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3.4.11.1: leucyl aminopeptidase

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

Word Map on EC 3.4.11.1

Reaction

release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low =

Synonyms

A-LAP, acidic M17 leucine aminopeptidase, AcLAP, adipocyte-derived leucine aminopeptidase, Aminopeptidase, aminopeptidase A, Aminopeptidase A/I, aminopeptidase I, aminopeptidase II, Aminopeptidase III, aminopeptidase LAP2, aminopeptidase N, AP 28, AP 56, APDkam589, APN, b/LAP, bovine lens/leucine aminopeptidase, BSAP, cathepsin III, CsLAP1, CsLAP2, cysteinyl-glycine hydrolysing activity, cysteinylglycine-hydrolysing activity, cytosol aminopeptidase, DR57, EC 3.4.1.1, Eg-LAP, endoplasmic reticulum aminopeptidase, ER-aminopeptidase-1, ERAP, ERAP1, ERAP2, FgLAP, FrvX, FTBL protein, FTBL proteins, HSA, L-leucine aminopeptidase, la, LAP, LAP yspII, LAP-A, LAP-N, LAP1, LAP2, lap3, LapA, LAPc, LeuAP, leucinamide aminopeptidase, leucinaminopeptidase, leucine amino peptidase, leucine aminopeptidase, leucine aminopeptidase 1, leucine aminopeptidase 2, leucine aminopeptidase 3, leucine aminopeptidase A, leucine aminopeptidase LAP-N, leucine aminopeptidase N, leucine aminopeptidase,, leucine aminopeptidase-A, Leucyl aminopeptidase, leucyl aminopeptidase (animal), leucyl aminopeptidase (plant), leucyl aminopeptidase yspII, leucyl peptidase, leucylaminopeptidase, leucylpeptidase, LmLAP-A, M17 family leucyl aminopeptidase metalloprotease, M17 LAP, M17 leucine amino peptidase, M17 leucine aminopeptidase, M17 leucyl aminopeptidase, M42 aminopeptidase, major leucyl aminopeptidase, More, PA2939, PaAP, PepA, PepA peptidase A, PepB, peptidase B, peptidase II, peptidase S, pepZ, PfLAP, PH1527, PhTET2, PILS-AP, PILSAP, Placental leucine aminopeptidase, PLAP, proline aminopeptidase, Prolyl aminopeptidase, proteins, specific or class, FTBL, PtLAP, puromycin insensitive leucyl-specific aminopeptidase, puromycin-insensitive leucine specific aminopeptidase, puromycin-insensitive leucyl-specific aminopeptidase, PVX_118180, rLAP, rMHJ_0461, S-Lap1, S-Lap2, S-Lap3, S-Lap4, S-Lap5, S-Lap6, S-Lap7, S-Lap8, SmLAP1, SmLAP2, Smp_03000, Smp_083870, sperm-leucylaminopeptidase, TbLAP-A, TbLAP1, TcLAP-A, TM0042, TpLAP, XoLAP

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.1 leucyl aminopeptidase

Engineering

Engineering on EC 3.4.11.1 - leucyl aminopeptidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R440A
-
essential residue in catalysis
N345L
the mutation results in 93% reduction in LAP activity
N345Q
the mutation results in 72% reduction in LAP activity
N435E
the mutation results in complete loss of the LAP activity
N435L
the mutation results in complete loss of the LAP activity
N435Q
the mutation results in complete loss of the LAP activity
N435R
the mutation results in complete loss of the LAP activity
D375A
-
leukotriene A4 hydrolase mutant
K528A
-
gene A-LAP, site-directed mutagenesis, the mutant enzyme shows reduced activity
K528H
-
gene A-LAP, site-directed mutagenesis, the mutant enzyme shows reduced activity
K528M
-
gene A-LAP, site-directed mutagenesis, the mutant enzyme shows reduced activity
K528R
E343A
-
site-directed mutagenesis, inactive, dominant-negative mutant
E365A
-
site-directed mutagenesis, inactive mutant
K310V
increased specificty for Leu as Xaa, no activity with Asp-Leu in opposite to the wild-type enzyme
R402W
reduced activity with Asp-Leu compared to the wild-type enzyme
D347E
D347G
-
oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme, nearly catalytically inactive with dipeptide substrates
D347I
-
oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
D347N
D347R
D347S
-
oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
D347V
-
oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
D347Y
-
oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
D354E
-
oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
D354M
-
oligonucleotide site-directed mutagenesis, reduced catalytic activity with dipeptide substrates compared to the wild-type
D354R
-
oligonucleotide site-directed mutagenesis, no formation of stable hexamer, reduced catalytic activity with dipeptide substrates compared to the wild-type
E429A
-
oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
E429D
E429G
-
oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
E429Q
-
oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
E429R
inactive mutant with disrupted hexameric structure has increased chaperone activity
E429S
-
oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme
E429V
E429W
-
oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme, nearly catalytically inactive with dipeptide substrates
E429X
-
site-directed mutagenesis, inactive mutants, overview
K354E
K354G
-
oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354M
-
oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354N
-
oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354R
K354T
-
oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354W
-
oligonucleotide site-directed mutagenesis, formation of a more complex structure compared to the wild-type enzyme
K354X
-
site-directed mutagenesis, inactive mutants, overview
R431A
R431G
-
oligonucleotide site-directed mutagenesis, no formation of stable hexamer, inactive mutant
R431K
R431Q
-
oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme
R431V
-
oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme
R431W
-
oligonucleotide site-directed mutagenesis, formation of a stable hexamer corresponding to the wild-type enzyme
additional information