KEGG   ENZYME: 4.2.1.141Help
Entry
EC 4.2.1.141                Enzyme                                 

Name
2-dehydro-3-deoxy-D-arabinonate dehydratase
Class
Lyases;
Carbon-oxygen lyases;
Hydro-lyases
BRITE hierarchy
Sysname
2-dehydro-3-deoxy-D-arabinonate hydro-lyase (2,5-dioxopentanoate-forming)
Reaction(IUBMB)
2-dehydro-3-deoxy-D-arabinonate = 2,5-dioxopentanoate + H2O [RN:R09186]
Reaction(KEGG)
Substrate
2-dehydro-3-deoxy-D-arabinonate [CPD:C03826]
Product
2,5-dioxopentanoate [CPD:C00433];
H2O [CPD:C00001]
Comment
The enzyme participates in pentose oxidation pathways that convert pentose sugars to the tricarboxylic acid cycle intermediate 2-oxoglutarate.
History
EC 4.2.1.141 created 2013
Pathway
ec00040  Pentose and glucuronate interconversions
Orthology
K14259  2-dehydro-3-deoxy-D-arabinonate dehydratase
Genes
PSU: Psesu_2921
PSUW: WQ53_05940
SCL: sce8243(faa)
SCU: SCE1572_47080
BCL: ABC1112
BMEG: BG04_4038
BEO: BEH_11885
BMUR: ABE28_011530
GKA: GK1967
GTM: GT3921_09715
GTN: GTNG_1866
PMW: B2K_12085
SBH: SBI_09206
SMAL: SMALA_0412
BCV: Bcav_0314
KFL: Kfla_6633
GOB: Gobs_0128
AMD: AMED_6194
AMN: RAM_31775
AMM: AMES_6104
AMZ: B737_6104
AFS: AFR_12580
RXY: Rxyl_0545
TRO: trd_1918
TTR: Tter_0269
OTE: Oter_2671
RBA: RB8851(hpaG)
PSL: Psta_0399
PLM: Plim_2320
IPA: Isop_2260
SACI: Sinac_2247
ACA: ACP_0198
SUS: Acid_0967
FLN: FLA_2805
MUC: MuYL_3112
DFE: Dfer_3859
SLI: Slin_1198
LBY: Lbys_1449
FAE: FAES_1942
PSEZ: HME7025_01774(kdxD)
HMA: rrnAC1339
HHI: HAH_1926
HVO: HVO_B0027(xacE)
HLA: Hlac_2243
SSO: SSO3118
SOL: Ssol_0860
SSOA: SULA_0896
SSOL: SULB_0898
SSOF: SULC_0897
SAI: Saci_1939
SID: M164_2246
SII: LD85_2519
SIH: SiH_2188
SIR: SiRe_2129
SIC: SiL_2093
CMA: Cmaq_0259
VMO: VMUT_1239
 » show all
Taxonomy
Reference
1  [PMID:16849334]
  Authors
Brouns SJ, Walther J, Snijders AP, van de Werken HJ, Willemen HL, Worm P, de Vos MG, Andersson A, Lundgren M, Mazon HF, van den Heuvel RH, Nilsson P, Salmon L, de Vos WM, Wright PC, Bernander R, van der Oost J
  Title
Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment.
  Journal
J Biol Chem 281:27378-88 (2006)
DOI:10.1074/jbc.M605549200
  Sequence
[sso:SSO3118]
Reference
2  [PMID:18448118]
  Authors
Brouns SJ, Barends TR, Worm P, Akerboom J, Turnbull AP, Salmon L, van der Oost J
  Title
Structural insight into substrate binding and catalysis of a novel 2-keto-3-deoxy-D-arabinonate dehydratase illustrates common mechanistic features  of the FAH superfamily.
  Journal
J Mol Biol 379:357-71 (2008)
DOI:10.1016/j.jmb.2008.03.064
  Sequence
[sso:SSO3118]
Reference
3  [PMID:19584053]
  Authors
Johnsen U, Dambeck M, Zaiss H, Fuhrer T, Soppa J, Sauer U, Schonheit P.
  Title
D-xylose degradation pathway in the halophilic archaeon Haloferax volcanii.
  Journal
J Biol Chem 284:27290-303 (2009)
DOI:10.1074/jbc.M109.003814
  Sequence
[hvo:HVO_B0027]
Other DBs
ExplorEnz - The Enzyme Database: 4.2.1.141
IUBMB Enzyme Nomenclature: 4.2.1.141
ExPASy - ENZYME nomenclature database: 4.2.1.141
BRENDA, the Enzyme Database: 4.2.1.141

DBGET integrated database retrieval system