F
IPR002468

Peptidase M24A, methionine aminopeptidase, subfamily 2

InterPro entry
Short namePept_M24A_MAP2
Overlapping
homologous
superfamilies
 
family relationships

Description

This group of metallopeptidases belong to MEROPS peptidase family M24 (clan MG), subfamily M24A.

Methionine aminopeptidase (
3.4.11.18
) (MAP) catalyses the hydrolytic cleavage of the N-terminal methionine from newly synthesised polypeptides if the penultimate amino acid is small, with different tolerance to Val and Thr at this position
[5]
. All MAP studied to date are monomeric proteins that require cobalt ions for activity. Two subfamilies of MAP enzymes are known to exist
[4, 1]
. While being evolutionary related, they only share a limited amount of sequence similarity mostly clustered around the residues shown, in the Escherichia coli MAP
[3]
, to be involved in cobalt-binding. The first family consists of enzymes from prokaryotes as well as eukaryotic MAP-1 (
IPR002467
), while the second group is made up of archaeal MAP and eukaryotic MAP-2
[2]
and includes proteins which do not seem to be MAP, but that are clearly evolutionary related such as mouse proliferation-associated protein 1 and fission yeast curved DNA-binding protein.

References

1.Methionine aminopeptidase-1: the MAP of the mitochondrion? Keeling PJ, Doolittle WF. Trends Biochem. Sci. 21, 285-6, (1996). View articlePMID: 8772380

2.Methionine aminopeptidase from the hyperthermophilic Archaeon Pyrococcus furiosus: molecular cloning and overexpression in Escherichia coli of the gene, and characteristics of the enzyme. Tsunasawa S, Izu Y, Miyagi M, Kato I. J. Biochem. 122, 843-50, (1997). View articlePMID: 9399590

3.Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme. Roderick SL, Matthews BW. Biochemistry 32, 3907-12, (1993). View articlePMID: 8471602

4.Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes. Arfin SM, Kendall RL, Hall L, Weaver LH, Stewart AE, Matthews BW, Bradshaw RA. Proc. Natl. Acad. Sci. U.S.A. 92, 7714-8, (1995). View articlePMID: 7644482

5.Protein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases. Xiao Q, Zhang F, Nacev BA, Liu JO, Pei D. Biochemistry 49, 5588-99, (2010). View articlePMID: 20521764

GO terms

biological process

cellular component

  • None

Cross References

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