KEGG   ENZYME: 4.2.1.155
Entry
EC 4.2.1.155                Enzyme                                 

Name
(methylthio)acryloyl-CoA hydratase;
DmdD
Class
Lyases;
Carbon-oxygen lyases;
Hydro-lyases
Sysname
3-(methylsulfanyl)prop-2-enoyl-CoA hydro-lyase (acetaldehyde-forming)
Reaction(IUBMB)
3-(methylsulfanyl)acryloyl-CoA + 2 H2O = acetaldehyde + methanethiol + CoA + CO2 (overall reaction) [RN:R10936];
(1a) 3-(methylsulfanyl)acryloyl-CoA + H2O = 3-hydroxy-3-(methylsulfanyl)propanoyl-CoA [RN:R10945];
(1b) 3-hydroxy-3-(methylsulfanyl)propanoyl-CoA = 3-oxopropanoyl-CoA + methanethiol [RN:R10946];
(1c) 3-oxopropanoyl-CoA + H2O = 3-oxopropanoate + CoA [RN:R10947];
(1d) 3-oxopropanoate = acetaldehyde + CO2 [RN:R06973]
Reaction(KEGG)
Substrate
3-(methylsulfanyl)acryloyl-CoA [CPD:C20955];
H2O [CPD:C00001];
3-hydroxy-3-(methylsulfanyl)propanoyl-CoA [CPD:C20968];
3-oxopropanoyl-CoA [CPD:C05989];
3-oxopropanoate [CPD:C00222]
Product
acetaldehyde [CPD:C00084];
methanethiol [CPD:C00409];
CoA [CPD:C00010];
CO2 [CPD:C00011];
3-hydroxy-3-(methylsulfanyl)propanoyl-CoA [CPD:C20968];
3-oxopropanoyl-CoA [CPD:C05989];
3-oxopropanoate [CPD:C00222]
Comment
The enzyme is involved in the degradation of 3-(dimethylsulfonio)propanoate, an osmolyte produced by marine phytoplankton. Isolated from the bacterium Ruegeria pomeroyi.
History
EC 4.2.1.155 created 2015
Pathway
ec00920  Sulfur metabolism
ec01100  Metabolic pathways
Orthology
K20036  (methylthio)acryloyl-CoA hydratase
Genes
OTW: 112242891
PFS: PFLU_2454
PTV: AA957_02575
PAZO: AYR47_18985
PFW: PF1751_v1c21520
PFF: PFLUOLIPICF725950
PFX: A7318_10225
APRS: BI364_09690
HEL: HELO_3943
HAK: KO116_00192
RME: Rmet_2366
BXE: Bxe_C0923
BXB: DR64_7526
PPNO: DA70_03425
PPNM: LV28_02900
PPUL: RO07_21765
PSPU: NA29_15325
PAPI: SG18_20730
PUT: PT7_0125
AFQ: AFA_11055
RFR: Rfer_0274
POL: Bpro_3111
PNA: Pnap_0605
ACRA: BSY15_1662
CTES: O987_24730
RTA: Rta_25000
LIM: L103DPR2_01477(paaF_3)
LIH: L63ED372_00989(paaF_3)
HYB: Q5W_08965
HPSE: HPF_07975(paaF3)
CBAA: SRAA_0578
CBAB: SMCB_0808
LCH: Lcho_0994
DOE: DENOEST_0611(dmdD)
AZO: azo2498(paaG3)
AOA: dqs_2651
AZA: AZKH_2163
TCL: Tchl_1082
MLO: mlr6976
ATU: Atu1417(fad)
RHT: NT26_3192(fad)
BJA: blr7844(fad)
BRA: BRADO0962
BRS: S23_09440(fad)
AOL: S58_66670
BRAD: BF49_4145
RPA: RPA1786
RPB: RPB_3578
RPD: RPD_1886
RPE: RPE_3803
RPT: Rpal_1988
MNO: Mnod_6456
MAQU: Maq22A_c00770(caiD)
PHL: KKY_2321
BVR: BVIR_1682
BLAG: BLTE_16420(fad)
SIL: SPO3805(dmdD)
JAN: Jann_0665
PDE: Pden_2560
PGD: Gal_03918
PTP: RCA23_c26210(crt)
CID: P73_1463
LABT: FIU93_11965(paaF2)
AHT: ANTHELSMS3_04102(dmdD)
MARU: FIU81_05950(echA1)
MALU: KU6B_17010(fad)
TMO: TMO_c0641
PGV: SL003B_2869(fad)
SLAU: SLA_7088
BLIN: BLSMQ_1405
AMD: AMED_3269(paaG)
AMN: RAM_16630
AMM: AMES_3233(paaG)
AMZ: B737_3233(paaG)
PSEH: XF36_04825
PAUT: Pdca_17660(paaG_4)
SLI: Slin_1561
 » show all
Reference
1  [PMID:23704947]
  Authors
Tan D, Crabb WM, Whitman WB, Tong L
  Title
Crystal structure of DmdD, a crotonase superfamily enzyme that catalyzes the hydration and hydrolysis of methylthioacryloyl-CoA.
  Journal
PLoS One 8:e63870 (2013)
DOI:10.1371/journal.pone.0063870
  Sequence
[sil:SPO3805]
Other DBs
ExplorEnz - The Enzyme Database: 4.2.1.155
IUBMB Enzyme Nomenclature: 4.2.1.155
ExPASy - ENZYME nomenclature database: 4.2.1.155
BRENDA, the Enzyme Database: 4.2.1.155

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