4.4.1.3: dimethylpropiothetin dethiomethylase
This is an abbreviated version!
For detailed information about dimethylpropiothetin dethiomethylase, go to the full flat file.
Word Map on EC 4.4.1.3
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4.4.1.3
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h2s
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dimethylsulfide
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phytoplankton
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lyases
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hypotaurine
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roseobacter
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o-acetylserine
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ruegeria
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d-cysteine
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cupin
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rhodobacteraceae
- 4.4.1.3
- h2s
- dimethylsulfide
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phytoplankton
- lyases
- hypotaurine
- roseobacter
- o-acetylserine
- ruegeria
- d-cysteine
-
cupin
- rhodobacteraceae
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
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General Information
General Information on EC 4.4.1.3 - dimethylpropiothetin dethiomethylase
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physiological function
comparison of DMSP lyases and lyase-like enzymes. Two conserved sequence motifs of the superfamily include the metal-ligating residues that are absolutely essential and other residues including an active site tyrosine that seems to play a relatively minor role in DMSP lysis
physiological function
comparison of DMSP lyases and lyase-like enzymes. Two conserved sequence motifs of the superfamily include the metal-ligating residues that are absolutely essential and other residues including an active site tyrosine that seems to play a relatively minor role in DMSP lysis
physiological function
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DMSP decomposition employs a concerted beta-elimination mechanism, where the substrate alpha-proton abstraction by residue Asp377 is coupled with the Cbeta-S bond dissociation and Calpha-Cbeta double bond formation. The reaction proceeds without any Omy species bridging the two ferric ions, although an Omy bridging species is observed in the crystal structures. A neutral residue Lys419 may be more favorable for the catalysis than protonated Lys419
physiological function
-
DMSP decomposition employs a concerted beta-elimination mechanism, where the substrate alpha-proton abstraction by residue Asp377 is coupled with the Cbeta-S bond dissociation and Calpha-Cbeta double bond formation. The reaction proceeds without any Omy species bridging the two ferric ions, although an Omy bridging species is observed in the crystal structures. A neutral residue Lys419 may be more favorable for the catalysis than protonated Lys419
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