BRENDA Home
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB CommentsRequires Co2+ and bound NAD+. The hydrogen atoms on C-7 of the substrate are retained on C-2 of the product.
The taxonomic range for the selected organisms is: Thermus thermophilus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
3-dehydroquinate synthase, 5-dehydroquinate synthase, 3-dehydroquinate synthetase, hpdhqs, dehydroquinate synthetase,
morePlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
dehydroquinate synthase
-
3-dehydroquinate synthetase
-
-
-
-
3-dehydroquinic acid synthetase
-
-
-
-
5-dehydroquinate synthase
-
-
-
-
5-dehydroquinic acid synthetase
-
-
-
-
dehydroquinate synthase
-
-
-
-
dehydroquinate synthetase
-
-
-
-
synthase, 5-dehydroquinate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Zn2+
binding on the C-terminal alpha-helical domain
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NAD+
binding on the N-terminal alpha/beta domain
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
Uniprot
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
P83703_THETH
348
0
37510
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
78400
dynamic light scattering method, bimodal analysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
homodimer
dynamic light scattering with 1 mg/ml protein at pH 8.0, 18°C in 20 mM Tris-HCl buffer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
oil microbatch method, homodimer 1.8 A resolution
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expression in Escherichia coli BL21
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Sugahara, M.; Nodake, Y.; Sugahara, M.; Kunishima, N.
Crystal structure of dehydroquinate synthase from Thermus thermophilus HB8 showing functional importance of the dimeric state
Proteins
58
249-252
2004
Thermus thermophilus (P83703), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (P83703)
brenda
4.2.3.4 3-dehydroquinate synthase
top
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). 
