KEGG   ENZYME: 4.1.1.77Help
Entry
EC 4.1.1.77                 Enzyme                                 

Name
2-oxo-3-hexenedioate decarboxylase;
4-oxalocrotonate carboxy-lyase (misleading);
4-oxalocrotonate decarboxylase (misleading);
cnbF (gene name);
praD (gene name);
amnE (gene name);
nbaG (gene name);
xylI (gene name)
Class
Lyases;
Carbon-carbon lyases;
Carboxy-lyases
BRITE hierarchy
Sysname
(3E)-2-oxohex-3-enedioate carboxy-lyase (2-oxopent-4-enoate-forming)
Reaction(IUBMB)
(3E)-2-oxohex-3-enedioate = 2-oxopent-4-enoate + CO2 [RN:R02602]
Reaction(KEGG)
R02602;
(other) R05374
Show
Substrate
(3E)-2-oxohex-3-enedioate
Product
2-oxopent-4-enoate [CPD:C00596];
CO2 [CPD:C00011]
Comment
Involved in the meta-cleavage pathway for the degradation of phenols, modified phenols and catechols. The enzyme has been reported to accept multiple tautomeric forms [1-4]. However, careful analysis of the stability of the different tautomers, as well as characterization of the enzyme that produces its substrate, EC 5.3.2.6, 2-hydroxymuconate tautomerase, showed that the actual substrate for the enzyme is (3E)-2-oxohex-3-enedioate [4].
History
EC 4.1.1.77 created 1999, modified 2011, modified 2012
Pathway
ec00362  Benzoate degradation
ec00621  Dioxin degradation
ec00622  Xylene degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K01617  2-oxo-3-hexenedioate decarboxylase
Genes
PGE: LG71_12235
SLQ: M495_05200
PSD: DSC_09165
PPSE: BN5_3617(nahK)
PCQ: PcP3B5_23510(amnE)
PPW: PputW619_2010
PPI: ND083(nahK)
PPJ: RK21_04234
PVR: PverR02_14695
PSC: A458_06505
PKC: PKB_3258(amne1) PKB_3606(amne3)
PSOS: POS17_2260
PSET: THL1_489
AVN: Avin_08680(xylI) Avin_30600(lapH)
AVL: AvCA_08680(xylI) AvCA_30600(lapH)
AVD: AvCA6_08680(xylI) AvCA6_30600(lapH)
ACX: Achr_32760(xylI)
SWD: Swoo_1406
SALH: HMF8227_02737(hpaH)
CYQ: Q91_0511
CYY: CPC19_10500(dmpH)
APAC: S7S_07005
TBN: TBH_C0931
CHRO: CXB49_03845(dmpH)
RSO: RSp0892
RSE: F504_4325
RPI: Rpic_4619
RIN: ACS15_4682(amnE)
REH: H16_B0549(h16_B0549)
CNC: CNE_2c04950(dmpH) CNE_BB1p11980(xylI) CNE_BB1p13270(dmpH)
RME: Rmet_1318(dmpH) Rmet_5210(amnE)
BCJ: BCAM2123
BCEN: DM39_4831(dmpH)
BCEO: I35_6005
BMUL: NP80_3871(amnE)
BCT: GEM_5400
BCED: DM42_4990(dmpH)
BCON: NL30_24585
BTEI: WS51_00575
BPSL: WS57_12150
BXE: Bxe_A1150(amnE)
BXB: DR64_3309(amnE)
BFN: OI25_254(amnE)
PARB: CJU94_37885(dmpH) CJU94_38130(dmpH)
PPNO: DA70_10725
PPNM: LV28_20330
PPUL: RO07_14670
PSPU: NA29_22520
PAPI: SG18_14500
BHZ: ACR54_00827(amnE)
AMIM: MIM_c06230
POL: Bpro_5137
AJS: Ajs_0225
VEI: Veis_2784
VBO: CKY39_28490(dmpH)
SIMP: C6571_13630(dmpH)
MELA: C6568_07845(dmpH)
JAG: GJA_235(dmpH)
LCH: Lcho_3342
DEY: HYN24_14125(dmpH) HYN24_14195(dmpH)
AZO: azo1854(lapH) azo2430(nahK)
THK: CCZ27_10765(dmpH) CCZ27_16280(dmpH)
ARC: ABLL_2441
MXA: MXAN_0925
CCX: COCOR_00872(dmpH)
ARA: Arad_7266
RLE: pRL120704
BRA: BRADO5041
BBT: BBta_5513
MET: M446_1050
MSL: Msil_1480
NAR: Saro_3851
SMAZ: LH19_00750
SGI: SGRAN_3551(amnE)
SPKC: KC8_11575
SJP: SJA_C1-11880(hpaH_xylI)
SINB: SIDU_08325
SHYD: CJD35_06495(dmpH)
MAGQ: MGMAQ_0652
BLI: BL03907
BLD: BLi03993(xylI)
BCA: BCE_2158
BCX: BCA_2156
BCF: bcf_10220
BCER: BCK_24215
BTL: BALH_1845
BMYC: DJ92_4639
BMQ: BMQ_3586
BMD: BMD_3571
BMEG: BG04_460
BACO: OXB_2505
BGY: BGLY_4397
GTN: GTNG_3150(nbaG)
ASOC: CB4_02453(amnF)
AAC: Aaci_1618
AAD: TC41_1514
BTS: Btus_0970
SAY: TPY_0643
MIT: OCO_14790
MIA: OCU_15230
MJL: Mjls_4208
MVA: Mvan_0595
NFA: NFA_30430
NFR: ERS450000_00296(xylJ_1) ERS450000_01021(xylJ_2)
REY: O5Y_02265
REQ: REQ_05050(amnD)
RRT: 4535765_01257(amnE)
GBR: Gbro_0225
SBH: SBI_01536
TCU: Tcur_0537
SRO: Sros_9112
NML: Namu_0794
AMD: AMED_8622
AMN: RAM_44250
AMM: AMES_8491
AMZ: B737_8492
AOI: AORI_7401
PDX: Psed_4292
SAQ: Sare_3899
MIL: ML5_3358
IIS: EYM_02850
 » show all
Taxonomy
Reference
1  [PMID:1732207]
  Authors
Shingler V, Powlowski J, Marklund U.
  Title
Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600.
  Journal
J Bacteriol 174:711-24 (1992)
DOI:10.1128/JB.174.3.711-724.1992
  Sequence
Reference
2  [PMID:9683650]
  Authors
Takenaka S, Murakami S, Shinke R, Aoki K
  Title
Metabolism of 2-aminophenol by Pseudomonas sp. AP-3: modified meta-cleavage pathway.
  Journal
Arch Microbiol 170:132-7 (1998)
Reference
3  [PMID:10651637]
  Authors
Stanley TM, Johnson WH Jr, Burks EA, Whitman CP, Hwang CC, Cook PF
  Title
Expression and stereochemical and isotope effect studies of active 4-oxalocrotonate decarboxylase.
  Journal
Biochemistry 39:718-26 (2000)
DOI:10.1021/bi9918902
Reference
4  [PMID:17902707]
  Authors
Wang SC, Johnson WH Jr, Czerwinski RM, Stamps SL, Whitman CP
  Title
Kinetic and stereochemical analysis of YwhB, a 4-oxalocrotonate tautomerase homologue in Bacillus subtilis: mechanistic implications for the YwhB- and 4-oxalocrotonate tautomerase-catalyzed reactions.
  Journal
Biochemistry 46:11919-29 (2007)
DOI:10.1021/bi701231a
Reference
5  [PMID:19717587]
  Authors
Kasai D, Fujinami T, Abe T, Mase K, Katayama Y, Fukuda M, Masai E
  Title
Uncovering the protocatechuate 2,3-cleavage pathway genes.
  Journal
J Bacteriol 191:6758-68 (2009)
DOI:10.1128/JB.00840-09
Other DBs
ExplorEnz - The Enzyme Database: 4.1.1.77
IUBMB Enzyme Nomenclature: 4.1.1.77
ExPASy - ENZYME nomenclature database: 4.1.1.77
UM-BBD (Biocatalysis/Biodegradation Database): 4.1.1.77
BRENDA, the Enzyme Database: 4.1.1.77
CAS: 37325-55-6

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