137 products were found matching "K01265"!

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.,cofactor:Binds 1 sodium ion per subunit. The sodium ion has a structural role.,cofactor:Binds 2 cobalt ions per subunit.,cofactor:Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate....

The protein encoded by this gene is a member of the methionyl aminopeptidase family. The encoded protein functions both by protecting the alpha subunit of eukaryotic initiation factor 2 from inhibitory phosphorylation and by removing the amino-terminal methionine residue from nascent proteins. Increased expression...

Protein function: Cotranslationally 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). Required for normal progression through the cell cycle. [The...

Protein function: Cotranslationally 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). The catalytic activity of human METAP2 toward Met-Val peptides is...

Fumagillin is a fungal metabolite that has been found in A. fumigatus and has diverse biological activities. It inhibits methionyl aminopeptidase 2 (METAP2, IC50 = 10 nM). Fumagillin (10 ng/ml) inhibits tube formation in a rat blood vessel organ culture assay. It inhibits E. cuniculi replication in isolated rabbit...

ELISA Type: Competitive. Detection Range: 78-5000µg/mL. Sensitivity: 46.9µg/mL. Sample Types: Serum, Plasma. Protein function: Cotranslationally 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...

Antibiotic produced by Aspergillus fumigatus. It is an antiprotozoal. Commonly used to control nosema apis in honey bees. It was found to have antineoplastic activity. It is an inhibitor of angiogenesis.

The N-terminal methionine excision pathway is an essential process in which the N-terminal methionine is removed from many proteins, thus facilitating subsequent protein modification. In mitochondria, enzymes that catalyze this reaction are celled methionine aminopeptidases (MetAps, or MAPs, EC 3.4.11.18) (Serero et...

The N-terminal methionine excision pathway is an essential process in which the N-terminal methionine is removed from many proteins, thus facilitating subsequent protein modification. In mitochondria, enzymes that catalyze this reaction are celled methionine aminopeptidases (MetAps, or MAPs, EC 3.4.11.18) (Serero et...

Protein function: Cotranslationally 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). The catalytic activity of human METAP2 toward Met-Val peptides...

Protein 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). Requires deformylation of the N(alpha)-formylated initiator methionine before it...

Protein 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). Requires deformylation of the N(alpha)-formylated initiator methionine before it...