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Information on EC 1.1.1.25 - shikimate dehydrogenase (NADP+) and Organism(s) Thermus thermophilus and UniProt Accession Q5SJF8

for references in articles please use BRENDA:EC1.1.1.25
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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)+].
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This record set is specific for:
Thermus thermophilus
UNIPROT: Q5SJF8
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The taxonomic range for the selected organisms is: Thermus thermophilus
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
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5-dehydroshikimic reductase
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dehydroshikimic reductase
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DHS reductase
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shikimate 5-dehydrogenase
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shikimate dehydrogenase
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shikimate oxidoreductase
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shikimate:NADP oxidoreductase
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shikimate:NADP+ 5-oxidoreductase
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shikimate:NADP+ oxidoreductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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reduction
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ligand-free form, binary complexes with NADP+ or substrate shikimate, and ternary complex with both NADP+ and shikimate. Structures of the closed subunits with and without NADP(H) show no significant difference. Residues K64 and D100 are involved in hydride transfer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bagautdinov, B.; Kunishima, N.
Crystal structures of shikimate dehydrogenase AroE from Thermus thermophilus HB8 and its cofactor and substrate complexes: insights into the enzymatic mechanism
J. Mol. Biol.
373
424-438
2007
Thermus thermophilus (Q5SJF8), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SJF8)
Manually annotated by BRENDA team