Application of Phospholipid Phosphohydrolase 1 Antibodies_Industrial Additives

Background^[1-3]

Phospholipid phosphohydrolase 1 antibody is a type of polyclonal antibody that can specifically bind to phospholipid phosphohydrolase 1. It is mainly used in experiments related to the detection of phospholipid phosphohydrolase 1.

Phosphatase is an enzyme that can dephosphorylate the corresponding substrate, that is, by hydrolyzing phosphate monoesters to remove the phosphate group on the substrate molecule and generate phosphate ions and free hydroxyl groups. The role of phosphatase is the opposite of that of kinase. Kinase is a phosphorylase that can use energy molecules, such as ATP, to add phosphate groups to corresponding substrate molecules. One phosphatase that is ubiquitous in many organisms is alkaline phosphatase.

Phospholipid phosphohydrolase 1 antibody

The phosphorylation effect of phosphatase is opposite to that of kinase or phosphorylase. Phosphorylation can activate or inactivate an enzyme or enable a protein-protein interaction to occur; therefore, phosphatases are required for controlling phosphorylation in many signal transduction pathways. It is worth mentioning that phosphorylation or dephosphorylation does not necessarily correspond to enzyme activation or inhibition, and some enzymes have multiple phosphorylation sites involved in the regulation of activation or inhibition. For example, cyclin-dependent kinase (CDK) has multiple specific amino acid residues that can be phosphorylated, activating or inhibiting the phosphorylation corresponding to different residues. The reason why phosphate is important for signaling is that it can regulate the action of the protein it binds to; and removing phosphate has the opposite effect (if phosphorylation is activation, dephosphorylation is inhibition function), phosphatase plays an important role here.

Apply^[4][5]

For genome-wide study of the impact of phosphohydrolase on lycopene synthesis

Using Escherichia coli DH1 as the host strain, based on the existing initial strain that produces lycopene.

First, the copy number of crt EIB, a key gene in the lycopene synthesis pathway, was increased at the smf site of the genome of the initial strain. The characterization results showed that compared with the initial strain, the lycopene production was increased by 34%, and This bacterium was named lyc011.

Secondly, there is a series of phosphorylated intermediate metabolites of rubber additives in the MEP pathway of E. coli, and phosphohydrolase with a broad substrate spectrum may have catalytic activity on these intermediates.

Through direct prediction and systems biology methods, the phosphohydrolase in the DH1 genome that may have catalytic activity for intermediate metabolites in the lycopene synthesis pathway was analyzed and predicted. Finally, 57 phosphohydrolase genes were obtained.

Use the principle of CRISPR interference (CRISPRi) to screen the effects of these genes on lycopene production. To this end, we first successfully constructed 57 plasmids containing double single guide RNA (sg RNA), targeting the above 57 genes. The pd Cas9 plasmid and sg RNA expression plasmid were introduced into the initial strain lyc011, and finally through fermentation characterization, 15 phosphohydrolase genes that had a positive effect on increasing lycopene production were successfully screened: yjj G, aph A, nag D,yqa B,yid A,pph A,bac A,glp Q,pgp B,spo T,cpd B,nud J,dgt,pho Q. Taking the endogenous phosphohydrolase system of Escherichia coli as a case study, we can gain a deeper understanding of the impact of enzyme substrate non-specificity on metabolic systems, especially integrated heterologous pathways.

By decoupling the interaction between heterologous pathways and endogenous metabolism, this method has the potential to be used as a general strategy in future metabolic engineering research.