Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.23 (beta-galactosidase)
 14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. alpha 1-Proteinase inhibitor (alpha 1-antitrypsin) is excreted in a deglycosylated form (M(r) 38,000) in the faeces of healthy subjects and in patients with quiescent Crohn's disease. By contrast, in most patients with active Crohn's disease, alpha 1-proteinase inhibitor is excreted in a glycosylated form (M(r) 51,000). 2. Faecal extracts containing deglycosylated alpha 1-proteinase inhibitor are able to deglycosylate alpha 1-proteinase inhibitor by an exoglycosidic process. Conversely, we demonstrate that in faecal extracts from patients excreting glycosylated alpha 1-proteinase inhibitor, glycosidase activities, such as N-acetyl-beta-glucosaminidase (EC 3.2.1.30), alpha-mannosidase (EC 3.2.1.24) and particularly beta-galactosidase (EC 3.2.1.23), are strongly decreased. 3. Degradation of glycosidases by proteases could not explain the decreased glycosidase activity in these faecal extracts. 4. Our data suggest that a modification of the bacterial colonic flora (or of its metabolic activity) occurs in most patients with active Crohn's disease and could be responsible for an impaired colonic salvage of carbohydrates.
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PMID:Decreased faecal exoglycosidase activities identify a subset of patients with active Crohn's disease. 133 Apr 2

The VirB4 ATPase of Agrobacterium tumefaciens, a putative component of the T-complex transport apparatus, associates with the cytoplasmic membrane independently of other products of the Ti plasmid. VirB4 was resistant to extraction from membranes of wild-type strain A348 or a Ti-plasmidless strain expressing virB4 from an IncP replicon. To evaluate the membrane topology of VirB4, a nested deletion method was used to generate a high frequency of random fusions between virB4 and 'phoA, which encodes a periplasmically active alkaline phosphatase (AP) deleted of its signal sequence. VirB4::PhoA hybrid proteins exhibiting AP activity in Escherichia coli and A. tumefaciens had junction sites that mapped to two regions, between residues 58 and 84 (region 1) and between residues 450 and 514 (region 2). Conversely, VirB4::beta-galactosidase hybrid proteins with junction sites mapping to regions 1 and 2 exhibited low beta-galactosidase activities and hybrid proteins with junction sites elsewhere exhibited high beta-galactosidase activities. Enzymatically active VirB5::PhoA hybrid proteins had junction sites that were distributed throughout the length of the protein. Proteinase K treatment of A. tumefaciens spheroplasts resulted in the disappearance of the 87-kDa VirB4 protein and the concomitant appearance of two immunoreactive species of approximately 35 and approximately 45 kDa. Taken together, our data support a model in which VirB4 is topologically configured as an integral cytoplasmic membrane protein with two periplasmic domains.
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PMID:The VirB4 ATPase of Agrobacterium tumefaciens is a cytoplasmic membrane protein exposed at the periplasmic surface. 899 Feb 98

To avoid phagocytosis, parasites may mask themselves with host-like molecules that prevent recognition as nonself or they may produce substances that interfere with host cellular defenses. The protozoan parasite Haplosporidium nelsoni, which causes MSX disease in the eastern oyster Crassostrea virginica, is not ingested by host hemocytes. To assess potential avoidance mechanisms, oyster hemocytes were incubated with plasmodial stages of the parasite that had been pretreated with one of a variety of enzymes (proteases and carbohydrases) to alter surface molecules or with metabolic inhibitors to prevent the synthesis or active uptake of "masking" molecules, as well as the production and discharge of inhibitory substances. The maximum increase in phagocytosis resulting from treatment with carbohydrases was 12.5% (beta-galactosidase) and with proteases was 18% (Proteinase K). Inhibitors of aerobic metabolism resulted in a similar level of enhancement. In contrast, treatment of parasites with the glycolysis inhibitor iodoacetate enhanced phagocytosis by up to 66%. Thus, the process that obstructs phagocytosis involves aerobic and, especially, anaerobic pathways. The greater effect of a metabolic inhibitor compared to enzymes suggests that the mechanism involves more than just surface modification and may include the production of interference molecules.
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PMID:Altered response of oyster hemocytes to Haplosporidium nelsoni (MSX) plasmodia treated with enzymes or metabolic inhibitors. 970 17

The ability to rearrange membranes is a unique feature of nonstructural proteins 2B, 2C, and 2BC of some picornaviruses. To analyze in detail membrane binding of the respective proteins of hepatitis A virus (HAV), they were transiently expressed in the vaccinia/T7 system, and their effect on membrane permeability was studied using beta-galactosidase as reporter. Although 2C had no effect, the significantly increased reporter activity observed in the extracellular space of 2B- and 2BC-expressing cells points to a specific effect of HAV proteins 2B and 2BC on membrane permeability. In biochemical fractionation studies, HAV 2C and 2BC showed properties of intregral membrane proteins, whereas 2B was associated with membranes as a peripheral protein. Proteinase 3C-mediated cleavage of precursor 2BC in vivo was most efficient when the enzyme was coexpressed in its precursor forms P3 or 3ABC, which both include the membrane-anchoring domain 3A. 3ABC showed the same solubility pattern as 2BC, suggesting that colocalization of 2BC and 3ABC might be required for the efficient liberation of 2B and 2C and occurs on membranes that have been proposed as the site of viral RNA replication.
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PMID:Membrane permeability induced by hepatitis A virus proteins 2B and 2BC and proteolytic processing of HAV 2BC. 987 31