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4.1.1.50: adenosylmethionine decarboxylase

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

Word Map on EC 4.1.1.50

Reaction

S-adenosyl-L-methionine
=
S-adenosyl 3-(methylsulfanyl)propylamine
 +
CO2

Synonyms

Ado-MetDC, AdoMet decarboxylase, AdoMetDC, AdoMetDC/ODC, AMDC, BjSAMDC1, BjSAMDC2, BjSAMDC3, BjSAMDC4, BlsE, Bud2, MdSAMDC1, MdSAMDC2, OsSAMDC, PfAdoMetDC, protein SSO0585, S-adenosyl methionine decarboxylase, S-Adenosyl-L-methionine decarboxylase, S-adenosyl-methionine-decarboxylase, S-adenosylmethionine decarboxy-lase/ornithine decarboxylase, S-Adenosylmethionine decarboxylase, S-adenosylmethionine decarboxylase 1, S-adenosylmethionine decarboxylase 2, S-adenosylmethionine decarboxylase 3, S-adenosylmethionine decarboxylase 4, SAM decarboxylase, SAM-DC, SAMDC, SvPEPC, Tb927.6.4410

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.50 adenosylmethionine decarboxylase

Crystallization

Crystallization on EC 4.1.1.50 - adenosylmethionine decarboxylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
AdoMetDC F223A mutant complexed with S-adenosylmethionine and the wild type protein complexed with several substituted inhibitors, hanging drop vapor diffusion method, at 22°C in 13-16% PEG 8000, 100 mM Tris, pH 8.0-9.0, and 10 mM dithiothreitol
cocrystallized with 5'-deoxy-5'-dimethylthioadenosine and 5'-deoxy-5'-(N-dimethyl)amino-8-methyladenosine, hanging drop vapor diffusion method, at 22°C in 13-16% (w/v) polyethylene glycol 8000, 100 mM tris(hydroxymethyl)aminomethane (pH 8.0-9.0), and 10 mM dithiothreitol
docking of inhibitor 2-amino-3-[(E)-(2-fluorophenyl)diazenyl]-4,5,6,7-tetrahydro-8H-cyclopenta[d]pyrazolo[1,5-a]pyrimidin-8-one, compound binds the enzyme with interactions similar to known inhibitors. The major interactions are the ring-ring stacking interactions with Phe7 and Phe223, the polar interactions with the side-chain or main-chain atoms of Leu65, Ser68, Glu67, Asn224, and Cys226
-
in complex with different inhibitors and with a substrate analogue
hanging drop vapour diffusion method, structures of the wild-type proenzyme and the S63A mutant at 1.55 A and 1.7 A resolution
-
in complexes with S-adenosylmethionine methyl ester and 5'-deoxy-5'-dimethylthioadenosine, hanging drop vapor diffusion method, using 2.4-2.8 M ammonium formate and 100 mM HEPES pH 8.0
structure of proenzyme in complex with putrescine and inhibitor N4-(3,5-dibromophenyl)-6-methylpyrimidine-2,4-diamine
molecular modeling using enzymes from Solanum tuberosum and Homo sapiens as templates