KEGG   ENZYME: 4.2.1.93Help
Entry
EC 4.2.1.93                 Enzyme                                 

Name
ATP-dependent NAD(P)H-hydrate dehydratase;
reduced nicotinamide adenine dinucleotide hydrate dehydratase;
ATP-dependent H4NAD(P)+OH dehydratase;
(6S)-beta-6-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase(ATP-hydrolysing);
(6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ATP-hydrolysing;
NADH-forming)
Class
Lyases;
Carbon-oxygen lyases;
Hydro-lyases
BRITE hierarchy
Sysname
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ATP-hydrolysing; NADH-forming)
Reaction(IUBMB)
(1) ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = ADP + phosphate + NADH [RN:R00129];
(2) ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate = ADP + phosphate + NADPH [RN:R10288]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide [CPD:C04856];
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate [CPD:C04899]
Product
ADP [CPD:C00008];
phosphate [CPD:C00009];
NADH [CPD:C00004];
NADPH [CPD:C00005]
Comment
Acts equally well on hydrated NADH and hydrated NADPH. NAD(P)H spontaneously hydrates to both the (6S)- and (6R)- isomers, and these are interconverted by EC 5.1.99.6, NAD(P)H-hydrate epimerase, to a 60:40 ratio [4]. Hence EC 4.2.1.93 together with EC 5.1.99.6 can restore the mixture of hydrates into NAD(P)H [3,4]. The enzyme from eukaryotes has no activity with ADP, contrary to the enzyme from bacteria (cf. EC 4.2.1.136, ADP-dependent NAD(P)H-hydrate dehydratase) [4].
History
EC 4.2.1.93 created 1992, modified 2012
Orthology
K17757  
ATP-dependent NAD(P)H-hydrate dehydratase
Genes
HSA: 
55739(CARKD)
PTR: 
452663(CARKD)
PPS: 
100977905(CARKD)
GGO: 
101150913(CARKD)
PON: 
100173186(CARKD)
MCC: 
694722(CARKD)
MCF: 
102128889(CARKD)
MMU: 
69225(Carkd)
RNO: 
361185(Carkd)
CGE: 
HGL: 
101717804(Carkd)
TUP: 
102481205(CARKD)
CFA: 
607381(CARKD)
AML: 
FCA: 
101096534(CARKD)
BTA: 
613996(CARKD)
BOM: 
102284176(CARKD)
PHD: 
102342914(CARKD)
CHX: 
102171618(CARKD)
SSC: 
100153456(CARKD)
CFR: 
102507835(CARKD)
ECB: 
100066349(CARKD)
MYB: 
102242541(CARKD)
MDO: 
SHR: 
100921239(CARKD)
OAA: 
GGA: 
418755(CARKD)
MGP: 
TGU: 
100219904(CARKD)
FAB: 
101817373(CARKD)
PHI: 
102099739(CARKD)
APLA: 
101804240(CARKD)
FPG: 
FCH: 
102046376(CARKD)
CLV: 
102088516(CARKD)
ASN: 
102367921(CARKD)
PSS: 
102453397(CARKD)
ACS: 
XTR: 
549064(carkd)
DRE: 
TRU: 
OLA: 
XMA: 
LCM: 
102349649(CARKD)
BFO: 
CIN: 
SPU: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
AGA: 
AAG: 
CQU: 
AME: 
550956(GB16073)
NVI: 
TCA: 
BMOR: 
API: 
PHU: 
ISC: 
CEL: 
CELE_R107.2(R107.2)
CBR: 
BMY: 
LOA: 
SMM: 
NVE: 
HMG: 
TAD: 
AQU: 
ATH: 
ALY: 
CRB: 
EUS: 
CIT: 
CIC: 
GMX: 
CAM: 
FVE: 
CSV: 
RCU: 
POP: 
POPTR_0008s20800g(POPTRDRAFT_719850)
VVI: 
SLY: 
SOT: 
OSA: 
DOSA: 
Os11t0276300-01(Os11g0276300)
BDI: 
SBI: 
SORBI_05g010020(SORBIDRAFT_05g010020)
ZMA: 
SITA: 
SMO: 
PPP: 
CRE: 
VCN: 
OLU: 
MIS: 
MPP: 
CSL: 
CVR: 
CME: 
GSL: 
CCP: 
SCE: 
AGO: 
ERC: 
KLA: 
LTH: 
PPA: 
VPO: 
ZRO: 
CGR: 
NCS: 
NCAS_0F02350(NCAS0F02350)
NDI: 
NDAI_0C03850(NDAI0C03850)
TPF: 
TPHA_0E02390(TPHA0E02390)
TBL: 
TBLA_0A10100(TBLA0A10100)
TDL: 
TDEL_0E03700(TDEL0E03700)
KAF: 
KAFR_0E01710(KAFR0E01710)
DHA: 
PIC: 
PGU: 
LEL: 
CAL: 
CTP: 
CDU: 
COT: 
YLI: 
CLU: 
NCR: 
SMP: 
PAN: 
TTT: 
MTM: 
MGR: 
FGR: 
NHE: 
VAL: 
SSL: 
BFU: 
ANI: 
NFI: 
AFM: 
AOR: 
AOR_1_1070054(AO090011000624)
ANG: 
ANI_1_696144(An16g04910)
AFV: 
ACT: 
PCS: 
CIM: 
CPW: 
PBL: 
URE: 
ABE: 
TVE: 
AJE: 
PNO: 
PTE: 
ZTR: 
TML: 
SPO: 
CNE: 
CNB: 
CGI: 
PPL: 
LBC: 
MPR: 
CCI: 
SCM: 
UMA: 
MGL: 
PGR: 
ECU: 
EIN: 
EHE: 
NCE: 
DDI: 
DPP: 
DFA: 
EHI: 
EHI_194450(46.t00021)
EDI: 
ACAN: 
PCB: 
PTM: 
PTI: 
PIF: 
EHX: 
GTT: 
NGR: 
TVA: 
 » show all
Taxonomy
Reference
1  [PMID:13331940]
  Authors
MEINHART JO, CHAYKIN S, KREBS EG.
  Title
Enzymatic conversion of a reduced diphosphopyridine nucleotide derivative to reduced diphosphopyridine nucleotide.
  Journal
J. Biol. Chem. 220 (1956) 821-9.
  Organism
Saccharomyces cerevisiae [GN:sce]
  Sequence
[sce:YKL151C]
Reference
2
  Authors
Regueiro Varela, B., Amelunxen, R. and Grisolia, S.
  Title
Synthesis and degradation of monohydroxytetrahydronicotinamide adenine dinucleotide phosphate.
  Journal
Physiol. Chem. Phys. 2 (1970) 445-454.
Reference
3  [PMID:3061454]
  Authors
Acheson SA, Kirkman HN, Wolfenden R.
  Title
Equilibrium of 5,6-hydration of NADH and mechanism of ATP-dependent dehydration.
  Journal
Biochemistry. 27 (1988) 7371-5.
  Organism
Saccharomyces cerevisiae [GN:sce]
  Sequence
[sce:YKL151C]
Reference
4  [PMID:21994945]
  Authors
Marbaix AY, Noel G, Detroux AM, Vertommen D, Van Schaftingen E, Linster CL
  Title
Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair.
  Journal
J. Biol. Chem. 286 (2011) 41246-52.
  Organism
Mus musculus [GN:mmu], Saccharomyces cerevisiae [GN:sce]
  Sequence
[mmu:69225] [sce:YKL151C]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
116669-08-0

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