KEGG   ENZYME: 1.1.99.36
Entry
EC 1.1.99.36                Enzyme                                 

Name
alcohol dehydrogenase (nicotinoprotein);
NDMA-dependent alcohol dehydrogenase;
nicotinoprotein alcohol dehydrogenase;
np-ADH;
ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With unknown physiological acceptors
Sysname
ethanol:acceptor oxidoreductase
Reaction(IUBMB)
ethanol + acceptor = acetaldehyde + reduced acceptor [RN:R09552]
Reaction(KEGG)
R09552
Substrate
ethanol [CPD:C00469];
acceptor [CPD:C00028]
Product
acetaldehyde [CPD:C00084];
reduced acceptor [CPD:C00030]
Comment
Contains Zn2+. Nicotinoprotein alcohol dehydrogenases are unique medium-chain dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a tightly bound NAD+/NADH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro.
The enzyme from the Gram-positive bacterium Amycolatopsis methanolica can accept many primary alcohols as substrates, including benzylalcohol [1].
History
EC 1.1.99.36 created 2010
Orthology
K00119  alcohol dehydrogenase (nicotinoprotein)
Genes
MTU: Rv3086(adhD)
MTV: RVBD_3086
MTC: MT3171
MRA: MRA_3118(adhD)
MTF: TBFG_13103
MTB: TBMG_00881
MTK: TBSG_00887
MTZ: TBXG_000873
MTG: MRGA327_18975
MTI: MRGA423_19230
MTUR: CFBS_3254(adhD)
MTD: UDA_3086(adhD)
MTN: ERDMAN_3377(adhD)
MTUE: J114_16510
MTUH: I917_21670
MTUL: TBHG_03016
MTUT: HKBT1_3241(adhD)
MTUU: HKBT2_3246(adhD)
MTQ: HKBS1_3252(adhD)
MBO: BQ2027_MB3113(adhD)
MBB: BCG_3111(adhD)
MBT: JTY_3106(adhD)
MBM: BCGMEX_3108(adhD)
MBX: BCGT_2936
MAF: MAF_30930(adhD)
MMIC: RN08_3398
MCE: MCAN_31121(adhD)
MCQ: BN44_60602(adhD)
MCV: BN43_60078(adhD)
MCX: BN42_41103(adhD)
MCZ: BN45_60074(adhD)
MMI: MMAR_0127(adhD_1)
MMAE: MMARE11_01140(adhD_1)
MLI: MULP_00112(adhD_1)
MSG: MSMEI_3308(adhD)
MABB: MASS_4764
MJD: JDM601_2351(adhD_1)
MTER: 4434518_02283(adhD_1)
MMIN: MMIN_00430(adhD)
MHIB: MHIB_17950(adhD_1)
MKR: MKOR_39590(adhD)
NFA: NFA_11970
NFR: ERS450000_02912(flhA_2)
NNO: NONO_c26650(adhB1)
RER: RER_18210
REY: O5Y_08735
ROP: ROP_22230
REQ: REQ_36070
GBR: Gbro_3823
GOR: KTR9_3765
GRU: GCWB2_19310(adhD3)
GOM: D7316_04892(adhD)
PSIM: KR76_24400
FAL: FRAAL0199
MMAR: MODMU_2922(adhB) MODMU_2924(adhB) MODMU_2938(adh)
PSEE: FRP1_11630
PAUT: Pdca_08350(adhD_1) Pdca_38470(adhD_3) Pdca_47780(adhD_4) Pdca_47810(adhD_5)
ALO: CRK56109
 » show all
Reference
1  [PMID:8385013]
  Authors
Van Ophem PW, Van Beeumen J, Duine JA
  Title
Nicotinoprotein [NAD(P)-containing] alcohol/aldehyde oxidoreductases. Purification and characterization of a novel type from Amycolatopsis methanolica.
  Journal
Eur J Biochem 212:819-26 (1993)
DOI:10.1111/j.1432-1033.1993.tb17723.x
  Sequence
Reference
2  [PMID:9485460]
  Authors
Piersma SR, Visser AJ, de Vries S, Duine JA
  Title
Optical spectroscopy of nicotinoprotein alcohol dehydrogenase from Amycolatopsis  methanolica: a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase.
  Journal
Biochemistry 37:3068-77 (1998)
DOI:10.1021/bi972115u
Reference
3  [PMID:10784035]
  Authors
Schenkels P, Duine JA
  Title
Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes.
  Journal
Microbiology 146 ( Pt 4):775-85 (2000)
DOI:10.1099/00221287-146-4-775
Reference
4  [PMID:14690248]
  Authors
Piersma SR, Norin A, de Vries S, Jornvall H, Duine JA
  Title
Inhibition of nicotinoprotein (NAD+-containing) alcohol dehydrogenase by trans-4-(N,N-dimethylamino)-cinnamaldehyde binding to the active site.
  Journal
J Protein Chem 22:457-61 (2003)
DOI:10.1023/b:jopc.0000005461.53788.ee
Reference
5  [PMID:12827287]
  Authors
Norin A, Piersma SR, Duine JA, Jornvall H
  Title
Nicotinoprotein (NAD+ -containing) alcohol dehydrogenase: structural relationships and functional interpretations.
  Journal
Cell Mol Life Sci 60:999-1006 (2003)
DOI:10.1007/s00018-003-3105-9
Other DBs
ExplorEnz - The Enzyme Database: 1.1.99.36
IUBMB Enzyme Nomenclature: 1.1.99.36
ExPASy - ENZYME nomenclature database: 1.1.99.36
BRENDA, the Enzyme Database: 1.1.99.36
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