J. Bacteriol. 176 5788-5795 1994 Escherichia coli 8083170
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157288685 Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis J. Bacteriol. 176 5788-5795 1994 Escherichia coli JM83 8083170
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157288686 Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes J. Bacteriol. 180 4799-4803 1998 Bacillus subtilis 9733680
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157288686 Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes J. Bacteriol. 180 4799-4803 1998 Escherichia coli 9733680
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157288686 Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes J. Bacteriol. 180 4799-4803 1998 Neisseria gonorrhoeae 9733680
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157288686 Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes J. Bacteriol. 180 4799-4803 1998 Escherichia coli JM83 9733680
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157643073 Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture J. Biol. Chem. 276 11844-11851 2001 Streptococcus pneumoniae 11118459
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157643076 Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 A resolution J. Mol. Biol. 305 279-289 2001 Streptococcus pneumoniae 11124906
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157288688 Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into autonomously functional domains and evidence that trimerization is absolutely required for glucosamine-1-phosphate acetyltransferase activity and cell growth J. Biol. Chem. 276 3833-3839 2001 Escherichia coli 11084021
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