KEGG   ENZYME: 1.1.1.24
Entry
EC 1.1.1.24                 Enzyme                                 
Name
quinate/shikimate dehydrogenase (NAD+);
quinate dehydrogenase (ambiguous);
quinic dehydrogenase (ambiguous);
quinate:NAD oxidoreductase;
quinate 5-dehydrogenase (ambiguous);
quinate:NAD+ 5-oxidoreductase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
Sysname
L-quinate:NAD+ 3-oxidoreductase
Reaction(IUBMB)
L-quinate + NAD+ = 3-dehydroquinate + NADH + H+ [RN:R01872]
Reaction(KEGG)
R01872
Substrate
L-quinate [CPD:C00296];
NAD+ [CPD:C00003]
Product
3-dehydroquinate [CPD:C00944];
NADH [CPD:C00004];
H+ [CPD:C00080]
Comment
The enzyme, found mostly in bacteria (mostly, but not exclusively in Gram-positive bacteria), fungi, and plants, participates in the degradation of quinate and shikimate with a strong preference for NAD+ as a cofactor. While the enzyme can act on both quinate and shikimate, activity is higher with the former. cf. EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+], and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
History
EC 1.1.1.24 created 1961, modified 1976, modified 2004, modified 2021
Pathway
ec00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ec01100  Metabolic pathways
Orthology
K09484  quinate dehydrogenase
Genes
QSU112022117 112029077
DHADEHA2C03674g
PICPICST_30813
CTENCANTEDRAFT_91884
CAURCJI97_002595
OPAHPODL_00009
NCRNCU06025(qa-3)
NTENEUTE1DRAFT46730(NEUTE1DRAFT_46730)
SMPSMAC_07403(qa3)
PANPODANSg2393
TTTTHITE_2116892
MTMMYCTH_2309055
CTHRCTHT_0047970
MGRMGG_07781
PPEIPpBr36_03790
SSCKSPSK_00849 SPSK_06463
FGRFGSG_03880 FGSG_05704 FGSG_12357
FPUFPSE_06307 FPSE_06596 FPSE_06601
FVRFVEG_05965 FVEG_09879
FOXFOXG_04621 FOXG_08708 FOXG_10944
NHENECHADRAFT_32803 NECHADRAFT_51161
TRETRIREDRAFT_109687
TRRM419DRAFT_131881
MAWMAC_04533
MAJMAA_07943
CMTCCM_06001
PLJVFPFJ_10299
VALVDBG_08510
VDAVDAG_08175
CFJCFIO01_01549 CFIO01_09601
CHIGCH63R_14195
SAPOSAPIO_CDS6511
ELAUCREL1_1141 UCREL1_7618
PFYPFICI_03111 PFICI_14932 PFICI_15086
SSLSS1G_09188
BFUBCIN_06g00810
MBEMBM_00576 MBM_09548
PSCOLY89DRAFT_635429 LY89DRAFT_680000 LY89DRAFT_698602
GLZGLAREA_11530
ANIAN1137.2
AFMAFUA_1G11590 AFUA_3G14800
ACTACLA_024050
NFINFIA_013950
AORAO090038000263 AO090103000428 AO090103000431
ANGANI_1_1222184(An04g08100) ANI_1_1306034(An03g03710)
AFVAFLA_008750 AFLA_013099 AFLA_013104
ALUCAKAW2_30242S AKAW2_50769A
ACHEACHE_30247S ACHE_80025A
APUUAPUU_30054A APUU_31273S APUU_50617S
PCSPc13g08380
PDPPDIP_30870
TMFPMAA_028760 PMAA_038650
TRGTRUGW13939_02954 TRUGW13939_04943
PNOSNOG_10413 SNOG_11439
PTEPTT_10795
BZECOCCADRAFT_83737
BSCCOCSADRAFT_107251
BORCOCMIDRAFT_39029
AALTCC77DRAFT_994183
ZTRMYCGRDRAFT_84424(qa-3)
PFJMYCFIDRAFT_84957
FFUCLAFUR5_10641
BCOMBAUCODRAFT_32361
NPAUCRNP2_4112
SHSSTEHIDRAFT_87473
HIRHETIRDRAFT_476563
UMAUMAG_05412
PFPPFL1_00209
 » show all
Reference
1  [PMID:13208693]
  Authors
MITSUHASHI S, DAVIS BD.
  Title
Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase.
  Journal
Biochim Biophys Acta 15:268-80 (1954)
DOI:10.1016/0006-3002(54)90069-4
Reference
2
  Authors
Gamborg, O.L.
  Title
Aromatic metabolism in plants. III. Quinate dehydrogenase from mung bean cell suspension cultures.
  Journal
Biochim Biophys Acta 128:483-491 (1966)
Reference
3  [PMID:7049157]
  Authors
Hawkins AR, Giles NH, Kinghorn JR.
  Title
Genetical and biochemical aspects of quinate breakdown in the filamentous fungus Aspergillus nidulans.
  Journal
Biochem Genet 20:271-86 (1982)
DOI:10.1007/BF00484424
Reference
4  [PMID:18669580]
  Authors
Singh S, Stavrinides J, Christendat D, Guttman DS.
  Title
A phylogenomic analysis of the shikimate dehydrogenases reveals broadscale functional diversification and identifies one functionally distinct subclass.
  Journal
Mol Biol Evol 25:2221-32 (2008)
DOI:10.1093/molbev/msn170
Reference
5  [PMID:19376919]
  Authors
Teramoto H, Inui M, Yukawa H.
  Title
Regulation of expression of genes involved in quinate and shikimate utilization in Corynebacterium glutamicum.
  Journal
Appl Environ Microbiol 75:3461-8 (2009)
DOI:10.1128/AEM.00163-09
  Sequence
[cgt:cgR_0495]
Reference
6  [PMID:23306642]
  Authors
Kubota T, Tanaka Y, Hiraga K, Inui M, Yukawa H.
  Title
Characterization of shikimate dehydrogenase homologues of Corynebacterium glutamicum.
  Journal
Appl Microbiol Biotechnol 97:8139-49 (2013)
DOI:10.1007/s00253-012-4659-y
  Sequence
[cgt:cgR_0495]
Reference
7  [PMID:25524738]
  Authors
Peek J, Christendat D.
  Title
The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework.
  Journal
Arch Biochem Biophys 566:85-99 (2015)
DOI:10.1016/j.abb.2014.12.006
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.24
IUBMB Enzyme Nomenclature: 1.1.1.24
ExPASy - ENZYME nomenclature database: 1.1.1.24
BRENDA, the Enzyme Database: 1.1.1.24
CAS: 9028-28-8
LinkDB

DBGET integrated database retrieval system