Entry
Name
muconate cycloisomerase;
muconate cycloisomerase I;
cis,cis-muconate-lactonizing enzyme;
cis,cis-muconate cycloisomerase;
muconate lactonizing enzyme;
4-carboxymethyl-4-hydroxyisocrotonolactone lyase (decyclizing);
CatB;
MCI;
2,5-dihydro-5-oxofuran-2-acetate lyase (decyclizing);
2,5-dihydro-5-oxofuran-2-acetate lyase (ring-opening)
Class
Isomerases;
Intramolecular lyases;
Intramolecular lyases (only sub-subclass identified to date)
BRITE hierarchy
Sysname
(+)-muconolactone lyase (ring-opening)
Reaction(IUBMB)
(+)-muconolactone = cis,cis-muconate [RN:
R03959 ]
Reaction(KEGG)
Substrate
(+)-muconolactone [CPD:
C14610 ]
Product
Comment
Requires Mn2+. Also acts (in the reverse reaction) on 3-methyl-cis,cis-muconate and, very slowly, on cis,trans-muconate. Not identical with EC
5.5.1.7 (chloromuconate cycloisomerase) or EC
5.5.1.11 (dichloromuconate cycloisomerase).
History
EC 5.5.1.1 created 1961
Pathway
ec00361 Chlorocyclohexane and chlorobenzene degradation
ec01120 Microbial metabolism in diverse environments
Orthology
K01856 muconate cycloisomerase
Genes
REE : electrica_02604(catB)
RTG : NCTC13098_03821(catB)
KIE : NCTC12125_01049(catB_2)
BUF : D8682_03305 D8682_22185
SFJ : SAMEA4384070_3084(catB)
PAEB : NCGM1900_4020(catB)
PPRC : PFLCHA0_c39200(catB)
PFO : Pfl01_2325(catB) Pfl01_2963(catB)
PMUD : NCTC8068_02080(catB)
PFW : PF1751_v1c46420(catB)
PPUU : PputUW4_03261(catB)
PSAM : HU731_011145 HU731_026970
PTW : TUM18999_33650(catB)
PTAE : NCTC10697_01901(catB_1) NCTC10697_02699(catB_3)
PLAU : I0D68_03685 I0D68_18565
PSKP : KU43P_20590(catB_1) KU43P_26660(catB_2)
PDEU : QEP73_04830 QEP73_17385
ATZ : M5E07_06740 M5E07_08965
ALR : DS731_05510 DS731_05610
HBE : BEI_0569(catB1) BEI_1513(catB2)
HAAH : HALA3H3_380007(catB)
REH : H16_A1966(catB3) H16_B0536(catB4) PHG394(catB2) PHG405(catB1)
CNC : CNE_1c19360(catB) CNE_2c04820(catB)
CUH : BJN34_24340 BJN34_37385(cbnB)
REU : Reut_A1689 Reut_B4400
CCUP : BKK81_23195 BKK81_28965
CUP : BKK80_27410 BKK80_33095
CUU : BKK79_23980 BKK79_33325
COX : E0W60_20510 E0W60_36580 E0W60_36915
CUK : KB879_20130 KB879_22085
CUPP : CTP10_R18940 CTP10_R72300
BMN : BMA10247_A0231(catB)
BPM : BURPS1710b_A0986(catB)
BPL : BURPS1106A_A2566(catB)
BPD : BURPS668_A2710(catB)
BPZ : BP1026B_II2030(catB)
BUR : Bcep18194_B2328 Bcep18194_C7044
BCJ : BCAM0805(catB1) BCAS0498(catB2)
BCEN : DM39_4374 DM39_5088(catB)
BCEW : DM40_3779(catB) DM40_5138(catB)
BCEO : I35_4703(catB1) I35_7542(catB2)
BAC : BamMC406_3662 BamMC406_6302
BMJ : BMULJ_03554(catB) BMULJ_05290(catB)
BMUL : NP80_3319 NP80_3760
BCED : DM42_4281(catB) DM42_7062(catB)
BCEP : APZ15_20395 APZ15_36370
BPYR : ABD05_17755 ABD05_32045
BCON : NL30_21775 NL30_37475
BDF : WI26_17640 WI26_27650
BLAT : WK25_16370 WK25_21475
BTEI : WS51_02325 WS51_27235
BSEM : WJ12_16770 WJ12_24030
BPSL : WS57_00480 WS57_10025
BMEC : WJ16_18185 WJ16_23010
BSTL : BBJ41_31685 BBJ41_36440
BARI : NLX30_18630 NLX30_38125
BAEN : L3V59_33825 L3V59_35290
BSER : R0290_23685 R0290_32760
BUG : BC1001_1338 BC1001_2044
BYI : BYI23_A013730 BYI23_D002120
BUM : AXG89_16445 AXG89_31915
BURK : DM992_29655 DM992_37885
BURT : BTHE68_33090(catB_1) BTHE68_66540(catB_2)
BURM : GJG85_28255 GJG85_33460
BGE : BC1002_2315 BC1002_4686
BPY : Bphyt_1588 Bphyt_2153
BUZ : AYM40_04925 AYM40_09585 AYM40_25975
PSPW : BJG93_00445 BJG93_34195
PARB : CJU94_14570 CJU94_35215
PHS : C2L64_19095 C2L64_29855 C2L64_52620
PTER : C2L65_16970 C2L65_18545
PPAI : E1956_29870 E1956_38640
PLG : NCTC10937_02987(catB)
CABA : SBC2_54000(catB_1) SBC2_78320(catB_2) SBC2_79690(catB_3)
CABK : NK8_35970 NK8_62390(catB)
BUE : BRPE67_ACDS14150 BRPE67_DCDS03870
BPT : Bpet1401(catB1) Bpet3349(catB3) Bpet3734(catB4)
BTRM : SAMEA390648701947(catB1) SAMEA390648702396(catB3_1) SAMEA390648702879(catB3_2)
AXX : ERS451415_03028(catB)
ACID : CBP33_07795 CBP33_16230
ACIN : CBP34_07695 CBP34_17020
ACIS : CBP35_02240 CBP35_10565
HYN : F9K07_10865 F9K07_19210 F9K07_31110
DIH : G7047_12845 G7047_24370
HSE : Hsero_1306(catB2) Hsero_3665(catB2)
HSZ : ACP92_06535 ACP92_18270
HHF : E2K99_06450 E2K99_18550
HFR : G5S34_06715 G5S34_19780
HEW : HBDW_11850 HBDW_37610
MLIR : LPB04_16090 LPB04_18875
MALI : EYF70_07965 EYF70_17230
AMIH : CO731_00672(catB_1) CO731_02650(catB_2) CO731_05395(catB_3)
ANJ : AMD1_0694(catB) AMD1_2549(catB) AMD1_PA0004(catB)
PHT : BLM14_21550 BLM14_26905 BLM14_27465
SFD : USDA257_c54480(catB)
EAD : OV14_a1480 OV14_a1793
AVF : RvVAR031_pl03280(catB)
BBET : F8237_12550 F8237_17720
BVZ : BRAD3257_2206(catB) BRAD3257_8554
BCOU : IC761_03415 IC761_04060
BXN : I3J27_32585 I3J27_37075
XDI : EZH22_01085 EZH22_09290
MEE : DA075_02810 DA075_16960
MTEA : DK419_01400 DK419_08725
MIND : mvi_01320(catB_1) mvi_57290(catB_2)
BVY : NCTC9239_03015(catB)
RUT : FIU92_19990(catB1) FIU92_22580(catB2)
RMM : ROSMUCSMR3_03740(catB)
MANH : LA6_002978(catB_1) LA6_005895(catB_2)
SINA : KNJ79_21035 KNJ79_21060
SPHD : HY78_21640 HY78_29510
SNAP : PQ455_02535 PQ455_04695
SPMI : K663_21308 K663_22008
SPHT : K426_02220 K426_21249
SPAG : sphantq_03326(catB)
SPHJ : BSL82_17570 BSL82_18095
PALG : HFP57_08475 HFP57_16195
RGI : RGI145_05910 RGI145_20855
RMUC : FOB66_02990 FOB66_07735
AZM : DM194_14265 DM194_25890
AZS : E6C72_15500 E6C72_25325
PFER : IRI77_22540 IRI77_35510
BFD : NCTC4823_00584(catB_1) NCTC4823_00647(ykfB_1) NCTC4823_00807(catB_2)
CCYS : SAMEA4530656_0420(catB)
RCR : NCTC10994_02865(catB)
DLU : A6035_05595 A6035_15825
KSL : OG809_19775 OG809_32440
AMAZ : LUW76_35925 LUW76_36165
AMYY : YIM_10755(tfdD) YIM_15285(catB1)
PDX : Psed_0821 Psed_3094 Psed_6064
» show all
Taxonomy
Reference
Authors
Ornston LN
Title
The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. 3. Enzymes of the catechol pathway.
Journal
J Biol Chem 241:3795-9 (1966)
Reference
2
Authors
Ornston LN.
Title
Conversion of catechol and protocatechuate to beta-ketoadipate (Pseudomonas putida).
Journal
Methods Enzymol 17A:529-549 (1970)
Reference
Authors
SISTROM WR, STANIER RY.
Title
The mechanism of formation of beta-ketoadipic acid by bacteria.
Journal
J Biol Chem 210:821-36 (1954)
Other DBs
ExplorEnz - The Enzyme Database: 5.5.1.1
ExPASy - ENZYME nomenclature database: 5.5.1.1
UM-BBD (Biocatalysis/Biodegradation Database): 5.5.1.1
BRENDA, the Enzyme Database: 5.5.1.1