Disease relevance of Aspartyl phosphate

• The RapA and RapB proteins are aspartyl phosphate phosphatases that specifically dephosphorylate the Spo0F approximately P intermediate response regulator of the phosphorelay signal transduction system for sporulation initiation in Bacillus subtilis [1].
• Formation of a beta-aspartyl phosphate intermediate by the vanadate-sensitive ATPase of Streptococcus faecalis [2].
• These results provide definitive evidence for the channeling of beta-aspartyl phosphate between aspartokinase and aspartate semialdehyde dehydrogenase in E. coli and suggest that ASADH may provide a bridge to channel the intermediates between the non-consecutive reactions of AK-HDH I [3].
• In Bacillus anthracis nine possible histidine sensor kinases can positively activate the system, while two response regulator aspartyl phosphate phosphatases of the Rap family negatively impact the pathway by dephosphorylating the Spo0F intermediate response regulator [4].
• We have characterized a novel family of response regulator aspartyl-phosphate (RAP) phosphatases found exclusively in gram-positive bacteria [5].

Psychiatry related information on Aspartyl phosphate

• ASDH showed cooperative behavior for aspartyl phosphate with a K(0.5) value of 37 microM [6].

High impact information on Aspartyl phosphate

• Like the Ca(2+) pumps of the sarco/endoplasmic reticulum (SERCAs), which pump Ca(2+) from the cytosol into the endoplasmic reticulum, the PMCAs belong to the family of P-type primary ion transport ATPases characterized by the formation of an aspartyl phosphate intermediate during the reaction cycle [7].
• The peptide derives from a domain just C-terminal to the aspartyl phosphate of the active site [8].
• The predicted L. donovani protein contained all the structural and functional domains expected to be present in a cation-transporting ATPase of the aspartyl phosphate class [9].
• Based on a structural model with fluorescein isothiocyanate bound at the ATP site, we suggest that the stability as well as the low fluorescence of this phosphoenzyme is due to a fluorescein-mediated cross-link between two cytoplasmic domains that prevents hydrolysis of the aspartyl phosphate [10].
• There is strong evidence that Asp-378 of the yeast PMA1 ATPase plays an essential role in ATP hydrolysis by forming a covalent beta-aspartyl phosphate reaction intermediate [11].

Biological context of Aspartyl phosphate

• A diagnostic feature of P-ATPases is a phosphorylation motif (DKTGTLT), located in the hydrophilic center of the polypeptide chain, within which the beta-aspartyl-phosphate reaction intermediate is formed [12].
• We screened the putative rap-phr (response regulator aspartyl-phosphate phosphatase-phosphatase regulator) systems identified in the Bacillus subtilis genome for a rap gene that affects aprE (alkaline protease gene) expression by using a multicopy plasmid [13].
• The yeast plasma-membrane H(+)-ATPase is a member of the P-family of cation transporters, which share a characteristic membrane topology together with consensus sequences for ATP binding and formation of a beta-aspartyl phosphate reaction intermediate [14].

Anatomical context of Aspartyl phosphate

• Identification of the phosphorylated intermediate of the Neurospora plasma membrane H+-ATPase as beta-aspartyl phosphate [15].
• Amino acid analyses of the Na[3H]BH4 reduction products obtained from membranes containing phosphorylated and dephosphorylated ATPase identified [3H]homoserine, the expected reduction product of beta-aspartyl phosphate, as the only additional tritiated reduction product in the samples from phosphorylated membranes [15].
• Interactions of phosphate groups of ATP and Aspartyl phosphate with the sarcoplasmic reticulum Ca2+-ATPase: an FTIR study [16].

Associations of Aspartyl phosphate with other chemical compounds

• Glutamate at the site of phosphorylation of nitrogen-regulatory protein NTRC mimics aspartyl-phosphate and activates the protein [17].
• The specific activities corresponding to the forward reaction of AK and reverse reaction of HSDH of AK-HSDH were 5.4 micromol of aspartyl phosphate produced min(-1) mg(-1) of protein and 18.8 micromol of NADPH formed min(-1) mg(-1) of protein, respectively [18].

Gene context of Aspartyl phosphate

• Characterization of the beta-aspartyl phosphate intermediate formed by the H+-translocating ATPase from the yeast Schizosaccharomyces pombe [19].
• The potential channeling of the intermediate beta-aspartyl phosphate between the aspartokinase of this bifunctional enzyme and aspartate semialdehyde dehydrogenase (ASADH), the enzyme that catalyzes the intervening reaction, has been examined [3].
• Because of the inherent lability of aspartyl phosphate bonds and the intrinsic phosphatase activity of CheB, the activated, phosphorylated form of CheB cannot be isolated for further characterization [20].
• The pump itself acts as an H+ for K+ exchange ATPase which is most probably composed of at least two peptides of 100 000 Mr. That catalytic cycle consists of formation and breakdown of a covalent aspartyl phosphate [21].

Analytical, diagnostic and therapeutic context of Aspartyl phosphate

• A combined electron microscopic and graded tryptic dissection analysis of the catalytic protein of pure Na,K-motive ATPase reveals that the aspartyl phosphate residue-carrying catalytic center is located at the utmost radius of the hydrophilic cytoplasmic domain [22].

References