Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.1.1.24 - quinate/shikimate dehydrogenase (NAD+) and Organism(s) Corynebacterium glutamicum and UniProt Accession Q9X5C9

for references in articles please use BRENDA:EC1.1.1.24
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
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+).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Corynebacterium glutamicum
UNIPROT: Q9X5C9
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Corynebacterium glutamicum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
quinate dehydrogenase, quinate/shikimate dehydrogenase, cglqsdh, quinate 5-dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
quinate/shikimate dehydrogenase
the enzyme also shows activity with shikimate
dehydrogenase, quinate
-
-
-
-
NAD+-dependent QDH
-
-
NAD+-dependent quinate dehydrogenase
-
-
quinate: oxidoreductase
-
-
-
-
quinate:NAD oxidoreductase
-
-
-
-
quinate:NAD+ 5-oxidoreductase
-
-
-
-
additional information
-
the enzyme belongs to a functional class of the shikimate/quinate dehydrogenase family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-quinate:NAD+ 3-oxidoreductase
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+).
CAS REGISTRY NUMBER
COMMENTARY hide
9028-28-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-quinate + NAD+
3-dehydroquinate + NADH + H+
show the reaction diagram
shikimate + NAD+
3-dehydroshikimate + NADH + H+
show the reaction diagram
the enzyme also shows high activity with quinate. Clear substrate preference of the enzyme for quinate compared with shikimate both at the pH optimum and in a physiological pH range. The enzyme is strictly NAD(H) dependent
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
show the reaction diagram
shikimate + NAD+
3-dehydroshikimate + NADH + H+
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
structure of the potential binding site of quinate and shikimate includign the the completely conserved residues Lys92 and Asp102, overview. The crystal structure reveals that in contrast to shikimate, quinate forms a hydrogen bond to the NAD+. In addition, the hydroxyl group of a conserved active-site threonine hydrogen binds to quinate more effectively than to shikimate. Also, the hydroxyl group of a conserved tyrosine approaches the carboxylate group of quinate more closely than it does the carboxylate group of shikimate, active site structure, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-quinate + NAD+
3-dehydroquinate + NADH + H+
show the reaction diagram
the enzyme is involved in the catabolic quinate metabolism required for the degradation of lignin
-
-
r
L-quinate + NAD+
3-dehydroquinate + NADH + H+
show the reaction diagram
-
QDH plays a key role in the quinate-degradation pathway
-
-
r
shikimate + NAD+
3-dehydroshikimate + NADH + H+
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
strictly dependent on
NADH
strictly dependent on
NAD+
-
dependent on, 300fold higher activity compared to NADP+
NADH
-
binding site structure, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.6 - 2.4
L-quinate
0.13 - 0.87
NAD+
10.2 - 53.9
shikimate
10.2
L-quinate
-
pH 9.0, 30°C
46.6
shikimate
-
pH 10.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
50.8 - 104.9
L-quinate
43.7 - 223.1
NAD+
30.1 - 214.1
shikimate
61.9
L-quinate
-
pH 9.0, 30°C
85.2
shikimate
-
pH 10.0, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
33.3 - 44.05
L-quinate
71.6 - 826.6
NAD+
3.1 - 4.2
shikimate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 10.5
substrate: shikimate
9 - 9.5
substrate: L-quinate
10
-
shikimate dehydrogenase activity
9
-
quinate dehydrogenase activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
seconfdary and tertiary enzyme structures, the enzyme is composed of two alphabetaalpha domains containing two discontinuous segments, Asp22-Asn127 and Gly287-Leu302, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion sitting-drop method at 20°C. Atomic resolution crystal structures of the enzyme in different functional states: with bound NAD+ (binary complex) and as ternary complexes with NADH plus either shikimate or quinate
NAD+-dependent enzyme, X-ray diffraction structure determination and anaylsis at 1.64-8.0 A resolution, molecular replacement method, modelling of the ternary complexes, overview
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schoepe, J.; Niefind, K.; Schomburg, D.
1.6 A structure of an NAD(+)-dependent quinate dehydrogenase from Corynebacterium glutamicum
Acta Crystallogr. Sect. D
64
803-809
2008
Corynebacterium glutamicum
Manually annotated by BRENDA team
Hppner, A.; Schomburg, D.; Niefind, K.
Enzyme-substrate complexes of the quinate/shikimate dehydrogenase from Corynebacterium glutamicum enable new insights in substrate and cofactor binding, specificity, and discrimination
Biol. Chem.
394
1505-1516
2013
Corynebacterium glutamicum (Q9X5C9), Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032 (Q9X5C9)
Manually annotated by BRENDA team