4.4.1.3: dimethylpropiothetin dethiomethylase

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For detailed information about dimethylpropiothetin dethiomethylase, go to the full flat file.

Reaction

Synonyms

DddL lyase, dddP, DddQ, DddW, Dddy, desulfhydrase, dethiomethylase, dimethylpropiothetin, dimethylsulfoniopropionate lyase, DLA, DMSP, DMSP lyase, DMSP-lyase, F963_02809, SAMN05660830_03106, SL1157_2466

ECTree

     4 Lyases

         4.4 Carbon-sulfur lyases

             4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date)

                4.4.1.3 dimethylpropiothetin dethiomethylase

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Results	in table
5	Activating Compound
115	AA Sequence
1	CAS Registry Number
14	Cloned(Commentary)
3	Crystallization (Commentary)
4	Expression
4	General Information
19	Inhibitors
22	kcat/KM [mM/s]
30	KM Value [mM]
4	Localization
12	Metals/Ions
7	Molecular Weight [Da]
17	Natural Substrates/ Products (Substrates)
79	Organism
4	Pathway
6	PDB ID
9	pH Optimum
3	pH Range
15	Protein Variants
5	Purification (Commentary)
3	Reaction
1	Reaction Type
61	Reference
6	Specific Activity [micromol/min/mg]
1	Storage Stability
84	Substrates and Products (Substrate)
6	Subunits
76	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
1	Temperature Stability [°C]
23	Turnover Number [1/s]

Crystallization

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Crystallization on EC 4.4.1.3 - dimethylpropiothetin dethiomethylase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

to 1.5 A resolution. DddY contains a cap domain and a catalytic domain with a Zn2+ bound at its active site. Residues His265, Glu269, His338 and the acetate molecule participate in coordinating Zn2+. The DddY catalytic domain adopts a typical beta-barrel fold and contains two conserved cupin motifs. In the catalytic mechanism, residue Tyr271 acts as a general base to attack DMSP

Acinetobacter bereziniae

N8X9V6

748399

in complex with Fe(III) and substrate dimethylsulfoniopropionate, to 2.0-2.5 A resolution. The enzyme undergoes conformational changes upon substrate-binding. The substrate is positioned optimally to bind iron and is in the proximity of Tyr120 that acts as a Lewis base to initiate catalysis

Ruegeria lacuscaerulensis

D0CY60

747110

wild-type in complex with inhibitor 2-(N-morpholino)ethanesulfonic acid or PO43-, to 2.1 A resolution, and mutants Y366A and D377N bound to acrylate

Ruegeria lacuscaerulensis

D0CY07

748685