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evolution
leucine aminopeptidases (LAPs) are members of the aminopeptidase M1/M17 family
evolution
phylogenetic analysis reveals that AcLAP clusters into a clade closely related with LAPs from Amoebozoa, including Dictyostelium sp.. The enzyme contains the highly conserved M17 aminopeptidase family signature sequence (NTDAEGRL, residues 425-432) and highly conserved amino acid residues for metal binding (D350, D368, D427, E429) and catalytic site formation (K357, R431). The enzyme belongs to the M17 family of proteases
evolution
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the adipocyte-derived leucine aminopeptidase (A-LAP) is a member of the M1 family of zinc metallopeptidases
evolution
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the adipocyte-derived leucine aminopeptidase (A-LAP) is a member of the M1 family of zinc metallopeptidases
evolution
the enzyme belongs to the M17 family of proteases
evolution
the enzyme belongs to the M17 family of proteases
evolution
the enzyme belongs to the M17 peptidase family
evolution
the leucine aminopeptidase (LAP) is a member of the M17 family of metalloproteases
evolution
the leucine aminopeptidase (LAP) is a member of the M17 family of metalloproteases
evolution
the leucine aminopeptidase (LAP) is a member of the M17 family of metalloproteases
evolution
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the leucine aminopeptidases (LAPs) are members of the M17 family of Zn metalloproteases
evolution
the putative substrate binding site GGMEN, zinc-binding motif HEXXHX18E and the catalytic residues involved in aminopeptidase activity are all conserved, PtLAP is a member of M1 leucine aminopeptidases
evolution
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the enzyme belongs to the M17 family of proteases
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evolution
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the putative substrate binding site GGMEN, zinc-binding motif HEXXHX18E and the catalytic residues involved in aminopeptidase activity are all conserved, PtLAP is a member of M1 leucine aminopeptidases
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malfunction
disruption of the LAP-A hexameric structure increases chaperone activity
malfunction
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disruption of the pepZ gene results in an attenuation of virulence in both localized and systemic models of infection
malfunction
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inhibition of LAP with bestatin does not adversely affect growth of Staphylococcus aureus or biofilm formation
malfunction
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lysates from pepZ mutant cells show leucine aminopeptidase activity comparable to that of the wild-type strain suggesting that the majority of leucine aminopeptidase activity observed in Staphylococcus aureus cells comes from PepS, and not LAP
malfunction
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bestatin and knockdown of LAP3 upregulate phosphorylation of Hsp27 and downregulate expression of fascin. Phosphorylation of Akt and expression of matrix metalloproteinase-2/9 can also be downregulated. LAP3 overexpression showed the opposite results
malfunction
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knockdown of A-LAP expression by siRNA inhibits HUVEC angiogenesis
malfunction
lack of extracellular PaAP in biofilms leading to bacterial cell death implies that PaAP might function as a nutrient recycler within a biofilm. Biomass reduction of mutant DELTApaaP grown under a continuous media flow has one day delay compared with the DELTApaaP pellicles grown on static media. Lack of extracellular PaAP triggers bacterial cell death and bacterial cell death in DELTApaaP biofilms is independent of Psl, while the disruption of DELTApaaP biofilms is a result of the degradation of Psl matrix by PslG released from the dead bacteria within biofilms, which in turn led to the dispersion of live bacteria from biofilms into effluents
malfunction
lack or downregulation of AcLAP activity causes ultrastructural changes of the cell wall in Acanthamoeba castellanii that are closely associated with inhibition of cyst formation
malfunction
S-Lap1 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids
malfunction
S-Lap2 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids
malfunction
S-Lap3 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids
malfunction
S-Lap4 gene mutant homozygotes are male semi-sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids
malfunction
S-Lap5 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids
malfunction
S-Lap6 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids
malfunction
S-Lap7 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids
malfunction
S-Lap8 gene mutant homozygotes are male sterile. The male sterile phenotype of S-Lap enzyme mutants is caused by defects in paracrystalline material accumulation and abnormal structure of the elongated major mitochondrial derivatives and elongated spermatids
malfunction
TbLAP1 knockdown results in delayed cytokinesis and ectopic expression leading to kDNA loss and decreased cell proliferation. Knockdown of TbLAP1 by RNAi leads to accumulation of 2K2N cells. Recombinant Ectopic expression of HA-tagged TbLAP1 in procyclic Trypanosoma brucei induces a significant growth defect, which is manifested by the accumulation of 0K1N cells and a defect in mt membrane potential. RNAi-mediated downregulation of TbLAP1 results in a growth defect
malfunction
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lack of extracellular PaAP in biofilms leading to bacterial cell death implies that PaAP might function as a nutrient recycler within a biofilm. Biomass reduction of mutant DELTApaaP grown under a continuous media flow has one day delay compared with the DELTApaaP pellicles grown on static media. Lack of extracellular PaAP triggers bacterial cell death and bacterial cell death in DELTApaaP biofilms is independent of Psl, while the disruption of DELTApaaP biofilms is a result of the degradation of Psl matrix by PslG released from the dead bacteria within biofilms, which in turn led to the dispersion of live bacteria from biofilms into effluents
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malfunction
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lack of extracellular PaAP in biofilms leading to bacterial cell death implies that PaAP might function as a nutrient recycler within a biofilm. Biomass reduction of mutant DELTApaaP grown under a continuous media flow has one day delay compared with the DELTApaaP pellicles grown on static media. Lack of extracellular PaAP triggers bacterial cell death and bacterial cell death in DELTApaaP biofilms is independent of Psl, while the disruption of DELTApaaP biofilms is a result of the degradation of Psl matrix by PslG released from the dead bacteria within biofilms, which in turn led to the dispersion of live bacteria from biofilms into effluents
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malfunction
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lack of extracellular PaAP in biofilms leading to bacterial cell death implies that PaAP might function as a nutrient recycler within a biofilm. Biomass reduction of mutant DELTApaaP grown under a continuous media flow has one day delay compared with the DELTApaaP pellicles grown on static media. Lack of extracellular PaAP triggers bacterial cell death and bacterial cell death in DELTApaaP biofilms is independent of Psl, while the disruption of DELTApaaP biofilms is a result of the degradation of Psl matrix by PslG released from the dead bacteria within biofilms, which in turn led to the dispersion of live bacteria from biofilms into effluents
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malfunction
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lack of extracellular PaAP in biofilms leading to bacterial cell death implies that PaAP might function as a nutrient recycler within a biofilm. Biomass reduction of mutant DELTApaaP grown under a continuous media flow has one day delay compared with the DELTApaaP pellicles grown on static media. Lack of extracellular PaAP triggers bacterial cell death and bacterial cell death in DELTApaaP biofilms is independent of Psl, while the disruption of DELTApaaP biofilms is a result of the degradation of Psl matrix by PslG released from the dead bacteria within biofilms, which in turn led to the dispersion of live bacteria from biofilms into effluents
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malfunction
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lack of extracellular PaAP in biofilms leading to bacterial cell death implies that PaAP might function as a nutrient recycler within a biofilm. Biomass reduction of mutant DELTApaaP grown under a continuous media flow has one day delay compared with the DELTApaaP pellicles grown on static media. Lack of extracellular PaAP triggers bacterial cell death and bacterial cell death in DELTApaaP biofilms is independent of Psl, while the disruption of DELTApaaP biofilms is a result of the degradation of Psl matrix by PslG released from the dead bacteria within biofilms, which in turn led to the dispersion of live bacteria from biofilms into effluents
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malfunction
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lack of extracellular PaAP in biofilms leading to bacterial cell death implies that PaAP might function as a nutrient recycler within a biofilm. Biomass reduction of mutant DELTApaaP grown under a continuous media flow has one day delay compared with the DELTApaaP pellicles grown on static media. Lack of extracellular PaAP triggers bacterial cell death and bacterial cell death in DELTApaaP biofilms is independent of Psl, while the disruption of DELTApaaP biofilms is a result of the degradation of Psl matrix by PslG released from the dead bacteria within biofilms, which in turn led to the dispersion of live bacteria from biofilms into effluents
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malfunction
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TbLAP1 knockdown results in delayed cytokinesis and ectopic expression leading to kDNA loss and decreased cell proliferation. Knockdown of TbLAP1 by RNAi leads to accumulation of 2K2N cells. Recombinant Ectopic expression of HA-tagged TbLAP1 in procyclic Trypanosoma brucei induces a significant growth defect, which is manifested by the accumulation of 0K1N cells and a defect in mt membrane potential. RNAi-mediated downregulation of TbLAP1 results in a growth defect
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malfunction
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lack of extracellular PaAP in biofilms leading to bacterial cell death implies that PaAP might function as a nutrient recycler within a biofilm. Biomass reduction of mutant DELTApaaP grown under a continuous media flow has one day delay compared with the DELTApaaP pellicles grown on static media. Lack of extracellular PaAP triggers bacterial cell death and bacterial cell death in DELTApaaP biofilms is independent of Psl, while the disruption of DELTApaaP biofilms is a result of the degradation of Psl matrix by PslG released from the dead bacteria within biofilms, which in turn led to the dispersion of live bacteria from biofilms into effluents
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physiological function
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LAP may play regulatory roles in protein biosynthesis and degradation in basophilic cells
physiological function
LAP plays a central role in hatching of the miracidium from the schistosome egg
physiological function
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LAP plays a vital role in the development of oocytes, vitellogenesis
physiological function
lapA is a late wound-response gene of tomato, LapA is involved in protection against Manduca sexta damage
physiological function
the enzyme is responsible for the catabolism of host hemoglobin
physiological function
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the M17 leucine aminopeptidase of the intraerythrocytic stages of the malaria parasite Plasmodium falciparum plays a role in releasing amino acids from host hemoglobin that are used for parasite protein synthesis, growth, and development
physiological function
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enzymatic properties to participate in generating or destroying MHC class I-presented peptides
physiological function
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key roles in senescence, stress response and amino acid turn over
physiological function
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immunization with recombinant Fasciola gigantica LAP (FgLAP) elicits high levels of immune responses and protection against Fasciola gigantica in mice
physiological function
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LAP is required for survival inside human macrophages
physiological function
LAP-A exhibits chaperone activity which is independant of its peptidase activity
physiological function
rMHJ_0461 binds plasminogen and facilitates plasmin conversion
physiological function
AcLAP is a typical M17 family enzyme that plays an essential role during encystation of Acanthamoeba castellanii
physiological function
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adipocyte-derived leucine aminopeptidase (A-LAP) plays a crucial role in angiogenesis
physiological function
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adipocyte-derived leucine aminopeptidase (A-LAP) plays a crucial role in angiogenesis
physiological function
enzyme Lap1 improves the degree of hydrolysis of casein and soy protein hydrolysates and also decreases their bitterness, indicating its potential utility in food production
physiological function
expression of leucine aminopeptidase 3 (LAP3) is associated with the prognosis for and malignant transformation of many types of tumors
physiological function
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isozyme SmLAP1 is involved in digestion
physiological function
leucine aminopeptidase is an important metalloexopeptidase that catalyze the hydrolysis of N-terminal leucine residues from polypeptides and proteins
physiological function
leucine aminopeptidases (LAPs) are metallopeptidases that catalyze the hydrolysis of leucine residues and other N-terminal residues from proteins and peptides. The extracellular enzyme PtLAP executes the degradation of organic matters, contributes to the adaptive survival of microbe in deep-sea environment and may play important roles in marine biogeochemical cycles. The recombinant enzyme rPtLAP can significantly promote the proliferation of tumor cells, including the cell lines HCT116, BEL-7402 and Hela, while displays no effect on that of normal cell line 3T3
physiological function
leucine aminopeptidases (LAPs) of the M17 peptidase family have important functions in regulating the balance of catabolism and anabolism, cell maintenance, growth and defense
physiological function
M17 leucine amino peptidase (M17 LAP) plays an important role in the hydrolysis of amino acids essential for growth and development of Plasmodium vivax
physiological function
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overexpression of leucine aminopeptidase 3 (LAP3) is involved in proliferation, migration, and invasion of several tumor cells and plays a crucial role in tumor metastasis, role of LAP3 in the regulation of cancer cell migration and invasion, overview. High LAP3 expression is correlated with the grade of malignancy, phenotypes, overview. LAP3 promotes fascin expression through the p38-Hsp27-NF-kappaB signaling pathway
physiological function
sperm-leucylaminopeptidases are required for male fertility as structural components of mitochondrial paracrystalline material in Drosophila melanogaster sperm
physiological function
the enzyme is not required for the growth of this parasite either in vitro or in vivo. Role of LAP-A in leucine starvation, overview
physiological function
the enzyme is not required for the growth of this parasite either in vitro or in vivo. Role of LAP-A in leucine starvation, overview
physiological function
the enzyme is not required for the growth of this parasite either in vitro or in vivo. Role of LAP-A in leucine starvation, overview
physiological function
the extracellular aminopeptidase PaAP can release amino acids from the N-terminus of peptide or protein. It modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide Psl and bacterial cell death. PaAP is a quorum sensing-regulated protein, thus its expression is largely activated at high bacterial density. PaAP might function as a nutrient recycler within a biofilm
physiological function
the leucine aminopeptidase is involved in kinetoplast DNA segregation in Trypanosoma brucei. TbLAP1 is a mt protein that dynamically associates with kDNA during the cell cycle. The protein localizes to kDNA and the umbilicus, the prominent proteinaceous structure which in the mammalian parasite Trypanosoma brucei connecting progeny kDNAs at late stages of segregation, indicating a role of TbLAP1 in resolving kDNA replication. TbLAP1 is required for correct segregation of kinetoplast DNA and the separation of daughter kinetoplast DNA, overview
physiological function
trigger enzymes combine metabolic function with regulation of gene expression. Escherichia coli aminopeptidase A (PepA) is a trigger enzyme endowed with catalytic activity and DNA-binding properties prominent in transcriptional regulation and site-specific DNA recombination. PepA is a repressor in its own right, capable of specifically inhibiting transcription initiation at promoter P1 of the carAB operon, encoding carbamoylphosphate synthase. Furthermore, PepA binding constrains a single positive supercoil in the carP1 control region. Such a topological event is understood to constitute an impediment to transcription initiation and may serve as a mechanism to regulate gene expression. The observed inhibitory effect of PepA at carP1 is specific
physiological function
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the extracellular aminopeptidase PaAP can release amino acids from the N-terminus of peptide or protein. It modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide Psl and bacterial cell death. PaAP is a quorum sensing-regulated protein, thus its expression is largely activated at high bacterial density. PaAP might function as a nutrient recycler within a biofilm
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physiological function
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enzyme Lap1 improves the degree of hydrolysis of casein and soy protein hydrolysates and also decreases their bitterness, indicating its potential utility in food production
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physiological function
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LAP may play regulatory roles in protein biosynthesis and degradation in basophilic cells
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physiological function
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M17 leucine amino peptidase (M17 LAP) plays an important role in the hydrolysis of amino acids essential for growth and development of Plasmodium vivax
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physiological function
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the extracellular aminopeptidase PaAP can release amino acids from the N-terminus of peptide or protein. It modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide Psl and bacterial cell death. PaAP is a quorum sensing-regulated protein, thus its expression is largely activated at high bacterial density. PaAP might function as a nutrient recycler within a biofilm
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physiological function
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the extracellular aminopeptidase PaAP can release amino acids from the N-terminus of peptide or protein. It modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide Psl and bacterial cell death. PaAP is a quorum sensing-regulated protein, thus its expression is largely activated at high bacterial density. PaAP might function as a nutrient recycler within a biofilm
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physiological function
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the extracellular aminopeptidase PaAP can release amino acids from the N-terminus of peptide or protein. It modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide Psl and bacterial cell death. PaAP is a quorum sensing-regulated protein, thus its expression is largely activated at high bacterial density. PaAP might function as a nutrient recycler within a biofilm
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physiological function
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the extracellular aminopeptidase PaAP can release amino acids from the N-terminus of peptide or protein. It modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide Psl and bacterial cell death. PaAP is a quorum sensing-regulated protein, thus its expression is largely activated at high bacterial density. PaAP might function as a nutrient recycler within a biofilm
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physiological function
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the extracellular aminopeptidase PaAP can release amino acids from the N-terminus of peptide or protein. It modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide Psl and bacterial cell death. PaAP is a quorum sensing-regulated protein, thus its expression is largely activated at high bacterial density. PaAP might function as a nutrient recycler within a biofilm
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physiological function
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the leucine aminopeptidase is involved in kinetoplast DNA segregation in Trypanosoma brucei. TbLAP1 is a mt protein that dynamically associates with kDNA during the cell cycle. The protein localizes to kDNA and the umbilicus, the prominent proteinaceous structure which in the mammalian parasite Trypanosoma brucei connecting progeny kDNAs at late stages of segregation, indicating a role of TbLAP1 in resolving kDNA replication. TbLAP1 is required for correct segregation of kinetoplast DNA and the separation of daughter kinetoplast DNA, overview
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physiological function
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leucine aminopeptidases (LAPs) are metallopeptidases that catalyze the hydrolysis of leucine residues and other N-terminal residues from proteins and peptides. The extracellular enzyme PtLAP executes the degradation of organic matters, contributes to the adaptive survival of microbe in deep-sea environment and may play important roles in marine biogeochemical cycles. The recombinant enzyme rPtLAP can significantly promote the proliferation of tumor cells, including the cell lines HCT116, BEL-7402 and Hela, while displays no effect on that of normal cell line 3T3
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physiological function
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the extracellular aminopeptidase PaAP can release amino acids from the N-terminus of peptide or protein. It modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide Psl and bacterial cell death. PaAP is a quorum sensing-regulated protein, thus its expression is largely activated at high bacterial density. PaAP might function as a nutrient recycler within a biofilm
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additional information
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regulation of the tick molecules involved in nutrient metabolism for the reproduction, including blood digestion and vitellogenesis, would help in controlling the tick population and tick-borne pathogens
additional information
recombinant Lap1 enzyme has a conserved functional charge/dipole complex and a hydrogen bond network of Zn2-D179-S228-Q177-D229-S158 around its active center. An acidic Asp residue is found at the bottom of the substrate binding pocket, which explains its preference for basic N-terminal amino acid substrates such as Arg and Lys. Three-dimensional structure modelling of rLap1 and substrate-docking analysis
additional information
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recombinant Lap1 enzyme has a conserved functional charge/dipole complex and a hydrogen bond network of Zn2-D179-S228-Q177-D229-S158 around its active center. An acidic Asp residue is found at the bottom of the substrate binding pocket, which explains its preference for basic N-terminal amino acid substrates such as Arg and Lys. Three-dimensional structure modelling of rLap1 and substrate-docking analysis
additional information
structure comparisons of plasmodial LAP-As from Trypanosoma brucei subsp. brucei, Trypanosoma cruzi, and Leishmania major, overview. Structural differences in LmLAP-A compared to TbLAP-A and TcLAP-A are mostly located in the loop regions
additional information
structure comparisons of plasmodial LAP-As from Trypanosoma brucei subsp. brucei, Trypanosoma cruzi, and Leishmania major, overview. Structural differences in LmLAP-A compared to TbLAP-A and TcLAP-A are mostly located in the loop regions
additional information
structure comparisons of plasmodial LAP-As from Trypanosoma brucei subsp. brucei, Trypanosoma cruzi, and Leishmania major, overview. Structural differences in LmLAP-A compared to TbLAP-A and TcLAP-A are mostly located in the loop regions
additional information
structure homology modelling of Plasmodium vivax LAP using the crystal structure of Plasmodium falciparum LAP, PDB ID 3KQX, as template, overview
additional information
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structure homology modelling of Plasmodium vivax LAP using the crystal structure of Plasmodium falciparum LAP, PDB ID 3KQX, as template, overview
additional information
the enzyme contains a signal peptide (residues 1-21), a peptidase_M1 domain (Pfam 01433, residues 32-398) and a leuk-A4-hydro_C domain (SMART 001263, residues 474-612) in PtLAP. Both of the putative substrate binding site GGMEN and zinc-binding motif HEXXHX18E in peptidase_M1 domain are conserved in PtLAP, locating from ressidues 282-286 and 309-332, respectively. The catalytic residues involved in aminopeptidase activity are Glu285 and Tyr395 in PtLAP, which probably act as a general base and a proton donor
additional information
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recombinant Lap1 enzyme has a conserved functional charge/dipole complex and a hydrogen bond network of Zn2-D179-S228-Q177-D229-S158 around its active center. An acidic Asp residue is found at the bottom of the substrate binding pocket, which explains its preference for basic N-terminal amino acid substrates such as Arg and Lys. Three-dimensional structure modelling of rLap1 and substrate-docking analysis
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additional information
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structure homology modelling of Plasmodium vivax LAP using the crystal structure of Plasmodium falciparum LAP, PDB ID 3KQX, as template, overview
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additional information
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the enzyme contains a signal peptide (residues 1-21), a peptidase_M1 domain (Pfam 01433, residues 32-398) and a leuk-A4-hydro_C domain (SMART 001263, residues 474-612) in PtLAP. Both of the putative substrate binding site GGMEN and zinc-binding motif HEXXHX18E in peptidase_M1 domain are conserved in PtLAP, locating from ressidues 282-286 and 309-332, respectively. The catalytic residues involved in aminopeptidase activity are Glu285 and Tyr395 in PtLAP, which probably act as a general base and a proton donor
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