Minerals as co-ezymes Dr. Shariq Syed Shariq AIKC/SYB/2014.

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Presentation transcript:

Minerals as co-ezymes Dr. Shariq Syed Shariq AIKC/SYB/2014

Role of Minerals Minerals act as cofactors for enzyme reactions Maintain pH balance within body Facilitate transfer of nutrients across cell membranes Maintain proper nerve conduction Help contract, relax muscles Regulate body tissue growth Structural, functional support for body Shariq AIKC/SYB/2014

Role of Minerals Minerals divided in 2 category based on amount needed in body Major Minerals (Macro-minerals) Needed in greater amount in diets, body Micro Minerals (Trace-minerals) Needed in small quantities Shariq AIKC/SYB/2014

Composition of Minerals in body Shariq AIKC/SYB/2014

Copper Copper (Cu) is an essential trace element shifts between the cuprous (Cu1+) and cupric (Cu2+) forms The ability of copper to easily accept and donate electrons explains its important role in oxidation-reduction (redox) reactions Capturing free radicals Shariq AIKC/SYB/2014

Copper Copper enzymes (cuproenzymes) regulate various physiologic pathways energy production iron metabolism connective tissue maturation neurotransmission Shariq AIKC/SYB/2014

Copper Energy production: Copper-dependent enzyme, cytochrome c oxidase, plays a critical role in cellular energy production Connective tissue formation: lysyl oxidase, is required for the cross-linking of collagen and elastin which are essential for the formation of strong and flexible connective tissue Shariq AIKC/SYB/2014

Copper Iron Metabolism: Four copper-containing enzymes (multi-copper oxidases (MCO) or ferroxidases) These enzymes have capacity to oxidize ferrous iron (Fe2+) to ferric iron (Fe3+) Ferric iron can be loaded onto the protein transferrin for transport to the site of red blood cell formation Shariq AIKC/SYB/2014

Copper CNS Functioning: A number of reactions essential to normal function of the brain and nervous system are catalyzed by cuproenzymes Neurotransmitter synthesis: Dopamine b-hyroxylase Dopamine Norepinephrine Shariq AIKC/SYB/2014

Iron (Fe) longest and best described history among all the micronutrients In humans, iron is an essential component of hundreds of proteins and enzymes key element in the metabolism Shariq AIKC/SYB/2014

Biological role of Iron (Fe) Oxygen transport and storage: Heme is an iron-containing compound Hemoglobin and myoglobin are heme-containing proteins that are involved in the transport and storage of oxygen Electron transport and energy metabolism: Cytochromes are heme-containing compounds serve as electron carriers during the synthesis of ATP Cytochrome P450 is a family of enzymes important role in the metabolism Heme Hemoglobin is the primary protein found in red blood cells and represents about two thirds of the body's iron. The vital role of hemoglobin in transporting oxygen from the lungs to the rest of the body is derived from its unique ability to acquire oxygen rapidly during the short time it spends in contact with the lungs and to release oxygen as needed during its circulation through the tissues. Myoglobin functions in the transport and short-term storage of oxygen in muscle cells, helping to match the supply of oxygen to the demand of working muscles The heme group is a highly-conjugated ring system (which allows its electrons to be very mobile) surrounding a metal ion, which readily interconverts between the oxidation states. For many cytochromes, the metal ion present is that of iron, which interconverts between Fe2+ (reduced) and Fe3+ (oxidized) states (electron-transfer processes) or between Fe2+ (reduced) and Fe3+(formal, oxidized) states (oxidative processes). Cytochromes are, thus, capable of performing oxidation and reduction. Because the cytochromes (as well as other complexes) are held within membranes in an organized way, the redox reactions are carried out in the proper sequence for maximum efficiency. In the process of oxidative phosphorylation, which is the principal energy-generating process undertaken by organisms, other membrane-bound and -soluble complexes and cofactors are involved in the chain of redox reactions, with the additional net effect that protons (H+) are transported across the mitochondrial inner membrane. The resulting transmembrane proton gradient([protonmotive force]) is used to generate ATP, which is the universal chemical energy currency of life. ATP is consumed to drive cellular processes that require energy (such as synthesis of macromolecules, active transport of molecules across the membrane, and assembly of flagella). Shariq AIKC/SYB/2014

Biological role of Iron (Fe) Antioxidant functions: Catalase and peroxidases are heme-containing enzymes They protect cells against the accumulation of hydrogen peroxide, a potentially damaging reactive oxygen species (ROS) The enzyme catalyze a reaction that converts hydrogen peroxide to water and oxygen Shariq AIKC/SYB/2014

Molybdenum The molybdenum atom is part of the molybdenum cofactor in the active site of four enzymes in humans: sulfite oxidase xanthine oxidase aldehyde oxidase mitochondrial amidoxime reducing component Molybdenum Cofactor Shariq AIKC/SYB/2014

Biological role of Molybdenum Sulfite oxidase: catalyzes the transformation of sulfite to sulfate Necessary reaction for the metabolism of sulfur-containing amino acids (methionine and cysteine) Xanthine oxidase: catalyzes the breakdown of nucleotides (precursors to DNA and RNA) to form uric acid Uric acid contributes to the plasma antioxidant capacity of the blood methionine cysteine Shariq AIKC/SYB/2014

Selenium Selenium is a trace element that is essential in small amounts, but like all essential elements, it is toxic at high levels Humans require selenium for the function of a number of selenium-dependent enzymes, also known as selenoproteins At least 25 selenoproteins have been identified, but the metabolic functions have been identified for only about one-half of them Shariq AIKC/SYB/2014

Biological role of Selenium Glutathione Peroxidases Anti-oxidant enzymes that reduce reactive oxygen species Selenoprotein P transport protein for selenium Anti-oxidant enzyme Selenophosphate synthetase Incorporation of selenocysteine into selenoproteins is directed by enzyme selenophosphate synthetase Shariq AIKC/SYB/2014

Zinc Zinc-dependent enzymes can be found in all known classes of enzymes Over 300 different enzymes depend on zinc for their ability to catalyze vital chemical reactions cellular metabolism reactions are zinc-dependent Zinc plays important roles in growth and development, the immune response, neurological function, and reproduction On the cellular level, the function of zinc can be divided into three categories: 1) catalytic, 2) structural, and 3) regulatory Shariq AIKC/SYB/2014

Biological role of Zinc Two examples of zinc-containing enzymes are carbonic anhydrase and carboxypeptidase, which are vital to the processes of carbon dioxide (CO2) regulation and digestion of proteins Carbonic anhydrase converts CO2 into bicarbonate and the same enzyme transforms the bicarbonate back into CO2 for exhalation through the lungs Carboxypeptidase cleaves peptide linkages during digestion of proteins Shariq AIKC/SYB/2014