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Literature summary extracted from

  • Shaik, M.M.; Cendron, L.; Percudani, R.; Zanotti, G.
    The structure of Helicobacter pylori HP0310 reveals an atypical peptidoglycan deacetylase (2011), PLoS ONE, 6, e19207.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.104 expression in Escherichia coli Helicobacter pylori

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.104 to 2.57 A resolution. The polypeptide folds into a single domain, characterized by a non-canonical TIM-barrel fold. Nine beta-strands are arranged in a central barrel surrounded by six alpha-helices. Four monomers are present in the asymmetric unit, arranged around a four-fold rotation axis Helicobacter pylori

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.104 Helicobacter pylori B5ZA76
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.104 additional information no substrates: N-acetyl putrescine, N-acetyl spermidine, N-acetyl cadaverine, and N-acetyl dipeptides Ac-D-Ala-D-Ala-OH, Ac-D-Ala-D-Ala-OCH3, Ac-DAla-L-Ala-OH, Ac-D-Ala-L-Ala-OCH3 Helicobacter pylori ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.104 tetramer crystallization data and gel filtration Helicobacter pylori

Synonyms

EC Number Synonyms Comment Organism
3.5.1.104 HP0310
-
 Helicobacter pylori
3.5.1.104 HpPgdA
-
 Helicobacter pylori