KEGG   ENZYME: 4.1.3.39Help
Entry
EC 4.1.3.39                 Enzyme                                 

Name 4-hydroxy-2-oxovalerate aldolase;
4-hydroxy-2-ketovalerate aldolase;
HOA;
DmpG;
4-hydroxy-2-oxovalerate pyruvate-lyase;
4-hydroxy-2-oxopentanoate pyruvate-lyase
Class Lyases;
Carbon-carbon lyases;
Oxo-acid-lyases
BRITE hierarchy
Sysname 4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming)
Reaction(IUBMB) 4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate [RN:R00750]
Reaction(KEGG) R00750
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Substrate 4-hydroxy-2-oxopentanoate [CPD:C03589]
Product acetaldehyde [CPD:C00084];
pyruvate [CPD:C00022]
Comment Requires Mn2+ for maximal activity [1]. The enzyme from Pseudomonas
putida is also stimulated by the presence of NADH [1]. In
Pseudomonas species, this enzyme forms part of a bifunctional enzyme
with EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). It
catalyses the penultimate step in the meta-cleavage pathway for the
degradation of phenols, cresols and catechol [1].
Pathway PATH: ec00360  Phenylalanine metabolism
PATH: ec00362  Benzoate degradation via hydroxylation
PATH: ec00621  Biphenyl degradation
PATH: ec00622  Toluene and xylene degradation
PATH: ec00627  1,4-Dichlorobenzene degradation
PATH: ec00628  Fluorene degradation
PATH: ec00629  Carbazole degradation
PATH: ec00642  Ethylbenzene degradation
PATH: ec00643  Styrene degradation
PATH: ec01100  Metabolic pathways
Orthology KO: K01666  4-hydroxy 2-oxovalerate aldolase
Genes ECO: b0352(mhpE)
ECJ: JW0343(mhpE)
EBW: BWG_0241(mhpE)
ECE: Z0452(mhpE)
ECS: ECs0407
ECF: ECH74115_0427(mhpE)
ETW: ECSP_0416(mhpE)
ECW: EcE24377A_0376(mhpE)
ECX: EcHS_A0416(mhpE)
ECM: EcSMS35_0383(mhpE)
ECY: ECSE_0377
ECL: EcolC_3273
ECK: EC55989_0359(mhpE)
ECQ: ECED1_0380(mhpE)
ECR: ECIAI1_0353(mhpE)
ECT: ECIAI39_0326(mhpE)
EUM: ECUMN_0395(mhpE)
EBL: B21_00310(mhpE)
EBD: ECBD_3305
EBR: ECB_00306(mhpE)
EOH: ECO103_0334(mhpE)
EOI: ECO111_0388(mhpE)
EOJ: ECO26_0388(mhpE)
SSN: SSON_0331(mhpE)
ECA: ECA1429(nahM)
PLU: plu4081
KPN: KPN_02117(mhpE)
KPE: KPK_2206(mhpE)
KPU: KP1_3212(mhpE)
SPE: Spro_3025
PPU: PP_1791
PPF: Pput_2873 Pput_2888
PPW: PputW619_1984 PputW619_2007
PSB: Psyr_3072
PSP: PSPPH_2158
PEN: PSEEN0975
AVN: Avin_08740(xylK) Avin_15130(mphE) Avin_30570(lapG) Avin_42120
SDN: Sden_2668
SPL: Spea_2116
SHL: Shal_2088
SWD: Swoo_1390
PHA: PSHAa2143(mhpE)
TTU: TERTU_1283(dmpG)
LPN: lpg2681
LPF: lpl2608
LPP: lpp2735
LPC: LPC_0455
AEH: Mlg_2462
MMW: Mmwyl1_3801
RSO: RS01666(RSp0895)
RPI: Rpic_4617
RPF: Rpic12D_3541
REU: Reut_B5823
REH: H16_A1807(mhpE2) H16_B0552(mhpE1) H16_B0595(bpHI)
RME: Rmet_1319 Rmet_5209
CTI: RALTA_B0399(mhpE)
BPS: BPSS1807(mhpE)
BPM: BURPS1710b_A0890(mhpE)
BPL: BURPS1106A_A2454
BPD: BURPS668_A2590(mhpE)
BTE: BTH_II0570(mhpE)
BVI: Bcep1808_5384 Bcep1808_7605
BUR: Bcep18194_B1188 Bcep18194_B1457 Bcep18194_B2959 Bcep18194_C7644
BCJ: BCAM1615(bphI) BCAM2121
BXE: Bxe_A1152(amnG) Bxe_A3546 Bxe_B2325 Bxe_C1187(bphI)
BPH: Bphy_3510 Bphy_4539
BPY: Bphyt_1468
BGL: bglu_2g02770 bglu_2g05720
BAV: BAV0600(bphF)
RFR: Rfer_0454
POL: Bpro_5136
PNA: Pnap_4142
AJS: Ajs_0224
VEI: Veis_2781
CTT: CtCNB1_1351 CtCNB1_3147
MPT: Mpe_A2266 Mpe_A3321
LCH: Lcho_3340
AZO: azo1857(lapG) azo1972(mhpE) azo2431(nahM)
DAR: Daro_0907 Daro_1356 Daro_3238 Daro_3782 Daro_3808
TMZ: Tmz1t_2079
CJD: JJD26997_0727
ABU: Abu_1489
SUN: SUN_2142
GLO: Glov_0787
DMA: DMR_24610(nahM)
HOH: Hoch_1083
ARA: Arad_7255
BTR: Btr_2080
XAU: Xaut_0938
MSL: Msil_1479
NAR: Saro_3687 Saro_3852
SWI: Swit_1641 Swit_2113 Swit_4923
BCA: BCE_2157
BCX: BCA_2155(dmpG)
BTL: BALH_1844
GTN: GTNG_3151(nbaI)
GYM: GYMC10_5131
GYC: GYMC61_2298
BBE: BBR47_29780
PJD: Pjdr2_1367
AAC: Aaci_1619
DSY: DSY3306
DHD: Dhaf_1245
PTH: PTH_0483(leuA)
EEL: EUBELI_01913
ERE: EUBREC_1320
CHY: CHY_1280(mhpE)
MTA: Moth_1775
MTU: Rv3469c(mhpE) Rv3534c
MTC: MT3575(bphI-1) MT3638(bphI-2)
MRA: MRA_3509(mhpE) MRA_3573(bphI)
MTF: TBFG_13506 TBFG_13567
MTB: TBMG_03517(TBMG_03517.1) TBMG_03574(TBMG_03574.1)
MBO: Mb3498c(mhpE) Mb3564c
MBB: BCG_3534c(mhpE) BCG_3598c
MBT: JTY_3534(mhpE) JTY_3599
MPA: MAP0533
MAV: MAV_0627
MSM: MSMEG_4150 MSMEG_5937
MUL: MUL_2435 MUL_4095
MVA: Mvan_0597 Mvan_4391 Mvan_5234
MGI: Mflv_1522
MAB: MAB_0626 MAB_4375
MMC: Mmcs_4659 Mmcs_5438
MKM: Mkms_4747 Mkms_5835
MJL: Mjls_4224 Mjls_5042
MMI: MMAR_1506 MMAR_5021
NFA: nfa30510 nfa33200 nfa4670
RHA: RHA1_ro00515 RHA1_ro03867 RHA1_ro04535(hsaF) RHA1_ro05801
     RHA1_ro08083(bphF3) RHA1_ro09019(bphF1) RHA1_ro10112(bphF4)
RER: RER_07410 RER_57580
ROP: ROP_34160(cmtG) ROP_37360 ROP_44500 ROP_54050 ROP_58620
GBR: Gbro_0238 Gbro_0911
SCO: SCP1.301 SCP1.53c
SGR: SGR_564
NCA: Noca_1649 Noca_2149
TCU: Tcur_0536 Tcur_3470
SRO: Sros_9113
FRE: Franean1_2882 Franean1_4743
FAL: FRAAL4663
NML: Namu_4081
STP: Strop_3525
SAQ: Sare_3900 Sare_4567
BVU: BVU_2661 BVU_4036
FSU: Fisuc_2032
SYW: SYNW0424
CTS: Ctha_2137
RRS: RoseRS_2573
RCA: Rcas_2410
CAU: Caur_1351
CAG: Cagg_2034
CHL: Chy400_1473
TRO: trd_1392
TTJ: TTHB246
MLA: Mlab_0987
NMR: Nmar_0140
Taxonomy
Reference
  Authors
  Title

  Journal
  Organism
1  [PMID:12764229]
Manjasetty BA, Powlowski J, Vrielink A.
Crystal structure of a bifunctional aldolase-dehydrogenase:
sequestering a reactive and volatile intermediate.
Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 6992-7.
Pseudomonas sp.
Reference
  Authors
  Title



  Journal
  Organism
2  [PMID:8419288]
Powlowski J, Sahlman L, Shingler V.
Purification and properties of the physically associated
meta-cleavage pathway enzymes 4-hydroxy-2-ketovalerate aldolase and
aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain
CF600.
J. Bacteriol. 175 (1993) 377-85.
Pseudomonas sp.
Reference
  Authors
  Title


  Journal
  Organism
3  [PMID:11264589]
Manjasetty BA, Croteau N, Powlowski J, Vrielink A.
Crystallization and preliminary X-ray analysis of dmpFG-encoded
4-hydroxy-2-ketovalerate aldolase--aldehyde dehydrogenase
(acylating) from Pseudomonas sp. strain CF600.
Acta. Crystallogr. D. Biol. Crystallogr. 57 (2001) 582-5.
Pseudomonas sp.
Other DBs ExplorEnz - The Enzyme Database: 4.1.3.39
IUBMB Enzyme Nomenclature: 4.1.3.39
ExPASy - ENZYME nomenclature database: 4.1.3.39
UM-BBD (Biocatalysis/Biodegradation Database): 4.1.3.39
BRENDA, the Enzyme Database: 4.1.3.39
CAS: 37325-52-3

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