Journal of Molecular Biology
Regular ArticleCrystal Structures of Streptococcus pneumoniaeN-Acetylglucosamine-1-phosphate Uridyltransferase, GlmU, in Apo Form at 2.33 Å Resolution and in Complex with UDP-N-Acetylglucosamine and Mg2+ at 1.96 Å Resolution☆,☆☆
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Cited by (86)
Study of duplicated galU genes in Rhodococcus jostii and a putative new metabolic node for glucosamine-1P in rhodococci
2021, Biochimica et Biophysica Acta - General SubjectsCitation Excerpt :In the first reaction, GlcN-1P is acetylated using acetyl-CoA and in the second reaction GlcNAc-1P and UTP are used to generate UDP-GlcNAc. Since we found RjoGalU2 was a GlcN-1P specific pyrophosphorylase enzyme with a trimeric quaternary structure typically described for GlmUs [42–45], we turned our attention to the characterization of the RjoGlmU enzyme. UDP-GlcNAc is a critical metabolite in lipopolysaccharide and peptidoglycan synthetic pathways [28]; therefore, it is important to understand possible GlcN-1P partitioning in R. jostii.
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Abbreviations used: GlmU, N-acetylglucosamine phosphate uridyltransferase; UDP-GlcNAc, UDP-N-acetylglucosamine; GlcN-1-P, glucosamine 1-phosphate; GlcNAlc-1-P, N-acetylglucosamine-1-phosphate; Uap1p, UDP-N-acetylglucosamine pyrophosphorylase; LβH, left-handed β-helix structure; SpGlmU, Streptococcus pneumoniae GlmU; tr-EcGlmU, truncated form of Escherichia coli GlmU; DapD, tetrahydrodipicolinate-N-succingltransferase; Cam, Methanosarcina thermophila carbonic anhydrase; LpxA, Escherichia coli UDP-N-acetylglucosamine acetyltransferase; EcGlmU, Escherichia coli GlmU; PaXAT, Pseudomonas aeruginosa hexapeptide xenobiotic acetyltransferase
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Edited by R. Huber
- f1
Corresponding author
- f2
E-mail address of the corresponding author: [email protected]
- f3
Present address: D. Kostrewa, Paul Scherrer Institute, Life Sciences, OSRA/007, CH-5232 Villigen PSI, Switzerland