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

BRENDA support

1.5.8.4: dimethylglycine dehydrogenase

This is an abbreviated version!
For detailed information about dimethylglycine dehydrogenase, go to the full flat file.

Word Map on EC 1.5.8.4

Reaction

N,N-dimethylglycine
+
5,6,7,8-tetrahydrofolate
 +
electron-transfer flavoprotein
=
sarcosine
 +
5,10-methylenetetrahydrofolate
 +
reduced electron-transfer flavoprotein

Synonyms

Csal_0990, DdhC, DMGDH, EC 1.5.99.2, Me2GlyDH, mMe2GlyDH, N,N-dimethylglycine oxidase, pMe2GlyDH

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.8 With a flavin or flavoprotein as acceptor
                1.5.8.4 dimethylglycine dehydrogenase

Crystallization

Crystallization on EC 1.5.8.4 - dimethylglycine dehydrogenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of the wild-type enzyme and determination of the structure to 3.1A resolution, microbatch method using different commercial crystallization screens
microbatch method using 10% (w/v) PEG 20000 and 20% (v/v) PEG MME 550
wild-type, to 3.1 resolution
crystal structure of the recombinant mature and precursor forms of enzyme and the enzyme complexed with 5,6,7,8-tetrahydrofolate. Both forms reveal similar kinetic parameters and have the same tertiary structure fold with two domains formed by N- and C-terminal halves of the protein. The active center is located in the N-terminal domain while the tetrahydrofolate binding site is located in the C-terminal domain about 40 A from the isoalloxazine ring of FAD. The folate binding site is connected with the enzyme active center via an intramolecular channel. This suggests the possible transfer of the intermediate imine of dimethylglycine from the active center to the bound 5,6,7,8-tetrahydrofolate where they can react producing a 5,10-methylenetetrahydrofolate
recombinant mature and precursor forms, in complex with tetrahydrofolate. Both forms of DMGDH reveal similar kinetic parameters and have the same tertiary structure fold with two domains formed by N- and C-terminal halves of the protein. The active center is located in the N-terminal domain while the THF binding site is located in the C-terminal domain about 40 A from the isoalloxazine ring of FAD. The folate binding site is connected with the enzyme active center via an intramolecular channel
using 0.2 M K/Na-tartrate-20% (w/v) PEG 3350 for the mature enzyme or 0.2 M NaSCN-20% (w/v) PEG 3350-0.1 M Tris pH 7.5 for the precursor