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Literature summary extracted from

  • Nocek, B.; Reidl, C.; Starus, A.; Heath, T.; Bienvenue, D.; Osipiuk, J.; Jedrzejczak, R.; Joachimiak, A.; Becker, D.P.; Holz, R.C.
    Structural evidence of a major conformational change triggered by substrate binding in DapE enzymes impact on the catalytic mechanism (2018), Biochemistry, 57, 574-584 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.18
-
Haemophilus influenzae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.18 crystal structure of the enzyme in complex with the products succinic acid and diaminopimelic acid, crystal structure is determined at 1.95 A Haemophilus influenzae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.18 Zn2+ dinuclear Zn(II) active site Haemophilus influenzae

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.18 Haemophilus influenzae P44514
-
-
3.5.1.18 Haemophilus influenzae ATCC 51907 P44514
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.18
-
Haemophilus influenzae

Synonyms

EC Number Synonyms Comment Organism
3.5.1.18 HiDapE
-
Haemophilus influenzae
3.5.1.18 N-succinyl-L,L-diaminopimelic acid desuccinylase
-
Haemophilus influenzae