KEGG   ENZYME: 1.14.13.247
Entry
EC 1.14.13.247              Enzyme                                 
Name
stachydrine N-demethylase;
L-proline betaine N-demethylase;
stc2 (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
L-proline betaine,NAD(P)H:oxygen oxidoreductase (formaldehyde-forming)
Reaction(IUBMB)
L-proline betaine + NAD(P)H + H+ + O2 = N-methyl-L-proline + formaldehyde + NAD(P)+ + H2O [RN:R12511 R12512]
Reaction(KEGG)
R12511 R12512
Substrate
L-proline betaine [CPD:C10172];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080];
O2 [CPD:C00007]
Product
N-methyl-L-proline [CPD:C22223];
formaldehyde [CPD:C00067];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006];
H2O [CPD:C00001]
Comment
The enzyme, characterized from the bacterium Sinorhizobium meliloti 1021, consists of three different types of subunits. The catalytic unit contains a Rieske [2Fe-2S] iron-sulfur cluster, and catalyses the monooxygenation of a methyl group. The resulting N-methoxyl group is unstable and decomposes spontaneously to form formaldehyde. The other subunits are involved in the transfer of electrons from NAD(P)H to the catalytic subunit.
History
EC 1.14.13.247 created 2017
Orthology
K24003  stachydrine N-demethylase
Genes
GAIIMCC3135_19215(doxB) IMCC3135_30555(antA)
SMESMa0751
SMKSinme_6509 Sinme_6764
SMQSinmeB_5206 SinmeB_5942
SMXSM11_pC0481 SM11_pC1269
SMIBN406_04196 BN406_04902
SMEGC770_GR4pB125 C770_GR4pC1082
SMELSM2011_a0751
SMERDU99_20225 DU99_23680
SMDSmed_5979
RHINGR_b23410
SFHSFHH103_04891
SAMESAMCFNEI73_Ch0735
SINOSS05631_c03910
PPHRAPZ00_21050
LAPACP90_16400
LABRCHH27_03915
LABPFJ695_19770
LABTFIU93_22465(antA)
LAGGB0E33_28235
SITTM1040_3219(benA)
RUTFIU92_15770(doxB)
PGAPGA1_c05010
PGLPGA2_c04530
PGDGal_04200
PHQD1820_13985
LMDMETH_15260
LEJETW24_16860
LAQUR2C4_15345
LEVETW23_02070
LCAEK3721_01665
YPACCEW88_06790
YANAYJ57_00100
TPROGa0080559_TMP1788
PABYGa0080574_TMP387
SMEDJNX03_10340
ROHFIU89_05235(antA1)
SAGUCDO87_25835
MARUFIU81_03270(antA)
ROTFIV09_19155(andAc)
RMHLVO79_16445
MALUKU6B_39690
PALXGQA70_14620 GQA70_21035
RSPRSP_3978
RSKRSKD131_4436
RCPRCAP_rcc03351
RHPLPB142_04695
PDEPden_1189 Pden_2832
PAMIJCM7686_3482
PYEA6J80_09815 A6J80_18945
PZHCX676_19050
PAROCUV01_04060
PAMNJCM7685_0217
PMUTDPM13_08015 DPM13_18050
PARSDRW48_09840
PARREOJ32_16320
PAAKFIU66_09370
PKDF8A10_00135 F8A10_05930
PPANESD82_09190 ESD82_21330
PLIAE4191_20995
PMAUCP157_03390(yeaW)
RSUNHU_03451
RMBK529_020165
DAAAKL17_0127
DONBSK21_09055
THWBMG03_13085
TECAKL02_012315
LVSLOKVESSMR4R_02619(doxB)
RBGBG454_01770
GFUKM031_19720
SALOEF888_07955
LITFPZ52_13750
PSHQF3W81_00465
PALWPSAL_034740
PPAFI8N54_16455
RBZB9057_04300
FAQG5B39_09560
PMEAKTC28_10785
TIIDY252_06205
THAIIT893_14795
NACINUH88_17760
 » show all
Reference
1  [PMID:22224443]
  Authors
Daughtry KD, Xiao Y, Stoner-Ma D, Cho E, Orville AM, Liu P, Allen KN
  Title
Quaternary ammonium oxidative demethylation: X-ray crystallographic, resonance Raman, and UV-visible spectroscopic analysis of a Rieske-type demethylase.
  Journal
J Am Chem Soc 134:2823-34 (2012)
DOI:10.1021/ja2111898
  Sequence
[sme:SMa0751]
Reference
2  [PMID:24520058]
  Authors
Kumar R, Zhao S, Vetting MW, Wood BM, Sakai A, Cho K, Solbiati J, Almo SC, Sweedler JV, Jacobson MP, Gerlt JA, Cronan JE
  Title
Prediction and biochemical demonstration of a catabolic pathway for the osmoprotectant proline betaine.
  Journal
MBio 5:e00933-13 (2014)
DOI:10.1128/mBio.00933-13
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.13.247
IUBMB Enzyme Nomenclature: 1.14.13.247
ExPASy - ENZYME nomenclature database: 1.14.13.247
BRENDA, the Enzyme Database: 1.14.13.247

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