Background[1-3]
Glycerophosphodiesterase phosphate domain 3 antibody is a type of polyclonal antibody that can specifically bind to the glycerophosphodiesterase phosphate domain 3 protein. It is mainly used for the in vitro detection of glycerol phosphodiesterase phosphate domain 3. .
Phosphodiesterases (PDEs) are a large multi-gene family. The development of selective phosphodiesterase inhibitors will open up new ideas for the treatment of various diseases.
PDEs is a large multi-gene family, which includes 11 types and more than 30 phosphodiesterase enzymes with different substrate specificities, enzyme kinetic characteristics, regulatory characteristics, and different cellular and subcellular distribution areas. Enzyme PDEs have similar structures and contain both regulatory and catalytic functional regions. More than 75% of the amino acid sequences in the catalytic regions of various types of PDEs are identical. Shows homology among family members. And determines the specificity for substrate or inhibitor. PDEs have different substrate specificities: PDEs 4, 7, and 8 act exclusively on cAMP, while PDEs 5, 6, and 9 act selectively on cGMP.
Immunohistochemistry of glycerophosphodiesterase phosphodomain 3
PDE3 binds to cAMP and cGMP with similar affinity, but hydrolyzes cGMP relatively poorly, so it is functionally regarded as specific for cAMP. cGMP acts as a negative regulator through competitive binding to the enzyme’s action site. . PDEs 1 and. 2 can hydrolyze both cAMP and cGMP, but PDE1 exerts different hydrolysis efficiencies on the two substrates due to its different subtypes.
The amino-terminal regulatory regions of PDEs are highly heterologous, reflecting the different cofactors of PDE family members. This region is the binding site for calmodulin (CaM) (PDE1), non-catalytic cGMP (PDE2, 5, 6) and transducin (PDE6). In addition, the amino-terminal parts of PDE3 and PDE4 also include target regions on the membrane, and PDE1, 3, 4, and 5 include protein kinase phosphorylation sites.
These phosphorylation sites can regulate catalytic activity and/or subcellular localization. The specific combination of substrates and cofactors makes the interaction between cAMP and cGMP systems possible. In platelets, nitro-expanding drugs or PDE5 inhibitors can increase cGMP, which in turn leads to the inhibition of PDE3 and a secondary increase in cAMP. On the contrary, in adrenal granulocytes, atrial natriuretic factor (atrial IIatri-tlret~factor, ANF) increases cGMP and inhibits cAMP-stimulated aldosterone synthesis through cGMP-mediated PDE2 activation.
Apply[4][5]
Functional study on the regulation of pathogen development by the cAMP phosphodiesterase gene of Phytophthora spp.
Using degenerate primer PCR method, two cAMP phosphodiesterase genes of Xanthomonas zeae were cloned, including 1 high-affinity cAMP phosphodiesterase gene (StH-PDE) and 1 low-affinity cAMP phosphodiesterase gene. enzyme gene (StL-PDE).
Create StH-PDE and StL-PDE gene knockout mutants respectively, and conduct functional studies on the target genes. The main research results are as follows: 1. A high-affinity cAMP phosphodiester was obtained from the genome of Xanthomonas cornis. enzyme gene and a low-affinity cAMP phosphodiesterase gene, named StH-PDE and StL-PDE respectively. Among them, the full length of StH-PDE gene DNA is 3208bp, containing 6 exons and 5 introns. The cDNA is 2898bp, encoding 965 amino acids. The calculated molecular weight of the encoded product is about 107.16kD; the full length of StL-PDE gene DNA is 5054bp. , containing 5 exons and 4 introns, the cDNA is 3089bp, encoding 1019 amino acids. The introns of the above genes basically conform to the GT-AG rule.
2. The amino acid sequence of the StH-PDE encoded product has a conservation similarity of 33.12% to 36.60% with the H-PDE amino acid sequence of various pathogenic fungi, such as Aspergillus fumigatus, Botrytis cinerea, Metarhizium acridum, Neosartorya fischeri, etc. Type I cAMP phosphodiesterase catalytic domain, type I cAMP phosphodiesterase conserved site and metal ion-dependent phosphohydrolase conserved “HD” motif (HD motif), but the similarity with StL-PDE is only is 20.33%, indicating that the two genes belong to different phosphodiesterase groups.
The amino acid sequence of the StL-PDE encoded product has a similarity of 21.98% and 23.06% with the L-PDE amino acid sequence of pathogenic fungi such as Trichoderma reesei, Beauveria bassiana, Colletotrichum higginsianum, Talaromyced stipitatus and other pathogenic fungi, which contains type II cAMP unique to L-PDE Phosphodiesterase catalytic domain.
