Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P50583 (asymmetrical)
12,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cerebroside sulfotransferase (CST) catalyzes the final step in the synthesis of sulfatide (sulfogalactocerebroside) by transferring the sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to galactocerebroside. Orientation of CST was studied in vesicles enriched in this enzyme obtained from 21-d-old rat brain. Several lines of evidence indicate that CST is located on the luminal side of these vesicles. (a) Sulfation of endogenous galactocerebroside occurred in vesicles only in the presence of a detergent to render the membranes permeable to exogenous PAPS. (b) There is a pool of latent enzyme within the vesicle, which is released by Triton X-100. (c) CST is not destroyed by trypsin unless the vesicle membranes are first made permeable by Triton X-100. (d) Glycolipid substrate, when covalently attached to agarose beads, was not sulfated unless the enzyme was solubilized. These results are similar to those obtained with thiamine pyrophosphatase, which is known to be located within the lumen of the vesicles. This study establishes that an enzyme synthesizing a complex glycolipid is localized within Golgi-enriched vesicles. Since the product of the CST reaction must also be localized to the luminal side of the vesicles, it is most likely that sulfatide is located at the intraperiod line (outer layer) of myelin. The orientation of CST within the vesicle provides a mechanism for the asymmetrical assembly of glycolipids in bilayers.
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PMID:Topography of cerebroside sulfotransferase in Golgi-enriched vesicles from rat brain. 613 86

Zinc, adenosine 5'-phosphate (AMP), and pyrophosphatase greatly stimulate the synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) by rat liver lysyl-tRNA synthetase. The synthesis of Ap4A does not require lysine; thus the lysyl-adenylate complex is not required. The substrates have been determined to be adenosine 5'-triphosphate (ATP) and AMP with apparent Km values of 2.1 mM and 1.5 mM, respectively. A zinc-dependent hydrolysis of ATP and AMP has been shown to be associated with the synthetase. In the presence of zinc there is a direct correlation between both the amount of AMP formed and the amount of Ap4A synthesized by lysyl-tRNA synthetase. Ap4A acts as a competitive inhibitor for ATP in the aminoacylation reaction of lysyl-tRNA synthetase with a KI of 2.5 microM. Concentrations of Ap4A up to 12.5 microM do not inhibit the synthesis of Ap4A by lysyl-tRNA synthetase. This suggests that there may be more than one binding site for ATP on the enzyme.
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PMID:Characterization of a homogeneous complex of arginyl- and lysyl-tRNA synthetase: zinc and adenosine 5'-phosphate dependent synthesis of diadenosine 5',5'''-P1,P4-tetraphosphate. 662 5

Two types of tonoplast proton pumps, H+ -pyrophosphatase (V-PPase) and the H+ -ATPase (V-ATPase), establish the proton gradient that powers molecular traffic across the tonoplast thereby facilitating turgor regulation and nutrient homeostasis. However, how proton pumps regulate development remains unclear. In this study, we investigated the function of two types of proton pumps in Arabidopsis embryo development and pattern formation. While disruption of either V-PPase or V-ATPase had no obvious effect on plant embryo development, knocking out both resulted in severe defects in embryo pattern formation from the early stage. While the first division in wild-type zygote was asymmetrical, a nearly symmetrical division occurred in the mutant, followed by abnormal pattern formation at all stages of embryo development. The embryonic defects were accompanied by dramatic differences in vacuole morphology and distribution, as well as disturbed localisation of PIN1. The development of mutant cotyledons and root, and the auxin response of mutant seedlings supported the hypothesis that mutants lacking tonoplast proton pumps were defective in auxin transport and distribution. Taking together, we proposed that two tonoplast proton pumps are required for vacuole morphology and PIN1 localisation, thereby controlling vacuole and auxin-related developmental processes in Arabidopsis embryos and seedlings.
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PMID:Two tonoplast proton pumps function in Arabidopsis embryo development. 3156 67