Pages that link to "Q37182368"

The following pages link to The dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase from Haemophilus influenzae contains two active-site histidine residues (Q37182368):

Displaying 9 items.

• Structural Basis for Catalysis by the Mono- and Dimetalated Forms of the dapE-Encoded N-succinyl-l,l-Diaminopimelic Acid Desuccinylase (Q27659615) (← links)
• The dimerization domain in DapE enzymes is required for catalysis (Q27683676) (← links)
• Identification of a Histidine Metal Ligand in the argE-Encoded N-Acetyl-L-Ornithine Deacetylase from Escherichia coli (Q35059170) (← links)
• Inhibition of the dapE-Encoded N-Succinyl-L,L-diaminopimelic Acid Desuccinylase from Neisseria meningitidis by L-Captopril. (Q36350977) (← links)
• Structural characterization of Zn(II)-, Co(II)-, and Mn(II)-loaded forms of the argE-encoded N-acetyl-L-ornithine deacetylase from Escherichia coli (Q36528140) (← links)
• Lysine biosynthesis in bacteria: a metallodesuccinylase as a potential antimicrobial target (Q37389657) (← links)
• Reconstruction of diaminopimelic acid biosynthesis allows characterisation of Mycobacterium tuberculosis N-succinyl-L,L-diaminopimelic acid desuccinylase. (Q38999210) (← links)
• A comparative modeling and molecular docking study on Mycobacterium tuberculosis targets involved in peptidoglycan biosynthesis. (Q40892778) (← links)
• Structural Evidence for a Major Conformational Change Triggered by Substrate Binding in DapE Enzymes: Impact on the Catalytic Mechanism. (Q47224410) (← links)