1.1.1.336: UDP-N-acetyl-D-mannosamine dehydrogenase
This is an abbreviated version!
For detailed information about UDP-N-acetyl-D-mannosamine dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.336
-
1.1.1.336
-
2-epimerase
-
polysaccharide
-
pyrococcus
-
enterobacterial
-
transposon
-
udp-n-acetylglucosamine
-
uridylyltransferase
-
horikoshii
-
diagnostics
- 1.1.1.336
-
2-epimerase
- polysaccharide
-
pyrococcus
-
enterobacterial
- transposon
- udp-n-acetylglucosamine
-
uridylyltransferase
- horikoshii
- diagnostics
Reaction
Synonyms
MMP0706, UDP-D-ManNAcDH, UDP-ManNAc 6-dehydrogenase, WbpA, wbpA2, wbpA_2, wecC
ECTree
Advanced search results
Crystallization
Crystallization on EC 1.1.1.336 - UDP-N-acetyl-D-mannosamine dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
crystal structure of the enzyme bound to the product UDP-N-acetyl-alpha-D-mannosaminuronate by X-ray diffraction to resolution of 1.55 A. Crystal structures reveal a tight dimeric polymer chains with product-bound in all the structures. The catalytic residues Cys258 and Lys204 are conserved. The Cys258 acts as catalytic nucleophile and Lys204 as acid/base catalyst. The product directly interacts with residues Arg211, Thr249, Arg244, Gly255, Arg289, Lys319 and Arg398. The SeMet-substituted enzyme is crystallized using microbatch sitting method under reservoir solution condition 10% (w/v) PEG 8000, 8% (v/v) ethylene glycol and 0.1 M HEPES, pH 7.5
-