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Information on EC 4.2.1.93 - ATP-dependent NAD(P)H-hydrate dehydratase and Organism(s) Bacillus subtilis and UniProt Accession P94368

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.93 ATP-dependent NAD(P)H-hydrate dehydratase
IUBMB Comments
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 . 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) .
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Bacillus subtilis
UNIPROT: P94368
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Word Map
  • 4.2.1.93
  • nadphx
  • epimerase
  • dehydrogenases
  • febrile
  • salvage
  • neurometabolic
  • epimer
  • neurodevelopmental
  • neurodegeneration
  • protein-truncating
  • reconvert
  • apolipoprotein
  • 5'-phosphate
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
nad(p)hx dehydratase, ykl151c, carkd, atp-dependent nnrd, atp-dependent nad(p)h-hydrate dehydratase, adp/atp-dependent nad(p)h-hydrate dehydratase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ADP-dependent (S)-NAD(P)H-hydrate dehydratase
UniProt
ADP/ATP-dependent NAD(P)H-hydrate dehydratase
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NAD(P)H-hydrate dehydratase
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ATP-dependent H4NAD(P)OH dehydratase
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reduced nicotinamide adenine dinucleotide hydrate dehydratase
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additional information
cf. EC 4.2.1.136
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-O bond cleavage by elimination of water
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ATP-hydrolysing; NADH-forming)
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].
CAS REGISTRY NUMBER
COMMENTARY hide
116669-08-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the Bacillus subtilis168 osmosensitive mutant, defective in the yxkO gene, gene yxkO knockout phenotype, overview. Changes in the protein value caused by yxkO disruption are also recorded for GroEL. In the mutant, the increase of protein level occurred in non-stressed conditions, as well when compared to the wild-type due to extension of the lag phase and the decline of the renewing of isocitrate dehydrogenase levels in the mutant according to wild-type after stress exposure, which denotes to failure of stress adaptation and triggers increased levels of GroEL as a result of the devastating effects of both stresses on cellular proteins. Identification of differences in protein levels under osmotic stress and ethanol stress, overview
physiological function
the regulatory adaptive system called general stress response (GSR) is dependent on the SigB transcription factor in Bacillus sp.. The GSR is one of the largest regulon in Bacillus sp., including about 100 genes. The yxkO gene (encoding a putative ribokinase) is recently assigned in vitro as an ADP/ATP-dependent NAD(P)H-hydrate dehydratase and belongs to the SigB operon. YxkO has an impact on the activity of SigB-dependent Pctc promoter and adaptation to osmotic and ethanol stress and potassium limitation respectively. The enzyme might play a significant role in the survival of stressed cells
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Petrovova, M.; Tkadlec, J.; Dvoracek, L.; Streitova, E.; Licha, I.
NAD(P)H-hydrate dehydratase - a metabolic repair enzyme and its role in Bacillus subtilis stress adaptation
PLoS ONE
9
e112590
2014
Bacillus subtilis (P94368), Bacillus subtilis, Bacillus subtilis 168 (P94368)
Manually annotated by BRENDA team