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ATP/ADP UTP,GTP,CTP
(rxn type, enzyme class, cosub or prosthetic) |
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transfer phosphoryl group kinases, synthases cosubstrate |
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pyridoxal phosphate
(rxn type, enzyme class, cosub or prosthetic) |
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transfers amine group transaminases prosthetic group |
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biotin
(rxn type, enzyme class, cosub or prosthetic) |
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transfers CO2 group carboxylases prosthetic group |
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CoenzymeA
(rxn type, enzyme class, cosub or prosthetic) |
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transfer acyl group pyruvate dehydrogenase prosthetic group |
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transfer acyl group pyruvate dehydrogenase prosthetic group |
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thiamine pyrophosphate (TTP)
(rxn type, enzyme class, cosub or prosthetic) |
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transfer activated aldehyde pyruvate dehydrogenase prosthetic group |
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cobalamin
(rxn type, enzyme class, cosub or prosthetic) |
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transfer methyl, methylene, formyl transferases, isomerases prosthetic group |
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tetrahydrofolate
(rxn type, enzyme class, cosub or prosthetic) |
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transfer methyl, methylene, formyl transferases, isomerases cosubstrate |
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S-adenosylmethionine
(rxn type, enzyme class) |
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transfer methyl, methylene, formyl transferases, isomerases |
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Tetrahydribiopterin
(rxn type, enzyme class) |
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transfer methyl, methylene, formyl transferases, isomerases |
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NAD+, NADP+ NADH, NADPH
(rxn type, enzyme class, cosub or prosthetic) |
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transfer 2e- and H+ dehydrogenases cosubstrate |
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FAD, FMN FADH2, FMNH2
(rxn type, enzyme class, cosub or prosthetic) |
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transfer 2e- + 2H+ (2 at a time) dehydrogenases prosthetic group |
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Ubiquinone, CoQ
(rxn type, enzyme class, cosub or prosthetic) |
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Definition
transfer 2e- + 2H+ (1 at a time) electron transport cosubstrate |
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Heme-Fe
(rxn type, enzyme class, cosub or prosthetic) |
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transfer e- cytochromes prosthetic group |
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Vitamin C
(coenzyme assoc., disease of deficiency, solubility) |
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Coenzyme: Ascorbic Acid Disease: Scurvy Solubility: Water |
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Vitamin A
(coenzyme assoc., disease of deficiency) |
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Definition
Coenzyme: Retinol, retinal, retinoic acid Disease: night vision loss, kerantinitis Solubility: lipid |
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Vitamin D
(coenzyme assoc., disease of deficiency) |
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Coenzyme: Choleccalciferol Disease: Rickets, osteiomalacia Solubility: lipid |
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Vitamen E
(coenzyme assoc., disease of deficiency) |
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Coenzyme: alpha-tocopherol Disease: Anemia of newborn Solubility: lipid |
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Vitamin K
(coenzyme assoc., disease of deficiency) |
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Definition
Coenzyme: Vitamin K Disease: Hemorrhagic disease of newborn Solubility: lipid |
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Pyridoxine (B6)
(coenzyme assoc., disease of deficiency) |
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Definition
Coenzyme: Pyridoxal phosphate Disease: Rare, isoniazid induced (TB treatment) Solubility: WAter |
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Biotin
(coenzyme assoc., disease of deficiency) |
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Coenzyme: Biotin Disease: intestinal flora synthesis (rare) Solubility: water |
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Pantothenic acid (B5)
(coenzyme assoc., disease of deficiency) |
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Coenzyme: Coenzyme A Disease: Burning foot syndrome Solubility: Water |
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Thiamin (B1)
(coenzyme assoc., disease of deficiency) |
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Coenzyme: Thiamin pyrophosphate (TTP) Disease: BeriBeri, Wernicke-Korsakoff syndrome Solubility: Water |
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Cobalamin (B12)
(coenzyme assoc., disease of deficiency) |
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Coenzyme: Cobalamin Disease: Pernicious anemia Solubility: Water |
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Folic Acid
(coenzyme assoc., disease of deficiency) |
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Coenzyme: Tetrahydrofolate Disease: Megaloblastic anemia (fetal development) Solubility: Water |
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Niacin (B3)
(coenzyme assoc., disease of deficiency) |
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Coenzyme: NAD+, NADP+ Disease: pellagra (Trp-deficiency-link) Solubility: WAter |
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Riboflavin (B2)
(coenzyme assoc., disease of deficiency) |
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Definition
Coenzyme: FAD, FADH2, FMN, FMNH2 Disease: dermatisis, cheilosis, glossitis Solubility: Water |
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generate useful energy and small molecule building blocks |
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build useful molecules but require useful energy to do so |
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ratio of conc. of the products and reactants of a particular reaction in the cell |
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1st law of thermodynamics |
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energy is conserved, not created or destroyed, but can change forms |
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2nd law of thermodynamics |
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spontaneous processes proceed inthe direction of greater chaos, entropy is maximized in the universe |
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disease associated with decreased or defective collagen production/processing, progressive bone and CT deformities, varies in severity |
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form in which collagen is synthesized and secreted from cell |
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enzymes that post-process procollagen into collagen extracellularly |
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triple helix form of collagen in the ECM, basic unit of collagen |
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poly-proline type II helix |
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triple helix form of collagen structure |
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mostly glycans with some protein for structure, part of the ECM; made of glycosaminoglycans and protein |
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long linear chains of disaccharide repeasts: one sac. is a amino sugar, the other is a uronic acid |
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core protein (in proteoglycans) |
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non-covalently attached around central strand of glycosaminoglycans, attachment strengthen by linking protein; a heavily modified protein |
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linking protein (in proteoglycans) |
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covalently attached to central strand of glycosaminoglycans, |
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remove the terminal sialic acids from glycoproteins to signal the glycoprotein's removal from circulation by the liver |
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aggregation of cell components in defective lysosomes due to a faulty marking system for glycoproteins to be distributed to lysosomes |
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oligosaccharide transferase |
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adds the "high mannose core" of glycoproteins to the growing polypeptide in the ER |
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the acceptor upon which the common core for glycoproteins is originally formed |
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a chaperone that prevents improperly folded glycoproteins from leaving the cell; recognized the three terminal glucoses on a improper folded molecule |
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type of coenzyme that binds to and release from the enzyme, needs a separate enzyme mechanism to recycle it |
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prosthetic group (coenzyme) |
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type of coenzyme that binds tightly to the enzyme and does not leave it; needs a secondary reaction at that enzyme to recycle, usually involves a second substrate |
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noncompetitive inhibitor
(define, effects on Km and Vmax) |
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binds to a site remote from the substrate-binding site
Km = same Vmax = decreased |
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inhibitor and substrate compete for the same binding site
Km = appears higher Vmax = same |
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influence the way multi-subunit enzymes function and cause their active sites to behave in a cooperative manner |
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enzymes that work on the same substrate but are coded for in different genes, usually work in different tissues or work with different affinities for the substrate |
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Serine Protease inhibitors form irreversible compounds with proteases, shuts down the activity |
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charged transition state is stabilized by interacting with side charges of amino acids within an enzyme |
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enzyme forms covalent enzyme-substrate complex, more efficient than acid-base catalysis |
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partial or total proton transfers with the amino acid side chains can stabilize the transition state, returning proton to or from the enzyme releases product(s) |
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enzymes has higher affintiy for transition state than for product or substrate; help to drive reaction to the transition state |
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