KEGG   ENZYME: 1.13.11.50
Entry
EC 1.13.11.50               Enzyme                                 
Name
acetylacetone-cleaving enzyme;
Dke1;
acetylacetone dioxygenase;
diketone cleaving dioxygenase;
diketone cleaving enzyme
Class
Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of two atoms of oxygen
Sysname
acetylacetone:oxygen oxidoreductase
Reaction(IUBMB)
pentane-2,4-dione + O2 = acetate + 2-oxopropanal [RN:R07183]
Reaction(KEGG)
R07183
Substrate
pentane-2,4-dione [CPD:C15499];
O2 [CPD:C00007]
Product
acetate [CPD:C00033];
2-oxopropanal [CPD:C00546]
Comment
An iron(II)-dependent enzyme. Forms the first step in the acetylacetone degradation pathway of Acinetobacter johnsonii. While acetylacetone is by far the best substrate, heptane-3,5-dione, octane-2,4-dione, 2-acetylcyclohexanone and ethyl acetoacetate can also act as substrates.
History
EC 1.13.11.50 created 2003
Orthology
K20148  acetylacetone-cleaving enzyme
Genes
PMED: E3Z27_09540
PSEP: C4K39_2447
BURT: BTHE68_39430
BXE: Bxe_A2876
BXB: DR64_557(dke1)
BPX: BUPH_08490
BUZ: AYM40_26235
PDIO: PDMSB3_1622(dke)
PPAI: E1956_29755
CABA: SBC2_46810(dke1)
RHY: RD110_03340
AAV: Aave_3966
MPT: Mpe_A3659
METP: C1M51_08180
ALH: G6N82_04105
TMO: TMO_b0515(dke1)
 » show all
Reference
1  [PMID:12379146]
  Authors
Straganz GD, Glieder A, Brecker L, Ribbons DW, Steiner W
  Title
Acetylacetone-cleaving enzyme Dke1: a novel C-C-bond-cleaving enzyme from Acinetobacter johnsonii.
  Journal
Biochem J 369:573-81 (2003)
DOI:10.1042/BJ20021047
  Sequence
[ag:AAN45859]
Other DBs
ExplorEnz - The Enzyme Database: 1.13.11.50
IUBMB Enzyme Nomenclature: 1.13.11.50
ExPASy - ENZYME nomenclature database: 1.13.11.50
BRENDA, the Enzyme Database: 1.13.11.50
CAS: 524047-53-8

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Gene (207)   
   MGENES (207)   
Protein sequence (19)   
   UniProt (14)   
   SWISS-PROT (1)   
   PDBSTR (4)   
DNA sequence (12)   
   GenBank (6)   
   EMBL (6)   
3D Structure (1)   
   PDB (1)   
Protein domain (3)   
   InterPro (3)   
All databases (242)   

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