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
QSU: 112022117 112029077
DHA: DEHA2C03674g
PIC: PICST_30813
CTEN: CANTEDRAFT_91884
CAUR: CJI97_002595
NCR: NCU06025(qa-3)
NTE: NEUTE1DRAFT46730(NEUTE1DRAFT_46730)
SMP: SMAC_07403(qa3)
PAN: PODANSg2393
TTT: THITE_2116892
MGR: MGG_07781
MAW: MAC_04533
MAJ: MAA_07943
CMT: CCM_06001
ANI: AN1137.2
ANG: ANI_1_1222184(An04g08100) ANI_1_1306034(An03g03710)
PTE: PTT_10795
ZTR: MYCGRDRAFT_84424(qa-3)
 » 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
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
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

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