Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.3.4.6 (urease)
 7,490 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Four microbial enzymes are known to require nickel: hydrogenase, methyl coenzyme M reductase, carbon monoxide dehydrogenase, and urease. Recent biochemical and molecular biological experiments have provided clear evidence for the existence of multiple auxiliary genes that facilitate nickel incorporation into urease and hydrogenase. Similarly, accessory factors are also likely to be required for the other two enzymes. One of the urease-related genes (ureE) encodes a cytoplasmic protein that has been purified and shown to bind nickel reversibly. We propose that the UreE protein serves as a nickel donor to urease apoprotein. A second urease-related auxiliary gene (ureG) possesses a sequence motif that is found in ATP- and GTP-binding proteins. We have shown that nickel incorporation into urease requires energy and speculate that the UreG protein may serve as an energy transducer, coupling the energy of NTP hydrolysis to metallocenter incorporation. The UreG protein is related in sequence to HypB, a protein that has been proposed to function in nickel processing in hydrogenases. Hence, the mechanisms for metallocenter biosynthesis in these two dissimilar enzymes may have evolved from a common nickel incorporation system.
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PMID:Nickel enzymes in microbes. 802 91

Nickel is an essential nutrient for selected microorganisms where it participates in a variety of cellular processes. Many microbes are capable of sensing cellular nickel ion concentrations and taking up this nutrient via nickel-specific permeases or ATP-binding cassette-type transport systems. The metal ion is specifically incorporated into nickel-dependent enzymes, often via complex assembly processes requiring accessory proteins and additional non-protein components, in some cases accompanied by nucleotide triphosphate hydrolysis. To date, nine nickel-containing enzymes are known: urease, NiFe-hydrogenase, carbon monoxide dehydrogenase, acetyl-CoA decarbonylase/synthase, methyl coenzyme M reductase, certain superoxide dismutases, some glyoxylases, aci-reductone dioxygenase, and methylenediurease. Seven of these enzymes have been structurally characterized, revealing distinct metallocenter environments in each case.
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PMID:Nickel uptake and utilization by microorganisms. 1282 70

With the world's ever increasing human population, the issues related to environmental degradation of toxicant chemicals are becoming more serious. Humans have accelerated the emission to the environment of many organic and inorganic pollutants such as pesticides, salts, petroleum products, acids, heavy metals, etc. Among different environmental heavy-metal pollutants, Ni has gained considerable attention in recent years, because of its rapidly increasing concentrations in soil, air, and water in different parts of the world. The main mechanisms by which Ni is taken up by plants are passive diffusion and active transport. Soluble Ni compounds are preferably absorbed by plants passively, through a cation transport system; chelated Ni compounds are taken up through secondary, active-transport-mediated means, using transport proteins such as permeases. Insoluble Ni compounds primarily enter plant root cells through endocytosis. Once absorbed by roots, Ni is easily transported to shoots via the xylem through the transpiration stream and can accumulate in neonatal parts such as buds, fruits, and seeds. The Ni transport and retranslocation processes are strongly regulated by metal-ligand complexes (such as nicotianamine, histidine, and organic acids) and by some proteins that specifically bind and transport Ni. Nickel, in low concentrations, fulfills a variety of essential roles in plants, bacteria, and fungi. Therefore, Ni deficiency produces an array of effects on growth and metabolism of plants, including reduced growth, and induction of senescence, leaf and meristem chlorosis, alterations in N metabolism, and reduced Fe uptake. In addition, Ni is a constituent of several metallo-enzymes such as urease, superoxide dismutase, NiFe hydrogenases, methyl coenzyme M reductase, carbon monoxide dehydrogenase, acetyl coenzyme-A synthase, hydrogenases, and RNase-A. Therefore, Ni deficiencies in plants reduce urease activity, disturb N assimilation, and reduce scavenging of superoxide free radical. In bacteria, Ni participates in several important metabolic reactions such as hydrogen metabolism, methane biogenesis, and acetogenesis. Although Ni is metabolically important in plants, it is toxic to most plant species when present at excessive amounts in soil and in nutrient solution. High Ni concentrations in growth media severely retards seed germinability of many crops. This effect of Ni is a direct one on the activities of amylases, proteases, and ribonucleases, thereby affecting the digestion and mobilization of food reserves in germinating seeds. At vegetative stages, high Ni concentrations retard shoot and root growth, affect branching development, deform various plant parts, produce abnormal flower shape, decrease biomass production, induce leaf spotting, disturb mitotic root tips, and produce Fe deficiency that leads to chlorosis and foliar necrosis. Additionally, excess Ni also affects nutrient absorption by roots, impairs plant metabolism, inhibits photosynthesis and transpiration, and causes ultrastructural modifications. Ultimately, all of these altered processes produce reduced yields of agricultural crops when such crops encounter excessive Ni exposures.
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PMID:Essential roles and hazardous effects of nickel in plants. 2191 27

Nickel enzymes, present in archaea, bacteria, plants, and primitive eukaryotes are divided into redox and nonredox enzymes and play key functions in diverse metabolic processes, such as energy metabolism and virulence. They catalyze various reactions by using active sites of diverse complexities, such as mononuclear nickel in Ni-superoxide dismutase, glyoxylase I and acireductone dioxygenase, dinuclear nickel in urease, heteronuclear metalloclusters in [NiFe]-carbon monoxide dehydrogenase, acetyl-CoA decarbonylase/synthase and [NiFe]-hydrogenase, and even more complex cofactors in methyl-CoM reductase and lactate racemase. The presence of metalloenzymes in a cell necessitates a tight regulation of metal homeostasis, in order to maintain the appropriate intracellular concentration of nickel while avoiding its toxicity. As well, the biosynthesis and insertion of nickel active sites often require specific and elaborated maturation pathways, allowing the correct metal to be delivered and incorporated into the target enzyme. In this review, the phylogenetic distribution of nickel enzymes will be briefly described. Their tridimensional structures as well as the complexity of their active sites will be discussed. In view of the latest findings on these enzymes, a special focus will be put on the biosynthesis of their active sites and nickel activation of apo-enzymes.
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PMID:Structure, function, and biosynthesis of nickel-dependent enzymes. 3202 53