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
MTURv3086(adhD)
MTVRVBD_3086
MTCMT3171
MRAMRA_3118(adhD)
MTFTBFG_13103
MTBTBMG_00881
MTKTBSG_00887
MTZTBXG_000873
MTGMRGA327_18975
MTIMRGA423_19230
MTECCDC5079_2842
MTURCFBS_3254(adhD)
MTLCCDC5180_2807
MTDUDA_3086(adhD)
MTNERDMAN_3377(adhD)
MTJJ112_16535
MTUBMT7199_3120
MTUEJ114_16510
MTXM943_15930
MTUHI917_21670
MTULTBHG_03016
MTUTHKBT1_3241(adhD)
MTUUHKBT2_3246(adhD)
MTQHKBS1_3252(adhD)
MBOBQ2027_MB3113(adhD)
MBBBCG_3111(adhD)
MBTJTY_3106(adhD)
MBMBCGMEX_3108(adhD)
MBKK60_032020
MBXBCGT_2936
MAFMAF_30930(adhD)
MMICRN08_3398
MCEMCAN_31121(adhD)
MCQBN44_60602(adhD)
MCVBN43_60078(adhD)
MCXBN42_41103(adhD)
MCZBN45_60074(adhD)
MMIMMAR_0127(adhD_1)
MMAEMMARE11_01140(adhD_1)
MLIMULP_00112(adhD_1)
MPSEMPSD_01220(adhD)
MSHOMSHO_11980
MGOAFA91_22830
MDXBTO20_38150
MPAGC0J29_01120
MNMMNVM_36990(adhD)
MGORH0P51_01075
MBRDMBRA_28350(adhD_1) MBRA_56770(adhD_3)
MKRMKOR_39590(adhD)
MHERK3U94_13280
MVMMJO54_13065 MJO54_17850
MSMMSMEG_3388
MSGMSMEI_3308(adhD)
MSBLJ00_16860
MSNLI99_16865
MSHLI98_16870
MCBMycch_5391
MPHLMPHLCCUG_02540
MRHMycrhN_3021
MPHUMPHO_52900(adhD)
MMUCC1S78_021145
MMATMMAGJ_21980(adhD)
MABBMASS_4764
MIZBAB75_26605
MJDJDM601_2351(adhD_1)
MTER4434518_02283(adhD_1)
MMINMMIN_00430(adhD)
MHIBMHIB_17950(adhD_1)
MPAKMIU77_03820
NFANFA_11970
NFRERS450000_02912(flhA_2)
NNONONO_c26650(adhB1)
RHARHA1_ro02497
RERRER_18210
REYO5Y_08735
REBXU06_08975
RQIC1M55_09210
ROPROP_22230
ROAPd630_LPD06723
RPYY013_25445
RAVAAT18_18375
RHWBFN03_19700
RRZCS378_07895
RHODAOT96_19575
RTMG4H71_10320
RKOJWS14_13105 JWS14_38140 JWS14_42065 JWS14_44215
RGOKYT97_09455
ROZCBI38_27490
RPSKJWS13_32475 JWS13_32695
RGORNMQ04_19370 NMQ04_21330
REQREQ_36070
GBRGbro_3823
GPOGPOL_c36850
GORKTR9_3765
GOQACH46_16240
GTABCM27_19720
GOCCXX93_02880 CXX93_18470
GITC6V83_16365
GRUGCWB2_19310(adhD3)
GOMD7316_04892(adhD)
GAVC5O27_08810
GODGKZ92_18260
GJIH1R19_18060
GOILK459_15575
GHNMVF96_18655
GAMIIHQ52_22240
GMGNWF22_03695 NWF22_10315
TSMASU32_16570
DTMBJL86_0663
DITC3V38_02320
DIZCT688_12595
DPCA6048_13215
DLUA6035_12345
DKNNHB83_11575 NHB83_12670
TOYFO059_02245
SBROGQF42_08075
MSEDE3O41_00750 E3O41_00760
MCAWF6J84_03120 F6J84_03130 F6J84_15160
CIGE7744_12695
JLIEXU32_11070
NAROCFH99_21810 CFH99_24600
NAQUENKNEFLB_04435
NPSKRR39_16450
PSIMKR76_24400
FALFRAAL0199
MMARMODMU_2922(adhB) MODMU_2924(adhB) MODMU_2938(adh)
SACGFDZ84_32530
AMQAMETH_2023 AMETH_3366 AMETH_3367 AMETH_4929
AMYCCU254_29815
AACDLWP59_19720 LWP59_19725 LWP59_29670 LWP59_32705
APRTMUY14_14435
ATHML1857_12530 L1857_13940 L1857_14230 L1857_27400
PDXPsed_0661 Psed_1492
PSEAWY02_14170 WY02_25165 WY02_25180
PSEEFRP1_11630
PSEQAD006_19340
PECQAD017_27180
PHHAFB00_08695
PAUTPdca_08350(adhD_1) Pdca_38470(adhD_3) Pdca_47780(adhD_4) Pdca_47810(adhD_5)
PBROHOP40_14245 HOP40_32375
PPELH6H00_19955
ALOCRK56109
PMADBAY61_30750
SACEGIY23_05210
AMSAMIS_27050
DVCDvina_28770
EKEEK0264_07300
 » 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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