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3.4.11.18: methionyl aminopeptidase

This is an abbreviated version!
For detailed information about methionyl aminopeptidase, go to the full flat file.

Word Map on EC 3.4.11.18

Reaction

release of N-terminal amino acids, preferentially methionine, from peptides and arylamides =

Synonyms

aminopeptidase, methionine, c1MetAP-Ia, c2MetAP-Ia, c3MetAP-Ib, CoCoEcMetAP, Ebp1, eMet-AP, ErbB-3 receptor binding protein, initiation factor 2 associated 67 kDa glycoprotein, L-methionine aminopeptidase, LdBPK_210960, MAP, MAP-2, MAP-Pfu, MAP11, MAP1D, mAPA, MapB, MetAP, MetAP-1, MetAP-2, MetAP-I, MetAP-II, MetAP1, MetAP1a, MetAP1b, MetAP1c, MetAP1D, MetAP2, methionine amino peptidase type 2, methionine aminopeptidase, methionine aminopeptidase 1, methionine aminopeptidase 1b, methionine aminopeptidase 2, methionine aminopeptidase AbMetAPx, methionine aminopeptidase AbMetAPy, methionine aminopeptidase II, methionine aminopeptidase type 1, methionine aminopeptidase type 1a, methionine aminopeptidase type 1c, methionine aminopeptidase type 2, methionine aminopeptidase type I, methionine aminopeptidase type II, methionine aminopeptidase type-2, methionine aminopeptidase-1, methionine aminopeptidase-2, methionine aminopetidase-2, More, p67, p67eIF2, peptidase M, PVX_094985, TM1478, type 1 methionine aminopeptidase, type 2 methionine aminopeptidase, type I MetAP, type I methionine aminopeptidase, YpdF

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.18 methionyl aminopeptidase

Posttranslational Modification

Posttranslational Modification on EC 3.4.11.18 - methionyl aminopeptidase

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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
isoform MetAP2 is post-translationally regulated by an allosteric disulfide bond, which controls substrate specificity and catalytic efficiency. Isoform MetAP2 contains a single Cys228-Cys448 disulfide bond that has an -RH-staple configuration and links two beta-loop structures, which are hallmarks of allosteric disulfide bonds. The disulfide bond exists in oxidized and reduced states in the recombinant enzyme. The disulfide has a standard redox potential of -261 mV and is efficiently reduced by the protein reductant, thioredoxin, with a rate constant of 16180 per M and s. The MetAP2 disulfide bond also exists in oxidized and reduced states in glioblastoma tumor cells, and stressing the cells by oxygen or glucose deprivation results in more oxidized enzyme. Oxidized and reduced isoforms have different catalytic efficiencies for hydrolysis of MetAP2 peptide substrates