4.3.99.4: choline trimethylamine-lyase

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For detailed information about choline trimethylamine-lyase, go to the full flat file.

Reaction

Synonyms

choline TMA-lyase, cutC, Dde_3282, glycyl radical enzyme

ECTree

     4 Lyases

         4.3 Carbon-nitrogen lyases

             4.3.99 Other carbon-nitrogen lyases

                4.3.99.4 choline trimethylamine-lyase

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Results	in table
1	Activating Compound
684	AA Sequence
3	Cloned(Commentary)
2	Crystallization (Commentary)
8	General Information
5	KM Value [mM]
1	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
14	Organism
3	Pathway
22	PDB ID
2	pH Optimum
21	Protein Variants
2	Purification (Commentary)
3	Reaction
9	Reference
1	Specific Activity [micromol/min/mg]
14	Substrates and Products (Substrate)
3	Subunits
18	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
6	Turnover Number [1/s]

Crystallization

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Crystallization on EC 4.3.99.4 - choline trimethylamine-lyase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

sitting drop method, crystal structures of both the choline-bound and choline free forms of CutC are determined, binding of choline at the ligand-binding site triggers conformational changes in the enzyme structure. Choline-bound CutC crystals exhibit an orthorhombic lattice and space group P212121 with 8 molecules in the asymmetric unit. CutC crystals without choline exhibited a monoclinic lattice and space group P21 with 4 molecules in the asymmetric unit

Klebsiella pneumoniae

A0A0M3KL45

748194

optimized crystals are grown using hanging drop vapor diffusion at 21°C

Oleidesulfovibrio alaskensis

Q30W70

747482