KEGG ENZYME: 1.4.1.18

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)

R00446 R02317 R10054

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

BSM:	BSM4216_3155

BFD:	NCTC4823_01480(lys1_1)

BBAD:

K7T73_05075

BACO:

OXB_1319

BACA:

FAY30_13795

OIH:

OB0862

OCN:	CUC15_05270

OCB:	CV093_05535

OJD:	NP439_08555

OON:	NP440_08815

GKA:

GK0375

GTE:	GTCCBUS3UF5_4780

GTK:	GT3570_01870

GTM:	GT3921_17330

GLI:	GLN3_12360

BCAL:

CWI35_08225

GTN:

GTNG_0350

GWC:	GWCH70_0384

GYC:	GYMC61_1254

GYA:	GYMC52_0376

GCT:	GC56T3_0428

GMC:	GY4MC1_3402

GGH:	GHH_c03960

GJF:	M493_02215

GEA:	GARCT_00423(lysDH)

GEL:	IB49_12375

GSE:	GT50_11655

GSR:	GS3922_13755

GEJ:	A0V43_17680

GZA:	IC807_15565

GTH:	Geoth_3493

PTL:	AOT13_05410

PTB:	DER53_06535

PCAL:

BV455_01368(lysDH)

PARG:

PspKH34_34450

AFL:

Aflv_1247

AGN:	AFK25_08275

LSP:

Bsph_0857

LGY:	T479_02020

LFU:	HR49_21770

LYS:	LBYS11_02060

LYB:	C3943_02635

LYZ:	DCE79_01530

LYG:	C1N55_01580

LPAK:

GDS87_02105

LAGR:

FJQ98_02200

LMAC:

I6G82_16430

LYC:	FH508_0001850

LCAP:

ICJ70_22465

LYP:	MTP04_03090

LIU:	OU989_01830

LLB:	R6U77_03105

HHD:	HBHAL_1906

HMN:	HM131_13195

HLI:

HLI_20185

VIR:	X953_03825

VHL:	BME96_03055

VIG:	BKP57_05405

VIL:	CFK37_02300

VNE:	CFK40_18805

VPN:	A21D_02343(lysDH)

VIM:	GWK91_11930

VPT:	KBP50_16885

VNT:	OLD84_05425

VIK:	KFZ58_05080

LAO:	AOX59_10485

LEX:	Len3610_20015

BTHV:

CQJ30_09060

PSYH:

D0S48_09755

PSYO:

PB01_02625

PSYB:

KD050_13760

RUE:	DT065_08910

SALE:

EPH95_09010

SCIB:

HUG20_16285

SCIA:

HUG15_19205

POF:	GS400_06935

PCHU:

QNI29_10835

BLEN:

NCTC4824_00341(lys1_1)

BVJ:	I5776_17760

BOU:	I5818_22160

FHL:	OE105_05045

FAF:	OE104_06080

SFOR:

QNH23_03560

PUK:	PU629_08595

SIV:

SSIL_3578

SSIL:

SOLI23_00485

SOB:	CSE16_01715

PLN:	Plano_2504

PKU:	AUO94_03095

PRT:	AUC31_13560

PLL:	I858_010255

PANA:

BBH88_06375

PDG:	BCM40_02670

PHC:	BBI08_09770

PPLA:

BBI15_08745

PFAE:

AJGP001_14455

PLX:	CW734_14795

PMAT:

BBI11_14375

PDEC:

H1Q58_13675

PGQ:	FK545_03780

KUR:	ASO14_2660

SPSY:

AZE41_20080

SPOR:

SporoP33_11020

SPOP:

SporoP37_11425

SURE:

SporoP32a_11690

SPOS:

DV702_15635

SPAE:

E2C16_12035

SPOO:

J3U78_17685

SURL:

BI350_16170

RST:	ATY39_16195

PAEK:

D3873_01840

PANC:

E2636_14110

PLAY:

DNR44_007165

VIJ:	JNUCC6_16880

UTH:	DKZ56_01210

PARN:

NBH00_04800

GAU:

GAU_0501

GPH:	GEMMAAP_03155

GGR:	HKW67_12630

GBA:

J421_2400

RLO:	GQ464_013260

HALX:

M0R89_04870

HAXY:

NGM07_09875

» 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

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

[ag:BAB39707]

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

DBGET integrated database retrieval system