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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
4.2.1.10
5485
The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction
Nat. Struct. Biol.
6
521-525
1999
Mycobacterium tuberculosis
10360352
4.2.1.10
5485
The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction
Nat. Struct. Biol.
6
521-525
1999
Mycobacterium tuberculosis H37Rv
10360352
4.2.1.10
704811
Theoretical study of the reaction mechanism of Streptomyces coelicolor type II dehydroquinase
J. Chem. Theory Comput.
5
1284-1294
2009
Streptomyces coelicolor
26609719
4.2.1.10
677327
Type II dehydroquinase: molecular replacement with many copies
Acta Crystallogr. Sect. D
64
108-118
2008
Helicobacter pylori
18094474
4.2.1.10
677327
Type II dehydroquinase: molecular replacement with many copies
Acta Crystallogr. Sect. D
64
108-118
2008
Streptomyces coelicolor
18094474
4.2.1.10
714749
Understanding the key factors that control the inhibition of type II dehydroquinase by (2R)-2-benzyl-3-dehydroquinic acids
ChemMedChem
5
1726-1733
2010
Mycobacterium tuberculosis
20815012
4.2.1.10
714749
Understanding the key factors that control the inhibition of type II dehydroquinase by (2R)-2-benzyl-3-dehydroquinic acids
ChemMedChem
5
1726-1733
2010
Helicobacter pylori
20815012
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