P56218 · MAP2_PYRFU

Function

function

Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).

Catalytic activity

  • Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
    EC:3.4.11.18 (UniProtKB | ENZYME | Rhea)

Cofactor

Co2+ (UniProtKB | Rhea| CHEBI:48828 )

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
9.2 mMa Met-Ala-Ser peptide (for the Fe2+-complexed enzyme)
11.8 mMa Met-Ala-Ser peptide (for the Co2+-complexed enzyme)
5 mMa Met-Gly-Met-Met peptide (for the Fe2+-complexed enzyme)
5.1 mMa Met-Gly-Met-Met peptide (for the Co2+-complexed enzyme)
1.3 mMa Met-Ser-Ser-His-Arg-Trp-Asp-Trp peptide (for the Fe2+-complexed enzyme)
2 mMa Met-Ser-Ser-His-Arg-Trp-Asp-Trp peptide (for the Co2+-complexed enzyme)

pH Dependence

Optimum pH is 7-8.

Temperature Dependence

Optimum temperature is about 90 degrees Celsius.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site62substrate
Binding site82a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site93a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site93a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site153a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site161substrate
Binding site187a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site280a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site280a divalent metal cation 2 (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functioninitiator methionyl aminopeptidase activity
Molecular Functionmetal ion binding
Molecular Functionmetalloaminopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Methionine aminopeptidase
  • EC number
  • Short names
    MAP
    ; MetAP
  • Alternative names
    • Peptidase M

Gene names

    • Name
      map
    • Ordered locus names
      PF0541

Organism names

Accessions

  • Primary accession
    P56218

Proteomes

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis161Reduces enzymatic activity by 96% at 37 degrees Celsius and by 88% at 87 degrees Celsius; when associated with A-173.
Mutagenesis173Reduces enzymatic activity by 96% at 37 degrees Celsius and by 88% at 87 degrees Celsius; when associated with A-161.

Chemistry

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001489781-295Methionine aminopeptidase

Proteomic databases

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    295
  • Mass (Da)
    32,842
  • Last updated
    1998-07-15 v1
  • MD5 Checksum
    A3D0BCB6FD56AEBE03F62F526AEE7CEC
MDTEKLMKAGEIAKKVREKAIKLARPGMLLLELAESIEKMIMELGGKPAFPVNLSINEIAAHYTPYKGDTTVLKEGDYLKIDVGVHIDGFIADTAVTVRVGMEEDELMEAAKEALNAAISVARAGVEIKELGKAIENEIRKRGFKPIVNLSGHKIERYKLHAGISIPNIYRPHDNYVLKEGDVFAIEPFATIGAGQVIEVPPTLIYMYVRDVPVRVAQARFLLAKIKREYGTLPFAYRWLQNDMPEGQLKLALKTLEKAGAIYGYPVLKEIRNGIVAQFEHTIIVEKDSVIVTTE

Mass Spectrometry

Molecular mass is 32,848 Da. Determined by Electrospray.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE009950
EMBL· GenBank· DDBJ
AAL80665.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice.
Help