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UniProt functional annotation for P56218 | ||
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| UniProt code: P56218. |
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| Organism: | |
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). |
| Taxonomy: | |
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; Pyrococcus. |
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| 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). {ECO:0000255|HAMAP-Rule:MF_01975, ECO:0000269|PubMed:9399590}. |
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| Catalytic activity: | |
Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; Evidence={ECO:0000255|HAMAP-Rule:MF_01975, ECO:0000269|PubMed:9399590}; |
| Cofactor: | |
Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP-Rule:MF_01975, ECO:0000269|PubMed:12044150}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01975, ECO:0000269|PubMed:12044150}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01975, ECO:0000269|PubMed:12044150}; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-Rule:MF_01975, ECO:0000269|PubMed:12044150}; 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 Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site. {ECO:0000255|HAMAP-Rule:MF_01975, ECO:0000269|PubMed:12044150}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=9.2 mM for a Met-Ala-Ser peptide (for the Fe(2+)-complexed enzyme) {ECO:0000269|PubMed:12044150, ECO:0000269|PubMed:9399590}; KM=11.8 mM for a Met-Ala-Ser peptide (for the Co(2+)-complexed enzyme) {ECO:0000269|PubMed:12044150, ECO:0000269|PubMed:9399590}; KM=5.0 mM for a Met-Gly-Met-Met peptide (for the Fe(2+)-complexed enzyme) {ECO:0000269|PubMed:12044150, ECO:0000269|PubMed:9399590}; KM=5.1 mM for a Met-Gly-Met-Met peptide (for the Co(2+)-complexed enzyme) {ECO:0000269|PubMed:12044150, ECO:0000269|PubMed:9399590}; KM=1.3 mM for a Met-Ser-Ser-His-Arg-Trp-Asp-Trp peptide (for the Fe(2+)-complexed enzyme) {ECO:0000269|PubMed:12044150, ECO:0000269|PubMed:9399590}; KM=2.0 mM for a Met-Ser-Ser-His-Arg-Trp-Asp-Trp peptide (for the Co(2+)-complexed enzyme) {ECO:0000269|PubMed:12044150, ECO:0000269|PubMed:9399590}; pH dependence: Optimum pH is 7-8. {ECO:0000269|PubMed:12044150, ECO:0000269|PubMed:9399590}; Temperature dependence: Optimum temperature is about 90 degrees Celsius. {ECO:0000269|PubMed:12044150, ECO:0000269|PubMed:9399590}; |
| Subunit: | |
Monomer. {ECO:0000255|HAMAP-Rule:MF_01975, ECO:0000269|PubMed:15628852, ECO:0000269|PubMed:9811545}. |
| Mass spectrometry: | |
Mass=32848; Method=Electrospray; Evidence={ECO:0000269|PubMed:9399590}; |
| Similarity: | |
Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily. {ECO:0000255|HAMAP- Rule:MF_01975}. |
Annotations taken from UniProtKB at the EBI.