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Dipeptidase

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Hydrolyzes a wide range of dipeptides. Highest activity against Ala-Gln.

Below are the list of possible Dipeptidase products. If you cannot find the target and/or product is not available in our catalog, please click here to contact us and request the product or submit your request for custom elisa kit production, custom recombinant protein production or custom antibody production. Custom ELISA Kits, Recombinant Proteins and Antibodies can be designed, manufactured and produced according to the researcher's specifications.
 

Dipeptidase

 Dipeptidase ELISA Kit
 Dipeptidase Recombinant
 Dipeptidase Antibody
Hydrolyzes a wide range of dipeptides. Highest activity against Ala-Gln.
 pepD ELISA Kit
 pepD Recombinant
 pepD Antibody
 BL0479 ELISA Kit
 BL0479 Recombinant
 BL0479 Antibody
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Dipeptidase 1

 Dipeptidase 1 ELISA Kit
 Dipeptidase 1 Recombinant
 Dipeptidase 1 Antibody
Also known as Dipeptidase 1 (43 kDa renal band 3-related protein) (Microsomal dipeptidase).
Hydrolyzes a wide range of dipeptides. Implicated in the renal metabolism of glutathione and its conjugates. Converts leukotriene D4 to leukotriene E4; it may play an important role in the regulation of leukotriene activity.
 DPEP1 ELISA Kit
 DPEP1 Recombinant
 DPEP1 Antibody
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Dipeptidase 2

 Dipeptidase 2 ELISA Kit
 Dipeptidase 2 Recombinant
 Dipeptidase 2 Antibody
Probable metalloprotease which hydrolyzes leukotriene D4 (LTD4) into leukotriene E4 (LTE4).
 Dpep2 ELISA Kit
 Dpep2 Recombinant
 Dpep2 Antibody
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Dipeptidase 3

 Dipeptidase 3 ELISA Kit
 Dipeptidase 3 Recombinant
 Dipeptidase 3 Antibody
Probable metalloprotease which hydrolyzes cystinyl-bis-glycine. May be involved in meiosis ().
 Dpep3 ELISA Kit
 Dpep3 Recombinant
 Dpep3 Antibody
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Dipeptidase A

 Dipeptidase A ELISA Kit
 Dipeptidase A Recombinant
 Dipeptidase A Antibody
Hydrolyzes a wide range of dipeptides but unable to hydrolyze dipeptides containing proline. Highest activity against Met-Ala.
 pepDA ELISA Kit
 pepDA Recombinant
 pepDA Antibody
 pepD ELISA Kit
 pepD Recombinant
 pepD Antibody
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Dipeptidase gliJ

 Dipeptidase gliJ ELISA Kit
 Dipeptidase gliJ Recombinant
 Dipeptidase gliJ Antibody
Also known as Dipeptidase gliJ (Gliotoxin biosynthesis protein J).
Dipeptidase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to
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form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036). In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876).
 gliJ ELISA Kit
 gliJ Recombinant
 gliJ Antibody
 AFUA_6G09650 ELISA Kit
 AFUA_6G09650 Recombinant
 AFUA_6G09650 Antibody
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Dipeptidase sirJ

 Dipeptidase sirJ ELISA Kit
 Dipeptidase sirJ Recombinant
 Dipeptidase sirJ Antibody
Also known as Dipeptidase sirJ (Sirodesmin biosynthesis protein J).
Dipeptidase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola (PubMed:15387811, PubMed:18272357, PubMed:19762440). SirD catalyzes th
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e O-prenylation of L-tyrosine (L-Tyr) in the presence of dimethylallyl diphosphate (DMAPP) to yield 4-O-dimethylallyl-L-Tyr, and therefore represents probably the first pathway-specific enzyme in the biosynthesis of sirodesmin PL (PubMed:19762440, PubMed:21038099, PubMed:24083562). 4-O-dimethylallyl-L-Tyr, then undergoes condensation with L-Ser in a reaction catalyzed by the non-ribosomal peptide synthase sirP to form the diketopiperazine (DKP) backbone (PubMed:18272357). Further bishydroxylation of the DKP performed by the cytochrome P450 monooxygenase sirC leads to the production of the intermediate phomamide (PubMed:27390873). This step is essential to form the reactive thiol group required for toxicity of sirodesmin PL (PubMed:27390873). The next steps of sirodesmin biosynthesis are not well understood yet, but some predictions could be made from intermediate compounds identification (PubMed:18272357). Phomamide is converted into phomalizarine via oxidation, probably by sirT (PubMed:18272357). Further oxidation, methylation (by sirM or sirN) and reduction steps convert phomalizarine to deacetyl sirodesmin (PubMed:18272357). Finally, acetyltransferase sirH probably acetylates deacetyl sirodesmin to produce sirodesmin PL (PubMed:18272357).
 sirJ ELISA Kit
 sirJ Recombinant
 sirJ Antibody
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Dipeptidase tcpJ

 Dipeptidase tcpJ ELISA Kit
 Dipeptidase tcpJ Recombinant
 Dipeptidase tcpJ Antibody
Also known as Dipeptidase tcpJ (Thiocalpurine biosynthesis protein J).
Dipeptidase; part of the gene cluster that mediates the biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) lacking the reactive thiol group important for toxicity (PubMed:27390873). Firstly, L-tyrosine is prenylated by tcpD, before undergoing condensation with L-glycine in a reaction catalyzed by the NRPS
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tcpP leading to the diketopiperazine (DKP) backbone (PubMed:27390873). Afterwards the alpha-carbon of tyrosine is oxidized by the cytochrome P450 tcpC to form a hydroxyl group (PubMed:27390873). However, in contrast other ETP biosynthesis pathways studied so far, tcpC is not able to bishydroxylate the DKP at both alpha-carbon positions, but hydroxylates the alpha-carbon of the tyrosine part and the nitrogen of the glycine part (PubMed:27390873). The next steps involve an alpha,beta-elimination reaction catalyzed by tcpI, a methylation by the methyltransferase tcpN the action of the four enzyme cascade tcpG/K/J/I (PubMed:27390873). Due to a dysfunctional cytochrome P450 monooxygenase tcpC, the pathway leads to the biosynthesis of probable non-toxic metabolites lacking the reactive thiol group (PubMed:27390873).
 tcpJ ELISA Kit
 tcpJ Recombinant
 tcpJ Antibody
 CPUR_02673 ELISA Kit
 CPUR_02673 Recombinant
 CPUR_02673 Antibody
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