Protein Family Models

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

type I methionyl aminopeptidase (M24A family metallopeptidase) catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides

Date:

2024-04-23

Methionine aminopeptidase is a cobalt-binding enzyme. Bacterial and organellar examples (type I) differ from eukaroytic and archaeal (type II) examples in lacking a region of approximately 60 amino acids between the 4th and 5th cobalt-binding ligands. This model describes type I. The role of this protein in general is to produce the mature form of cytosolic proteins by removing the N-terminal methionine.

Gene:

map

Date:

2024-06-04