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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.1.1.25 - shikimate dehydrogenase (NADP+) and Organism(s) Staphylococcus epidermidis and UniProt Accession Q5HNV1

for references in articles please use BRENDA:EC1.1.1.25
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
NAD+ cannot replace NADP+ . In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10, 3-dehydroquinate dehydratase . cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+].
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Staphylococcus epidermidis
UNIPROT: Q5HNV1
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Staphylococcus epidermidis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
shikimate dehydrogenase, skdh, sasdh, mtbsdh, shikimate 5-dehydrogenase, hpsdh, mtbsd, shikimate:nadp+ oxidoreductase, hi0607, tgsdh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-dehydroshikimate reductase
-
-
-
-
5-dehydroshikimic reductase
-
-
-
-
dehydroshikimic reductase
-
-
-
-
DHS reductase
-
-
-
-
shikimate 5-dehydrogenase
-
-
-
-
shikimate dehydrogenase
-
-
-
-
shikimate oxidoreductase
-
-
-
-
shikimate:NADP oxidoreductase
-
-
-
-
shikimate:NADP+ 5-oxidoreductase
-
-
-
-
shikimate:NADP+ oxidoreductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
shikimate:NADP+ 3-oxidoreductase
NAD+ cannot replace NADP+ [3]. In higher organisms, this enzyme forms part of a multienzyme complex with EC 4.2.1.10, 3-dehydroquinate dehydratase [4]. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.282, quinate/shikimate dehydrogenase [NAD(P)+].
CAS REGISTRY NUMBER
COMMENTARY hide
9026-87-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
show the reaction diagram
-
-
-
r
additional information
?
-
no activity with quinate
-
-
?
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
shikimate + NADP+
3-dehydroshikimate + NADPH + H+
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
cofactor binding might trigger domain movement
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
NADP+
pH 7.0, 25°C, with shikimate
0.073
shikimate
pH 7.0, 25°C, with NADP+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22.8
NADP+
pH 7.0, 25°C, with shikimate
22.8
shikimate
pH 7.0, 25°C, with NADP+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
SDH is the archetypal member of a large protein family, which contains at least four additional functional classes with diverse metabolic roles. The different members of the SDH family share a highly similar three-dimensional structure and utilize a conserved catalytic mechanism, but exhibit distinct substrate preferences
metabolism
the enzyme catalyzes the fourth step of the shikimate pathway, a conserved biosynthetic route in plants, fungi, bacteria, and apicomplexan parasites
physiological function
shikimate dehydrogenase catalyzes the NADPH-dependent reduction of 3-deydroshikimate to shikimate, an essential reaction in the biosynthesis of the aromatic amino acids and a large number of other secondary metabolites in plants and microbes
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure determination of apoenzyme, PDB ID 3DON, and shikimate-bound binary enzyme complex, PDB ID 3DOO
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the shikimate C1-carboxyl is formed by the phenol hydroxyl of a tyrosine. Substitution of this residue in Staphyococcus epidermidis SDH causes a substantial reduction in turnover rate
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the essential enzyme is a potential target for herbicides and antimicrobials
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Peek, J.; Christendat, D.
The shikimate dehydrogenase family: functional diversity within a conserved structural and mechanistic framework
Arch. Biochem. Biophys.
566
85-99
2015
Aquifex aeolicus (O67049), Arabidopsis thaliana (Q9SQT8), Archaeoglobus fulgidus (O27957), Archaeoglobus fulgidus ATCC 49558 (O27957), Aspergillus nidulans (P07547), Aspergillus nidulans FGSC A4 (P07547), Corynebacterium glutamicum (A4QB65), Escherichia coli, Helicobacter pylori, Mycobacterium tuberculosis, Populus trichocarpa, Pseudomonas putida (Q88IJ7), Pseudomonas putida KT 2240 (Q88IJ7), Staphylococcus aureus, Staphylococcus epidermidis (Q5HNV1), Staphylococcus epidermidis ATCC 35984 (Q5HNV1), Toxoplasma gondii (Q6W3D0)
Manually annotated by BRENDA team