Reference on EC 1.3.1.98 - UDP-N-acetylmuramate dehydrogenase
Please use the Reference Search for a specific query.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Anwar, R.A.; Vlaovic, M.
Purification of UDP-N-acetylenolpyruvoylglucosamine reductase from Escherichia coli by affinity chromatography, its subunit structure and the absence of flavin as the prosthetic group
Can. J. Biochem.
57
188-196
1979
Escherichia coli
Wickus, G.G.; Rubenstein, P.A.; Warth, A.D.; Strominger, J.L.
Partial purification and some properties of the uridine diphospho-N-acetylglucosamine-enolpyruvate reductase from Staphylococcus epidermidis
J. Bacteriol.
113
291-294
1973
Staphylococcus epidermidis
Mengin-Lecreulx, D.; van Heijenoort, J.
Effect of growth conditions on peptidoglycan content and cytoplasmic steps of its biosynthesis in Escherichia coli
J. Bacteriol.
163
208-212
1985
Escherichia coli
Mengin-Lecreulx, D.; Flouret, B.; van Heijenoort, J.
Pool levels of UDP N-acetylglucosamine and UDP N-acetylglucosamine-enolpyruvate in Escherichia coli and correlation with peptidoglycan synthesis
J. Bacteriol.
154
1284-1290
1983
Escherichia coli
Taku, A.; Gunetileke, K.G.; Anwar, R.A.
Biosynthesis of uridine diphospho-N-acetylmuramic acid. 3. Purification and properties of uridine diphospho-N-acetylenolpyruvyl-glucosamine reductase
J. Biol. Chem.
245
5012-5016
1970
Enterobacter cloacae, Enterobacter cloacae NRC 492
Taku, A.; Anwar, R.A.
Biosynthesis of uridine diphospho-N-acetylmuramic acid. IV. Activation of uridine diphospho-N-acetylenolpyruvylglucosamine reductase by monovalent cations
J. Biol. Chem.
248
4971-4976
1973
Enterobacter cloacae, Enterobacter cloacae NRC 492
Dhalla, A.M.; Yanchunas, J.Jr.; Ho, H.T.; Falk, P.J.; Villafranca, J.J.; Robertson, J.G.
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
Biochemistry
34
5390-5402
1995
Escherichia coli
Benson, T.E.; Marquardt, J.L.; Marquardt, A.C.; Etzkorn, F.A.; Walsh, C.T.
Overexpression, purification, and mechanistic study of UDP-N-acetylenolpyruvylglucosamine reductase
Biochemistry
32
2024-2030
1993
Escherichia coli
Benson, T.E.; Walsh, C.T.; Massey, V.
Kinetic characterization of wild-type and S229A mutant MurB: evidence of the role of Ser 229 as a general acid
Biochemistry
36
796-805
1997
Escherichia coli
Sylvester, D.R.; Alvarez, E.; Patel, A.; Ratnam, K.; Kallender, H.; Wallis, N.G.
Identification and characterization of UDP-N-acetylenolpyruvylglucosamine reductase (MurB) from the gram-positive pathogen Streptococcus pneumoniae
Biochem. J.
355
431-435
2001
Streptococcus pneumoniae, Streptococcus pneumoniae 100993
Benson, T.E.; Walsh, C.T.; Hogle, J.M.
X-ray crystal structure of the S299A mutant and wild-type MurB in the presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine at 1.8-A resolution
Biochemistry
36
806-811
1997
Escherichia coli
Benson, T.E.; Walsh, C.T.; Hogle, J.M.
Crystallisation and preliminary X-ray crystallographic studies of UDP-N-acetylenolpyruvylglucosamine reductase
Protein Sci.
3
1125-1127
1994
Escherichia coli
Harris, M.S.; Herberg, J.T.; Cialdella, J.I.; Martin, J.T., Jr.; Benson, T.E.; Choi, G.H.; Baldwin, E.T.
Crystallisation and preliminary X-ray analysis of UDP-N-acetylenolpyruvylglucosamine reductase (MurB) from Staphylococcus aureus
Acta Crystallogr. Sect. D
57
1032-1035
2001
Staphylococcus aureus
Matsuo, M.; Kurokawa, K.; Nishida, S.; Li, Y.; Takimura, H.; Kaito, C.; Fukuhara, N.; Maki, H.; Miura, K.; Murakami, K.; Sekimizu, K.
Isolation and mutation site determination of the temperature-sensitive murB mutants of Staphylococcus aureus
FEMS Microbiol. Lett.
222
107-113
2003
Staphylococcus aureus (Q54A20), Staphylococcus aureus
Nishida, S.; Kurokawa, K.; Matsuo, M.; Sakamoto, K.; Ueno, K.; Kita, K.; Sekimizu, K.
Identification and characterization of amino acid residues essential for the active site of UDP-N-acetylenolpyruvylglucosamine reductase (MurB) from Staphylococcus aureus
J. Biol. Chem.
281
1714-1724
2006
Staphylococcus aureus (P61431), Staphylococcus aureus
Gilbert, A.M.; Failli, A.; Shumsky, J.; Yang, Y.; Severin, A.; Singh, G.; Hu, W.; Keeney, D.; Petersen, P.J.; Katz, A.H.
Pyrazolidine-3,5-diones and 5-hydroxy-1H-pyrazol-3(2H)-ones, inhibitors of UDP-N-acetylenolpyruvyl glucosamine reductase
J. Med. Chem.
49
6027-6036
2006
Candida albicans, Streptococcus pneumoniae, Escherichia coli, Enterococcus faecalis, Staphylococcus aureus, Staphylococcus aureus GC 1131, Escherichia coli GC 4560 imp, Streptococcus pneumoniae GC 1894, Enterococcus faecalis GC 2242
Kim, M.; Cho, M.K.; Song, H.; Kim, D.; Park, B.; Lee, J.H.; Kang, G.B.; Kim, S.H.; Im, Y.J.; Lee, D.; Eom, S.H.
Crystal structure of UDP-N-acetylenolpyruvylglucosamine reductase (MurB) from Thermus caldophilus
Proteins
66
751-754
2007
Thermus caldophilus (Q5SJC8), Thermus caldophilus
Babajan, B.; Anuradha, C.; Chaitanya, M.; Gowsia, D.; Kumar, C.
In silico structural characterization of Mycobacterium tuberculosis H37Rv UDP-N-acetylmuramate dehydrogenase
Int. J. Integr. Biol.
6
12-16
2009
Mycobacterium tuberculosis, Mycobacterium tuberculosis (B5AFK3), Mycobacterium tuberculosis H37Rv (B5AFK3)
-
Gautam, A.; Shukla, H.; Khan, S.; Rishi, P.; Bhakuni, V.; Tewari, R.
Structural and functional features of UDP-N-acetylenolpyruvylglucosamine reductase of Mycobacterium tuberculosis H37Rv
Int. J. Integr. Biol.
10
66-75
2010
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
-
Shapiro, A.B.; Livchak, S.; Gao, N.; Whiteaker, J.; Thresher, J.; Jahic, H.; Huang, J.; Gu, R.F.
A homogeneous, high-throughput-compatible, fluorescence intensity-based assay for UDP-N-acetylenolpyruvylglucosamine reductase (MurB) with nanomolar product detection
J. Biomol. Screen.
17
327-338
2012
Escherichia coli
Kumar, V.; Saravanan, P.; Arvind, A.; Mohan, C.G.
Identification of hotspot regions of MurB oxidoreductase enzyme using homology modeling, molecular dynamics and molecular docking techniques
J. Mol. Model.
17
939-953
2011
Mycobacterium tuberculosis (P9WJL9), Mycobacterium tuberculosis H37Rv (P9WJL9)
Naqvi, K.F.; Patin, D.; Wheatley, M.S.; Savka, M.A.; Dobson, R.C.; Gan, H.M.; Barreteau, H.; Blanot, D.; Mengin-Lecreulx, D.; Hudson, A.O.
Identification and partial characterization of a novel UDP-N-acetylenolpyruvoylglucosamine reductase/UDP-N-acetylmuramate L-alanine ligase fusion enzyme from Verrucomicrobium spinosum DSM 4136(T)
Front. Microbiol.
7
362
2016
Verrucomicrobium spinosum, Verrucomicrobium spinosum DSM 4136
Videau, P.; Rivers, O.S.; Ushijima, B.; Oshiro, R.T.; Kim, M.J.; Philmus, B.; Cozy, L.M.
Mutation of the murC and murB genes impairs heterocyst differentiation in Anabaena sp. strain PCC 7120
J. Bacteriol.
198
1196-1206
2016
Anabaena sp. (Q8YM74), Anabaena sp. PCC 7120 (Q8YM74)
Chen, M.W.; Lohkamp, B.; Schnell, R.; Lescar, J.; Schneider, G.
Substrate channel flexibility in Pseudomonas aeruginosa MurB accommodates Two distinct substrates
PLoS ONE
8
e66936
2013
Pseudomonas aeruginosa (Q9HZM7)
Isa, M.; Mohammed, M.
Molecular docking and dynamic simulation of UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) obtained from Mycobacterium tuberculosis using in silico approach
Netw. Model. Anal. Health Inform. Bioinform.
10
40
2021
Mycobacterium tuberculosis (P9WJL9), Mycobacterium tuberculosis H37Rv (P9WJL9)
-
html completed
