Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

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
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
A flavoprotein (FAD). NADH can to a lesser extent replace NADPH.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Pseudomonas aeruginosa
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
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
-
-
-
-
type I UNAGEP reductase
-
UDP-GlcNAc-enoylpyruvate reductase
-
-
-
-
UDP-N-acetylenolpyruvoylglucosamine reductase
-
-
-
-
UDP-N-acetylglucosamine-enoylpyruvate reductase
-
-
-
-
UDP-N-acetylmuramate dehydrogenase
-
-
-
-
UNAGEP reductase
-
uridine diphospho-N-acetylglucosamine-enolpyruvate reductase
-
-
-
-
uridine-5'-diphospho-N-acetyl-2-amino-2-deoxy-3-O-lactylglucose:NADP-oxidoreductase
-
-
-
-
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
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
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
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
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
-
-
-
?
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A643IZ31_PSEAI
339
0
37687
TrEMBL
-
A0A8G7AI86_PSEAI
339
0
37658
TrEMBL
-
A0A8G3DD73_PSEAI
339
0
37619
TrEMBL
-
A0A7U0K3E6_PSEAI
339
0
37598
TrEMBL
-
A0A8F9NPC7_PSEAI
339
0
37614
TrEMBL
-
A0A431XCJ3_PSEAI
339
0
37390
TrEMBL
-
A0A509JP64_PSEAI
339
0
37628
TrEMBL
-
A0A8G6GMU1_PSEAI
339
0
37590
TrEMBL
-
A0A241XUT4_PSEAI
339
0
37658
TrEMBL
-
A0A0C6EEM9_PSEAI
339
0
37570
TrEMBL
-
A0A2R3IYF3_PSEAI
339
0
37359
TrEMBL
-
A0A8G7BW22_PSEAI
339
0
37683
TrEMBL
-
A0A8G5VZL5_PSEAI
339
0
37697
TrEMBL
-
A0A8G2Z3E7_PSEAI
339
0
37705
TrEMBL
-
A0A8G4ECB4_PSEAI
339
0
37575
TrEMBL
-
A0A5K1SPR3_PSEAI
339
0
37560
TrEMBL
-
A0A8G4AS38_PSEAI
339
0
37540
TrEMBL
-
A0A4P0UEQ5_PSEAI
121
0
13095
TrEMBL
-
A0A6A9JVQ7_PSEAI
339
0
37426
TrEMBL
-
A0A8G5ZZD2_PSEAI
339
0
37602
TrEMBL
-
A0A544S9V3_PSEAI
339
0
37628
TrEMBL
-
A0A7M3A3C3_PSEAI
339
0
37517
TrEMBL
-
A0A080VIE4_PSEAI
339
0
37647
TrEMBL
-
A0A8F9Y8P2_PSEAI
339
0
37617
TrEMBL
-
A0A8G7LUX8_PSEAI
339
0
37628
TrEMBL
-
A0A3S3X2B8_PSEAI
339
0
37598
TrEMBL
-
A0A643ELM4_PSEAI
339
0
37628
TrEMBL
-
A0A8G7RND8_PSEAI
339
0
37518
TrEMBL
-
A0A8G7DLC9_PSEAI
339
0
37570
TrEMBL
-
A0A8F9JRJ5_PSEAI
339
0
37542
TrEMBL
-
A0A8G4DH47_PSEAI
339
0
37594
TrEMBL
-
A0A8G2VRX5_PSEAI
339
0
37501
TrEMBL
-
A0A8G4Z9T8_PSEAI
339
0
37517
TrEMBL
-
A0A8G4RAJ8_PSEAI
339
0
37686
TrEMBL
-
A0A8G3FNK4_PSEAI
339
0
37512
TrEMBL
-
A0A8H0X763_PSEAI
339
0
37570
TrEMBL
-
A0A8G2VG03_PSEAI
339
0
37673
TrEMBL
-
A0A8G7CES3_PSEAI
339
0
37601
TrEMBL
-
A0A8B5ALH6_PSEAI
339
0
37575
TrEMBL
-
A0A8G5JFA1_PSEAI
339
0
37626
TrEMBL
-
A0A8G5RE96_PSEAI
339
0
37618
TrEMBL
-
A0A7M3B5J8_PSEAI
341
0
37867
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