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Information on EC 1.3.1.98 - UDP-N-acetylmuramate dehydrogenase and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC1.3.1.98

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IUBMB Comments

A flavoprotein (FAD). NADH can to a lesser extent replace NADPH.

The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

Synonyms
udp-n-acetylenolpyruvylglucosamine reductase, udp-n-acetylenolpyruvoylglucosamine reductase, murbab, udp-n-acetylenolpyruvyl glucosamine reductase, more

SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
reductase, uridine diphosphoacetylpyruvoylglucosamine
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type I UNAGEP reductase
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UDP-GlcNAc-enoylpyruvate reductase
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UDP-N-acetylenolpyruvoylglucosamine reductase
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UDP-N-acetylglucosamine-enoylpyruvate reductase
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UDP-N-acetylmuramate dehydrogenase
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UNAGEP reductase
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uridine diphospho-N-acetylglucosamine-enolpyruvate reductase
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uridine-5'-diphospho-N-acetyl-2-amino-2-deoxy-3-O-lactylglucose:NADP-oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-muramate + NADP+ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH + H+
show the reaction diagram
the nicotinamide ring of NADP+ stacks against the si face of the isoalloxazine ring of FAD, suggesting an unusual mode of hydride transfer to flavin. Both substrates share the binding site located between two lobes of the substrate-binding domain III, consistent with a ping pong mechanism with sequential substrate binding, structural analysis of the first half-reaction, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
MetaCyc
peptidoglycan recycling I, UDP-N-acetylmuramoyl-pentapeptide biosynthesis I (meso-diaminopimelate containing), UDP-N-acetylmuramoyl-pentapeptide biosynthesis II (lysine-containing), UDP-N-acetylmuramoyl-pentapeptide biosynthesis III (meso-diaminopimelate containing)
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-muramate:NADP+ oxidoreductase
A flavoprotein (FAD). NADH can to a lesser extent replace NADPH.
CAS REGISTRY NUMBER
COMMENTARY hide
39307-28-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY hide
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH + H+
UDP-N-acetyl-alpha-D-muramate + NADP+
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY hide
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH + H+
UDP-N-acetyl-alpha-D-muramate + NADP+
show the reaction diagram
Substrates: -
Products: -
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
binding structure, overview
NADPH
binding structure, overview. Hydride transfer occurs via the isoalloxazine si face
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
PaMurB crystal structure contains a potassium ion in the active site. The potassium ion displays a pentagonal bipyramidal coordination geometry with two main chain oxygen atoms (Ala237, Ser239), one side chain carboxyl oxygen atom from Glu-335, one side chain oxygen atom of Asn-57 and the O7n oxygen atom of the nicotinamide ring as ligands. The potassium ion activates MurB by facilitating substrate orientation and binding
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Gene Links
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A0C6EEM9_PSEAI
339
0
37570
TrEMBL
-
A0A241XUT4_PSEAI
339
0
37658
TrEMBL
-
A0A3S3X2B8_PSEAI
339
0
37598
TrEMBL
-
A0A509JP64_PSEAI
339
0
37628
TrEMBL
Secretory Pathway (Reliability: 5)
A0A544S9V3_PSEAI
339
0
37628
TrEMBL
-
A0A643ELM4_PSEAI
339
0
37628
TrEMBL
-
A0A643IZ31_PSEAI
339
0
37687
TrEMBL
-
A0A6A9JVQ7_PSEAI
339
0
37426
TrEMBL
-
A0A7M3A3C3_PSEAI
339
0
37517
TrEMBL
other Location (Reliability: 1)
A0AAQ3R3D4_PSEAI
339
0
37598
TrEMBL
-
A0ABD7K5A6_PSEAI
339
0
37390
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
three-dimensional structure analysis and comparison, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme MurB complexed with FAD and NADP+ in two crystal forms, hanging drop vapour diffusion method, for crystal type A: mixing of 0.001 ml of protein solution containing 25 mg/ml PaMurB, and 2 mM unbuffered NADPH, with 0.001 ml of reservoir solution containing 0.1 M Bis-Tris propane, pH 7.0, 0.2 M sodium potassium tartrate, and 15% w/v PEG 3350, and equilibration against 0.5 ml reservoir solution, crystals from these drops are cryoprotected with a solution containing additional 15% w/v PEG3350 and 2 mM NADPH before flash freezing, for crystal type B: the protein is mixed with a reservoir solution containing 40 mM potassium phosphate, 20% v/v glycerol, 16% w/v PEG 8000 and 2 mM Tris-buffered NADP+ sodium salt, the crystals are frozen directly without addition of a cryoprotectant, X-ray diffraction structure determination and analysis at 2.2 A and 2.1 A resolution, respectively, molecular replacement using the atomic coordinates of the complex of Escherichia coli MurB with UDP-N-acetylglucosamine enolpyruvate, PDB code 2MBR, stripped of all ligands and water molecules as search model, modeling
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage by TEV protease, followed by a second step of affinity chromatography to remove uncleaved protein and the His6-tagged TEV protease, further purification by preparation scale gel filtration, and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene murB, recombinant expression of N-terminally His6-tagged enzyme, harboring a TEV protease cleavage site, in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team