KEGG   ENZYME: 1.1.1.376Help
Entry
EC 1.1.1.376                Enzyme                                 

Name
L-arabinose 1-dehydrogenase [NAD(P)+];
L-arabino-aldose dehydrogenase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
L-arabinose:NAD(P)+ 1-oxidoreductase
Reaction(IUBMB)
L-arabinose + NAD(P)+ = L-arabinono-1,4-lactone + NAD(P)H + H+ [RN:R01757 R10787]
Reaction(KEGG)
Substrate
L-arabinose [CPD:C00259];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006]
Product
L-arabinono-1,4-lactone [CPD:C01114];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
The enzymes from the bacterium Azospirillum brasilense and the archaeon Haloferax volcanii are part of the L-arabinose degradation pathway and prefer NADP+ over NAD+. In vitro the enzyme from Azospirillum brasilense shows also high catalytic efficiency with D-galactose.
History
EC 1.1.1.376 created 2014
Pathway
ec00053  Ascorbate and aldarate metabolism
Orthology
K13873  L-arabinose 1-dehydrogenase
K19660  L-arabinose 1-dehydrogenase [NAD(P)+]
Genes
RPI: Rpic_3007
RPF: Rpic12D_2597
RMN: TK49_06585
BTE: BTH_II1629
BTQ: BTQ_4918(gal)
BTJ: BTJ_3542(gal)
BTZ: BTL_4391
BTD: BTI_5592
BTV: BTHA_3566
BTHE: BTN_4042
BTHM: BTRA_4051(gal)
BTHA: DR62_4078
BTHL: BG87_4374
BVE: AK36_4876
BCN: Bcen_5217
BCJ: BCAM2799(gal)
BCEN: DM39_5047
BCEW: DM40_3366
BCEO: I35_6678
BAM: Bamb_4922
BMU: Bmul_3205
BMJ: BMULJ_05320(gal)
BMK: DM80_4585
BMUL: NP80_3348
BCT: GEM_5608
BCED: DM42_5189
BDL: AK34_5008
BCON: NL30_17840
BLAT: WK25_29410
BTEI: WS51_10635
BSEM: WJ12_33855
BPSL: WS57_00270
BMEC: WJ16_32365
BSTG: WT74_32750
BGU: KS03_2639
BGO: BM43_5016
BUK: MYA_3490
BUL: BW21_5280
BGP: BGL_1c19700(gal)
BPH: Bphy_4216
SPHU: SPPYR_0554(araA)
HVO: HVO_B0032(xacB)
HTU: Htur_2413
NMG: Nmag_1167
NAT: NJ7G_1323
SALI: L593_09335
 » show all
Taxonomy
Reference
1
  Authors
Novick, N.J. and Tyler, M.E.
  Title
Partial purification and properties of an L-arabinose dehydrogenase from Azospirillum brasilense.
  Journal
Can J Microbiol 29:242-246 (1983)
Reference
2  [PMID:16326697]
  Authors
Watanabe S, Kodaki T, Makino K
  Title
Cloning, expression, and characterization of bacterial L-arabinose 1-dehydrogenase involved in an alternative pathway of L-arabinose metabolism.
  Journal
J Biol Chem 281:2612-23 (2006)
DOI:10.1074/jbc.M506477200
  Sequence
Reference
3  [PMID:23949136]
  Authors
Johnsen U, Sutter JM, Zaiss H, Schonheit P
  Title
L-Arabinose degradation pathway in the haloarchaeon Haloferax volcanii involves a novel type of L-arabinose dehydrogenase.
  Journal
Extremophiles 17:897-909 (2013)
DOI:10.1007/s00792-013-0572-2
  Sequence
[hvo:HVO_B0032]
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.376
IUBMB Enzyme Nomenclature: 1.1.1.376
ExPASy - ENZYME nomenclature database: 1.1.1.376
BRENDA, the Enzyme Database: 1.1.1.376
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