Q53353 · LSDX1_SPHPI
- ProteinLignostilbene-alpha,beta-dioxygenase isozyme I
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids485 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the cleavage of the interphenyl double bond (C alpha-C beta) of lignin-derived polyphenolic diaryl-propane type compounds (Stilbene).
Catalytic activity
- 1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene + O2 = 2 vanillin
Cofactor
Note: 1 Fe2+ ion per subunit.
Activity regulation
Activity is high with beta-1 type stilbene and minimal with beta-5 type stilbene. A 4-hydroxyl group and trans-stilbene structure is essential for the binding of substrates to the enzyme. Inhibited by N-benzylideneaniline-hydroxy and -methoxy derivatives and N-(4-hydroxybenzyl)-3-methoxyaniline but not N-benzylideneaniline. Fluorinated olefin (Z)-1-fluoro-1(4-hydroxyphenyl)-2-phenylethylene is also a potent inhibitor. Imine linkage instead of ethylene bridge in the substrate enhances the inhibitory activity.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
11 μM | 1,2-bis(4-hydroxy-3-methoxyphenyl)-ethylene | |||||
110 μM | oxygen | |||||
8.3 μM | 4-hydroxystilbene |
pH Dependence
Optimum pH is 8.5. Active from 5.5-10.5.
Temperature Dependence
Optimum temperature is 30 degrees Celsius. Stable at 4 degrees Celsius with minimal loss of activity.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | carotenoid dioxygenase activity | |
Molecular Function | iron ion binding | |
Molecular Function | lignostilbene alpha beta-dioxygenase activity | |
Biological Process | carotene catabolic process | |
Biological Process | lignin catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLignostilbene-alpha,beta-dioxygenase isozyme I
- EC number
- Short namesLSD-I
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingomonas
Accessions
- Primary accessionQ53353
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000416940 | 2-485 | Lignostilbene-alpha,beta-dioxygenase isozyme I | |||
Sequence: AHFPQTPGFSGTLRPLRIEGDILDIEIEGEVPPQLNGTFHRVHPDAQFPPRFEDDQFFNGDGMVSLFRFHDGKIDFRQRYAQTDKWKVERKAGKSLFGAYRNPLTDDASVQGMIRGTANTNVMVHAGKLYAMKEDSPCLIMDPLTLETEGYTNFDGKLQSQTFCAHPKIDPVTGNLCAFAYGAKGLMTLDMAYIEISPTGKLLKEIPFQNPYYCMMHDFGVTEDYAVFAVMPLLSSWDRLEQRLPFFGFDTTLPCYLGILPRNGDARDLRWFKTGNCFVGHVMNAFNDGTKVHIDMPVSRNNSFPFFDVHGAPFDPVAGQGFLTRWTVDMASNGDSFEKTERLFDRPDEFPRIDERYATRAYRHGWMLILDTEKPYEAPGGAFYALTNTLGHIDLATGKSSSWWAGPRCAIQEPCFIPRSPDAPEGDGYVIALVDDHVANYSDLAIFDAQHVDQGPIARAKLPVRIRQGLHGNWADASRLAVAA |
Interaction
Subunit
Homodimer of two alpha subunits.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length485
- Mass (Da)54,436
- Last updated1996-11-01 v1
- Checksum71A672E375D29A1C
Keywords
- Technical term