KEGG   ENZYME: 1.1.1.376
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
Sysname
alpha-L-arabinopyranose:NAD(P)+ 1-oxidoreductase
Reaction(IUBMB)
alpha-L-arabinopyranose + NAD(P)+ = L-arabinono-1,4-lactone + NAD(P)H + H+ [RN:R12971 R12972]
Reaction(KEGG)
R12971 R12972;
(other) R01757 R10787
Substrate
alpha-L-arabinopyranose [CPD:C02604];
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. The enzyme is specific for alpha-L-arabinopyranose [3,4].
History
EC 1.1.1.376 created 2014, modified 2022
Pathway
ec00053  Ascorbate and aldarate metabolism
Orthology
K13873  L-arabinose 1-dehydrogenase
K19660  L-arabinose 1-dehydrogenase [NAD(P)+]
Genes
RPIRpic_3007
RPFRpic12D_2597
RMNTK49_06585
BTEBTH_II1629
BTQBTQ_4918(gal)
BTJBTJ_3542(gal)
BTZBTL_4391
BTDBTI_5592
BTVBTHA_3566
BTHEBTN_4042
BTHMBTRA_4051(gal)
BTHADR62_4078
BTHLBG87_4374
BHGI6G56_24125
BVIBcep1808_3835
BVEAK36_4876
BURBcep18194_B0043
BCNBcen_5217
BCHBcen2424_5642
BCMBcenmc03_4587
BCJBCAM2799(gal)
BCENDM39_5047
BCEWDM40_3366
BCEOI35_6678
BAMBamb_4922
BACBamMC406_5477
BMJBMULJ_05320(gal)
BMUBmul_3205
BMKDM80_4585
BMULNP80_3348
BCTGEM_5608
BCEDDM42_5189
BCEPAPZ15_24590
BDLAK34_5008
BPYRABD05_21640
BCONNL30_17840
BDFWI26_26555
BLATWK25_29410
BTEIWS51_10635
BSEMWJ12_33855
BPSLWS57_00270
BMECWJ16_32365
BSTGWT74_32750
BANNJFN94_18015
BGLbglu_1g17840
BGUKS03_2639
BGDbgla_2g13480
BGOBM43_5016
BYIBYI23_D004050
BUKMYA_3490
BUEBRPE67_DCDS05760
BULBW21_5280
BGPBGL_1c19700(gal)
BPLAbpln_1g18010
BUDAQ610_26800
BUMAXG89_41345
BUIAX768_18490
BURKDM992_25755
BPHBphy_4216
BCAIK788_0000802
PARABTO02_21205
PHSC2L64_32810
PTERC2L65_29415
PCAFDSC91_001478
PTROG5S35_33965
PACPFAZ97_34315
PACSFAZ98_28810
PEWKZJ38_22550
CABASBC2_43760(araA)
BUOBRPE64_DCDS07820
SCUSCE1572_24590
NOHG5V57_02720
TSOIZ6_06580
TSVDSM104635_03107(araA)
TECAKL02_004470
NOGGKE62_05955
SPLMBXU08_18050
SPHCCVN68_10740
SYBTZ53_07825
SUFLFIL70_20185
SBARH5V43_16855
SANDH3309_02360
ABGAsbog_01850
KHAIFJ82_02680
KITCFP65_5708
LEDBBK82_32245
HALXM0R89_12130
HAXZM0R88_12415
HDOMUK72_03155
HVOHVO_B0032(xacB)
HGIABY42_15605
HALEG3A49_07025
HALMFCF25_09685
SRUBC2R22_01275
HTUHtur_2413
HDABB347_08300
HJTDVR14_16085 DVR14_20205
HSALJMJ58_16780
HLOJ0X27_17705
HAKZJ0X25_00720
NMGNmag_1167
HXAHalxa_4145
NATNJ7G_1323
NPENatpe_1381
NVRFEJ81_07295
NPLFGF80_04025
NAYHYG81_03285
HALYHYG82_05205
NGENatgr_2452
HRUHalru_1082
NOUNatoc_1323
SALIL593_09335
HLCCHINAEXTREME10435
NAJB1756_18050
NAGAArcMg_2507
NANAArc1_1220
NBGDV706_11390
NASGCU68_00750
SAWLNGM29_08730
 » show all
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]
Reference
4  [PMID:25236800]
  Authors
Aro-Karkkainen N, Toivari M, Maaheimo H, Ylilauri M, Pentikainen OT, Andberg M, Oja M, Penttila M, Wiebe MG, Ruohonen L, Koivula A.
  Title
L-arabinose/D-galactose 1-dehydrogenase of Rhizobium leguminosarum bv. trifolii characterised and applied for bioconversion of L-arabinose to L-arabonate with Saccharomyces cerevisiae.
  Journal
Appl Microbiol Biotechnol 98:9653-65 (2014)
DOI:10.1007/s00253-014-6039-2
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
LinkDB

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