Protein Family Models

NamZ is an exo-beta-N-acetylmuramidase which catalyzes an exo-lytic cleavage of beta-1,4-acetylmuramic acid from from the non-reducing ends of peptidoglycan chains [1] and it is a founding member of a new family of glycosidases (GH171). NamZ consists of a N-terminal catalytic domain with a Rossmann-like fold and a C-terminal auxiliary alpha/beta domain (represented in this entry). [1]. 33684445. The exo-beta-N-acetylmuramidase NamZ from Bacillus subtilis is the founding member of a family of exo-lytic peptidoglycan hexosaminidases. Muller M, Calvert M, Hottmann I, Kluj RM, Teufel T, Balbuchta K, Engelbrecht A, Selim KA, Xu Q, Borisova M, Titz A, Mayer C;. J Biol Chem. 2021;296:100519. (from Pfam)

Date:

2024-10-16

NamZ is an exo-beta-N-acetylmuramidase which catalyzes an exo-lytic cleavage of beta-1,4-acetylmuramic acid from from the non-reducing ends of peptidoglycan chains [1] and it is a founding member of a new family of glycosidases (GH171). NamZ consists of a N-terminal catalytic domain with a Rossmann-like fold (represented in this entry) and a C-terminal auxiliary alpha/beta domain [1]. [1]. 33684445. The exo-beta-N-acetylmuramidase NamZ from Bacillus subtilis is the founding member of a family of exo-lytic peptidoglycan hexosaminidases. Muller M, Calvert M, Hottmann I, Kluj RM, Teufel T, Balbuchta K, Engelbrecht A, Selim KA, Xu Q, Borisova M, Titz A, Mayer C;. J Biol Chem. 2021;296:100519. (from Pfam)

Date:

2024-10-16

YbbC family protein

Date:

2017-03-02