KEGG   ENZYME: 1.4.1.18
Entry
EC 1.4.1.18                 Enzyme                                 
Name
lysine 6-dehydrogenase;
L-lysine epsilon-dehydrogenase;
L-lysine 6-dehydrogenase;
LysDH
Class
Oxidoreductases;
Acting on the CH-NH2 group of donors;
With NAD+ or NADP+ as acceptor
Sysname
L-lysine:NAD+ 6-oxidoreductase (deaminating)
Reaction(IUBMB)
L-lysine + NAD+ = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + NADH + H+ + NH3 (overall reaction) [RN:R10054];
(1a) L-lysine + NAD+ + H2O = (S)-2-amino-6-oxohexanoate + NADH + H+ + NH3 [RN:R00446];
(1b) (S)-2-amino-6-oxohexanoate = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O (spontaneous) [RN:R02317]
Reaction(KEGG)
Substrate
L-lysine [CPD:C00047];
NAD+ [CPD:C00003];
H2O [CPD:C00001];
(S)-2-amino-6-oxohexanoate [CPD:C04076]
Product
(S)-2,3,4,5-tetrahydropyridine-2-carboxylate [CPD:C00450];
NADH [CPD:C00004];
H+ [CPD:C00080];
NH3 [CPD:C00014];
(S)-2-amino-6-oxohexanoate [CPD:C04076];
H2O [CPD:C00001]
Comment
The enzyme is highly specific for L-lysine as substrate, although S-(2-aminoethyl)-L-cysteine can act as a substrate, but more slowly. While the enzyme from Agrobacterium tumefaciens can use only NAD+, that from the thermophilic bacterium Geobacillus stearothermophilus can also use NADP+, but more slowly [1,4].
History
EC 1.4.1.18 created 1989, modified 2006, modified 2011
Pathway
ec00960  Tropane, piperidine and pyridine alkaloid biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K19064  lysine 6-dehydrogenase
Genes
BACOOXB_1319
BSMBSM4216_3155
BFDNCTC4823_01480(lys1_1)
BBADK7T73_05075
OIHOB0862
OCNCUC15_05270
OCBCV093_05535
GKAGK0375
GTEGTCCBUS3UF5_4780
GTKGT3570_01870
GTMGT3921_17330
GLIGLN3_12360
GTNGTNG_0350
GWCGWCH70_0384
GYCGYMC61_1254
GYAGYMC52_0376
GCTGC56T3_0428
GMCGY4MC1_3402
GGHGHH_c03960
GJFM493_02215
GEAGARCT_00423(lysDH)
GELIB49_12375
GSEGT50_11655
GSRGS3922_13755
GEJA0V43_17680
GZAIC807_15565
GTHGeoth_3493
PTLAOT13_05410
PTBDER53_06535
PCALBV455_01368(lysDH)
AFLAflv_1247
AGNAFK25_08275
LSPBsph_0857
LGYT479_02020
LFUHR49_21770
LYSLBYS11_02060
LYBC3943_02635
LYZDCE79_01530
LYGC1N55_01580
LPAKGDS87_02105
LAGRFJQ98_02200
LMACI6G82_16430
HHDHBHAL_1906
HMNHM131_13195
HLIHLI_20185
VIRX953_03825
VHLBME96_03055
VIGBKP57_05405
VILCFK37_02300
VNECFK40_18805
VPNA21D_02343(lysDH)
VIMGWK91_11930
VPTKBP50_16885
LAOAOX59_10485
BTHVCQJ30_09060
PSYHD0S48_09755
PSYOPB01_02625
RUEDT065_08910
SALEEPH95_09010
SCIBHUG20_16285
SCIAHUG15_19205
POFGS400_06935
BLENNCTC4824_00341(lys1_1)
BVJI5776_17760
BOUI5818_22160
SIVSSIL_3578
SSILSOLI23_00485
SOBCSE16_01715
PLNPlano_2504
PKUAUO94_03095
PRTAUC31_13560
PLLI858_010255
PANABBH88_06375
PDGBCM40_02670
PHCBBI08_09770
PPLABBI15_08745
PFAEAJGP001_14455
PLXCW734_14795
PMATBBI11_14375
PDECH1Q58_13675
PGQFK545_03780
KURASO14_2660
SPSYAZE41_20080
SPORSporoP33_11020
SPOPSporoP37_11425
SURESporoP32a_11690
SPOSDV702_15635
SPAEE2C16_12035
RSTATY39_16195
PAEKD3873_01840
PANCE2636_14110
PLAYDNR44_007165
VIJJNUCC6_16880
GAUGAU_0501
GPHGEMMAAP_03155
GGRHKW67_12630
GBAJ421_2400
HALXM0R89_04870
 » show all
Reference
1  [PMID:6801024]
  Authors
Misono H, Nagasaki S.
  Title
Occurrence of L-lysine epsilon-dehydrogenase in Agrobacterium tumefaciens.
  Journal
J Bacteriol 150:398-401 (1982)
DOI:10.1128/JB.150.1.398-401.1982
Reference
2
  Authors
Misono, H., Uehigashi, H., Morimoto, E. and Nagasaki, S.
  Title
Purification and properties of L-lysine epsilon-dehydrogenase from Agrobacterium tumefaciens.
  Journal
Agric Biol Chem 49:2253-2255 (1985)
Reference
3  [PMID:2768207]
  Authors
Misono H, Hashimoto H, Uehigashi H, Nagata S, Nagasaki S.
  Title
Properties of L-lysine epsilon-dehydrogenase from Agrobacterium tumefaciens.
  Journal
J Biochem (Tokyo) 105:1002-8 (1989)
DOI:10.1093/oxfordjournals.jbchem.a122757
Reference
4  [PMID:14766574]
  Authors
Heydari M, Ohshima T, Nunoura-Kominato N, Sakuraba H
  Title
Highly stable L-lysine 6-dehydrogenase from the thermophile Geobacillus stearothermophilus isolated from a Japanese hot spring: characterization, gene cloning and sequencing, and expression.
  Journal
Appl Environ Microbiol 70:937-42 (2004)
DOI:10.1128/AEM.70.2.937-942.2004
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.4.1.18
IUBMB Enzyme Nomenclature: 1.4.1.18
ExPASy - ENZYME nomenclature database: 1.4.1.18
BRENDA, the Enzyme Database: 1.4.1.18
CAS: 89400-30-6
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