Protein Family Models

This family includes the N-terminal non-catalytic domains from creatinase and prolidase. The exact function of this domain is uncertain. [1]. 1696320. Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures. Coll M, Knof SH, Ohga Y, Messerschmidt A, Huber R, Moellering H, Russmann L, Schumacher G;. J Mol Biol 1990;214:597-610. [2]. 15005612. Structure of the prolidase from Pyrococcus furiosus. Maher MJ, Ghosh M, Grunden AM, Menon AL, Adams MW, Freeman HC, Guss JM;. Biochemistry. 2004;43:2771-2783. (from Pfam)

Date:

2024-10-16

This family contains metallopeptidases. It also contains non-peptidase homologues such as the N terminal domain of Spt16 which is a histone H3-H4 binding module [3]. The structure of a representative of this family. [1]. 8471602. Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme. Roderick SL, Matthews BW. Biochemistry 1993;32:3907-3912. -!- Members of this family are metallopeptidases. They belong to family M24 in the classification of Rawlings and Barrett. [2]. 7674922. Evolutionary families of metallopeptidases. Rawlings ND, Barrett AJ;. Meth Enzymol 1995;248:183-228. [3]. 18579787. The FACT Spt16 "peptidase" domain is a histone H3-H4 binding module. Stuwe T, Hothorn M, Lejeune E, Rybin V, Bortfeld M, Scheffzek K, Ladurner AG;. Proc Natl Acad Sci U S A. 2008;105:8884-8889. (from Pfam)

Date:

2024-10-16

M24 family metallopeptidase cleaves amido-, imido- or amidino-containing bonds, exhibiting a fairly narrow substrate specificity compared to other metallo-aminopeptidases, possibly playing roles in regulation of biological processes

Date:

2024-06-29