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.

Reaction

Synonyms

MMP0706, UDP-D-ManNAcDH, UDP-ManNAc 6-dehydrogenase, WbpA, wbpA2, wbpA_2, wecC

ECTree

     1 Oxidoreductases

         1.1 Acting on the CH-OH group of donors

             1.1.1 With NAD⁺ or NADP⁺ as acceptor

                1.1.1.336 UDP-N-acetyl-D-mannosamine dehydrogenase

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Results	in table
4	Activating Compound
5595	AA Sequence
1	Application
4	Cloned(Commentary)
3	Cofactor
2	Crystallization (Commentary)
7	General Information
5	Inhibitors
5	KM Value [mM]
2	Metals/Ions
7	Molecular Weight [Da]
2	Natural Substrates/ Products (Substrates)
52	Organism
6	Pathway
1	pH Optimum
1	Protein Variants
2	Purification (Commentary)
1	Reaction
11	Reference
1	Source Tissue
1	Storage Stability
5	Substrates and Products (Substrate)
6	Subunits
13	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
1	Turnover Number [1/s]

Crystallization

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Crystallization on EC 1.1.1.336 - UDP-N-acetyl-D-mannosamine dehydrogenase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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

Pyrococcus horikoshii

-

729151

to 1.8 A resolution, space group P21

Pyrococcus horikoshii

O59284

718489