Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.4.11.7: glutamyl aminopeptidase

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

Word Map on EC 3.4.11.7

Reaction

release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide =

Synonyms

acid aminopeptidase, acidic alpha-aminopeptidase, Aminopeptidase, aminopeptidase A, aminopeptidase A ectopeptidase, aminopeptidase, aspartate, aminopeptidase-A, angiotensinase, angiotensinase A, antigen BP-1/6C3 of mouse B lymphocytes, AP A, APA, Asp-AP, aspartate aminopeptidase, aspartyl aminopeptidase, aspartyl-aminopeptidase, BP-1, BP-1/6C3 antigen, BP1/6C3, Ca2+-activated glutamate aminopeptidase, Differentiation antigen gp160, EAP, ENPEP, GAP, GluAP, glutamyl (aspartyl)-specific aminopeptidase A, glutamyl aminopeptidase, glutamyl aminopeptidase (Lactococcus), glutamyl peptidase, glutamyl-aminopeptidase, glutamyl-AP, hAPA, L-alpha-aspartyl(L-alpha-glutamyl)-peptide hydrolase, L-aspartate aminopeptidase, LAP-A, Lb-PepA, Lc-PepA, leucine aminopeptidase A, M18 aspartyl aminopeptidase, mAPA, membrane aminopeptidase II, membrane-bound aspartyl-AP, MHJ_0125, More, N-terminal acidic amino acid-specific aminopeptidase, PepA, tricorn interacting factor F3, tricorn protease-interacting factor F3, type II Zn2+ membrane-bound aminopeptidase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.7 glutamyl aminopeptidase

Cloned

Cloned on EC 3.4.11.7 - glutamyl aminopeptidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
BP-1/6C3 antigen, gene ENPEP, full-length DNA and amino acid sequence determination and analysis, genetic structure, determination of 5'-flanking regions, promoter sequence, and DNA-binding motifs for transcription factors, overview, transient or stable expression of recombinant enzyme with transmembrane regions or cytoplasmic regions by human interleukin 4 leader sequence in COS-7 cells
expressed in CHO cells
expressed in CHO-K1 cells
expressed in Sf9 cells
-
expression in CHO cells
expression in COS cells
expression in Escherichia coli BL21(DE3)
expression of His-tagged or FLAG-tagged wild-type enzyme, and of isolated His- or FLAG-tagged N-terminal, and HA-tagged C-terminal domain in CHO-K1 cells and AtT-20 cells, expression in trans of the separate C- and N-terminal domains rescues enzyme functions, overview
-
expression of recombinant enzyme in COS-7 cells
-
expression of soluble C-terminally His-tagged enzyme, possessing an N-terminal human trypsin II signal peptide, in Spodoptera frugiperda Sf9 insect cells using the baculovirus transfection system
-
expression of wild-type and mutant enzymes in CHO cells
gene APA, DNA and amino acid sequence determination and analysis
gene APA, DNA and amino acid sequence determination and analysis, genetic organization and structure
-
gene Enpep, quantitative real-time PCR enzyme expression analysis
gene ENPEP, quantitative RT-PCR enzyme expression analysis
gene pepA, recombinant expression of C-terminally His6-tagged enzyme and of untagged enzyme in Escherichia coli strain BL21(DE3)
gene pepA, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
His-tagged protein expressed in Escherichia coli BL21(DE3)
into the pENTR-D-TOPO vector and into the baculovirus transfer vector pDEST8
-
recombinant expression of His-tagged wild-type and mutant enzymes in CHO-K1 cells
the full-length human GATEWAY ENPEP cDNA clone is cloned into the pEGFP-N1 vector for transfection of COS-1 cells
-
the plasmid pBLapA1 is constructed, the plasmid is linearized and used as template for in vitro-transcription and in vitro-translation reactions
-
using codons for optimized gene expression in the yeast Pichia pastoris, for protein expression Sf9 insect cells are infected with PfM18AAP recombinant Baculovirus, furthermore pGEM, pHGFPB and pHcmycB are used
wild type and mutant enzymes are expressed in CHO-K1 cells