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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.2.3.4 - 3-dehydroquinate synthase and Organism(s) Staphylococcus aureus and UniProt Accession Q6GGU4

for references in articles please use BRENDA:EC4.2.3.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.4 3-dehydroquinate synthase
IUBMB Comments
Requires Co2+ and bound NAD+. The hydrogen atoms on C-7 of the substrate are retained on C-2 of the product.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Staphylococcus aureus
UNIPROT: Q6GGU4
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: Staphylococcus aureus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
3-dehydroquinate synthase, 5-dehydroquinate synthase, 3-dehydroquinate synthetase, hpdhqs, dehydroquinate synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydroquinate synthase
-
3-dehydroquinate synthetase
-
-
-
-
3-dehydroquinic acid synthetase
-
-
-
-
5-dehydroquinate synthase
-
-
-
-
5-dehydroquinic acid synthetase
-
-
-
-
dehydroquinate synthase
-
-
-
-
dehydroquinate synthetase
-
-
-
-
synthase, 5-dehydroquinate
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
3-deoxy-D-arabino-hept-2-ulosonate-7-phosphate phosphate-lyase (cyclizing; 3-dehydroquinate-forming)
Requires Co2+ and bound NAD+. The hydrogen atoms on C-7 of the substrate are retained on C-2 of the product.
CAS REGISTRY NUMBER
COMMENTARY hide
37211-77-1
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapour-diffusion crystallisation at 4°C utilising microbridges, crystals of unliganded enzyme as well as in complexes with NAD, the substrate analogue [1R-(1alpha,3beta,4alpha,5beta)]-5-phosphonomethyl-1,3,4-trihydroxycyclohexane-1-carboxylic acid and together with both, NAD and [1R-(1alpha,3beta,4alpha,5beta)]-5-phosphonomethyl-1,3,4-trihydroxycyclohexane-1-carboxylic acid
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nichols, C.E.; Ren, J.; Leslie, K.; Dhaliwal, B.; Lockyer, M.; Charles, I.; Hawkins, A.R.; Stammers, D.K.
Comparison of ligand-induced conformational changes and domain closure mechanisms, between prokaryotic and eukaryotic dehydroquinate synthases
J. Mol. Biol.
343
533-546
2004
Aspergillus nidulans (P07547), Staphylococcus aureus (Q6GGU4)
Manually annotated by BRENDA team