KEGG   ENZYME: 1.2.1.87Help
Entry
EC 1.2.1.87                 Enzyme                                 

Name
propanal dehydrogenase (CoA-propanoylating);
BphJ
Class
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
propanal:NAD+ oxidoreductase (CoA-propanoylating)
Reaction(IUBMB)
propanal + CoA + NAD+ = propanoyl-CoA + NADH + H+ [RN:R09097]
Reaction(KEGG)
R09097;
(other) R01172
Show
Substrate
propanal [CPD:C00479];
CoA [CPD:C00010];
NAD+ [CPD:C00003]
Product
propanoyl-CoA [CPD:C00100];
NADH [CPD:C00004];
H+ [CPD:C00080]
Comment
The enzyme forms a bifunctional complex with EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase, with a tight channel connecting the two subunits [1,2,3]. Also acts, more slowly, on glycolaldehyde and butanal. In Pseudomonas species the enzyme forms a bifunctional complex with EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). NADP+ can replace NAD+ with a much slower rate [3].
History
EC 1.2.1.87 created 2013
Pathway
ec00622  Xylene degradation
ec00640  Propanoate metabolism
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K13922  propionaldehyde dehydrogenase
K18366  acetaldehyde/propanal dehydrogenase
Genes
ECG: E2348C_2143(pduP)
ECW: EcE24377A_2292(pduP)
ECC: c4534
ECV: APECO1_2291(eutE)
ECQ: ECED1_3458
EUM: ECUMN_2347
ECZ: ECS88_4675
ELN: NRG857_10215
ELF: LF82_343
EFE: EFER_2021
STY: STY2256(pduP)
STT: t0823(pduP)
STM: STM2051(pduP)
SEO: STM14_2540(pduP)
SEY: SL1344_2027(pduP)
SEJ: STMUK_2081(pduP)
SEB: STM474_2136(pduP)
SEF: UMN798_2216(pduP)
SENR: STMDT2_20241(pduP)
SEND: DT104_21081(pduP)
SENI: CY43_11070
SPT: SPA0820(pduP)
SEK: SSPA0767
SEI: SPC_1663(pduP)
SEC: SCH_2059(pduP)
SHB: SU5_02645
SENS: Q786_10125
SED: SeD_A2387
SEG: SG2080(pduP)
SEL: SPUL_0849(pduP)
SEGA: SPUCDC_0849(pduP)
SET: SEN2049(pduP)
SENA: AU38_10340
SENO: AU37_10350
SENV: AU39_10350
SENQ: AU40_11595
SENL: IY59_10635
SEEP: I137_03830
SENE: IA1_10235
SSN: SSON_2071(pduP)
KPN: KPN_03216(pduP)
KPU: KP1_4485(pduP)
KPP: A79E_0893
KPE: KPK_0899(pduP)
KPR: KPR_1818(pduP)
KPJ: N559_1023
KPX: PMK1_00697(adhE_2)
KPNU: LI86_05055
KPNK: BN49_0892(pduP)
KVA: Kvar_0854
KOX: KOX_01510
KOE: A225_4767
KLW: DA718_05410(pduP)
CKO: CKO_00785
CRO: ROD_21371(pduP)
CAMA: F384_10465
METY: MRY16398_18470(pduP)
AHN: NCTC12129_00739(eutE)
YEN: YE2741(pduP)
YEY: Y11_16281
YEW: CH47_2090
YET: CH48_3140
YEE: YE5303_31741(pduP)
YAL: AT01_4022
YFR: AW19_708
YIN: CH53_3356
YKR: CH54_954
PEC: W5S_4254
SOD: Sant_2129(eutE)
PSD: DSC_09370
PPI: ND085(nahO)
PPUT: L483_14060
PPUN: PP4_27270(mhpF)
PPUU: PputUW4_01661(mhpF)
PKC: PKB_4238(nahO)
PSET: THL1_1434
PSIL: PMA3_11730
AVN: Avin_30580(lapF)
AVL: AvCA_30580(lapF)
AVD: AvCA6_30580(lapF)
SPL: Spea_2117
SHL: Shal_2089
SWD: Swoo_1391
PHA: PSHAa2142(mhpF)
PTN: PTRA_a2595(bphJ)
PNG: PNIG_a2789(bphJ)
SALH: HMF8227_02731(bphJ)
CYQ: Q91_0509(nahO) Q91_1490
AEH: Mlg_2461
TAU: Tola_1697
TBN: TBH_C0929
GPB: HDN1F_27080(aphF)
RPI: Rpic_4618
REH: H16_B0596(h16_B0596)
RME: Rmet_1320(mhpF)
CTI: RALTA_B0400(mhpF)
BCJ: BCAM1614(mhpF)
BCEO: I35_5474(mhpF)
BMEC: WJ16_26795
BXE: Bxe_C1188(bphJ)
BXB: DR64_8617
BFN: OI25_4590
RFR: Rfer_0455
PNA: Pnap_4143
AJS: Ajs_0223
VEI: Veis_2782
CTES: O987_07735
LCH: Lcho_3341
AZO: azo1856(lapF) azo1973(mhpF) azo2432(nahO)
ARC: ABLL_2443
SHZ: shn_33315
RPC: RPC_1174
RCP: RCAP_rcc02201(adhE)
CID: P73_1381
RSU: NHU_00544(adhE)
SGI: SGRAN_1580(mhpF)
SJP: SJA_C1-11900(mhpF)
SINB: SIDU_08315
SFLA: SPHFLASMR4Y_02367(bphJ)
RRU: Rru_A0914
RRF: F11_04715
TXI: TH3_21413
HTL: HPTL_0048
BSE: Bsel_3117
LMO: lmo1165
LMOC: LMOSLCC5850_1154(pduP)
LMOE: BN418_1367
LMOB: BN419_1365
LMOD: LMON_1158
LMOW: AX10_14330
LMOQ: LM6179_1472(eutE)
LMR: LMR479A_1186(eutE)
LMOM: IJ09_04510
LMF: LMOf2365_1173(pduP)
LMOG: BN389_11840(eutE)
LMP: MUO_06020
LMOL: LMOL312_1152(pduP)
LMOX: AX24_03195
LMQ: LMM7_1171(pduP)
LML: lmo4a_1148(pduP)
LMS: LMLG_1099
LMW: LMOSLCC2755_1157(pduP)
LMX: LMOSLCC2372_1160(pduP)
LMZ: LMOSLCC2482_1204(pduP)
LMON: LMOSLCC2376_1116(pduP)
LMOS: LMOSLCC7179_1132(pduP)
LMOY: LMOSLCC2479_1161(pduP)
LMOT: LMOSLCC2540_1143(pduP)
LMOA: LMOATCC19117_1165(pduP)
LMOK: CQ02_05990
LIN: lin1129
LWE: lwe1123(pduP)
LSG: lse_1043(pduP)
LIV: LIV_1097
KZO: NCTC404_01742(bphJ)
LBR: LVIS_1603
LRE: Lreu_1735
LRF: LAR_1623
PCE: PECL_1370(pduP)
CBK: CLL_A1748
CBT: CLH_1846
CSB: CLSA_c22740(eutE) CLSA_c33640(ald)
CSQ: CSCA_5280
RUM: CK1_20690
ROB: CK5_18240
CPY: Cphy_1178
EHL: EHLA_3029
CST: CLOST_0674(eutE)
ELM: ELI_4072
AWO: Awo_c25770(pduP)
OVA: OBV_17600
THX: Thet_0994
TOC: Toce_0560
TSH: Tsac_0219
VDN: NCTC11831_01740(sucD)
PUF: UFO1_1126
PFT: JBW_03293
PAC: PPA1741
PAW: PAZ_c18150(eutE)
PACC: PAC1_08955
PACH: PAGK_1670
CACN: RN83_09030
CGRN: 4412665_00729(sucD_1)
PFR: PFREUD_09130(pduP)
PFRE: RM25_1259
ACIJ: JS278_01049(adhE)
BIP: Bint_1611
TLI: Tlie_0209
SBR: SY1_15720
 » show all
Taxonomy
Reference
1  [PMID:19476337]
  Authors
Baker P, Pan D, Carere J, Rossi A, Wang W, Seah SY
  Title
Characterization of an aldolase-dehydrogenase complex that exhibits substrate channeling in the polychlorinated biphenyls degradation pathway.
  Journal
Biochemistry 48:6551-8 (2009)
DOI:10.1021/bi9006644
  Sequence
[bxe:Bxe_C1188]
Reference
2  [PMID:21838275]
  Authors
Carere J, Baker P, Seah SY
  Title
Investigating the molecular determinants for substrate channeling in BphI-BphJ, an aldolase-dehydrogenase complex from the polychlorinated biphenyls degradation  pathway.
  Journal
Biochemistry 50:8407-16 (2011)
DOI:10.1021/bi200960j
  Sequence
[bxe:Bxe_C1188]
Reference
3  [PMID:22316175]
  Authors
Baker P, Hillis C, Carere J, Seah SY
  Title
Protein-protein interactions and substrate channeling in orthologous and chimeric aldolase-dehydrogenase complexes.
  Journal
Biochemistry 51:1942-52 (2012)
DOI:10.1021/bi201832a
  Sequence
[ttj:TTHB247]
Other DBs
ExplorEnz - The Enzyme Database: 1.2.1.87
IUBMB Enzyme Nomenclature: 1.2.1.87
ExPASy - ENZYME nomenclature database: 1.2.1.87
BRENDA, the Enzyme Database: 1.2.1.87

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