Bmb 401 Exam 2

Front 1

define amphipathic

Back 1

part polar, part non polar. Used to refer to the hydrophobicity of lipids

Front 2

Omega N fatty acids

Back 2

A way to count double bonds from the end of the tail. The location of that bond is denoted by omega

Front 3

Define acylglycerol

Back 3

fatty acids esterified with glycerol are better for storage because they are almost entirely non polar. Therefore, you can fit them close tog

Front 4

phospholipids

Back 4

Main material of membranes. Often saturated at position 1 and unsaturated at position 2. Could be 2 saturated but RARELY two unsaturated. Nature doesn't work that way

Front 5

define genomics

Back 5

study of whole genome of organism

Front 6

transciprtomics

Back 6

study of transcribed genome

Front 7

proteomics

Back 7

study of protein expression and their modifications

Front 8

metabolomics

Back 8

study of all metabolites (no estimate of possible number)

Front 9

systems biology

Back 9

integration of data to develop predictive models

Front 10

synthetis biology/biochemical engineering

Back 10

it is: the design and construction of new biological parts, devices and systems, and the re-design of existing, natural biological systems for useful purposes. (e.g. bacteria used to produce biofuel from glucose

Front 11

autotrophs

Back 11

just use CO2 as carbon source

Front 12

heterotrophs

Back 12

use organic forms of carbon

Front 13

phototrophs

Back 13

use light as energy source

Front 14

chemotrophs

Back 14

use organic chemicals as energy and in some case oxidisable inorganics

Front 15

metabolons

Back 15

multienzyme complexes (common). metabolites are passed from one active site to another without complete equilibration with the bulk cellular fluids. this decreases intermediate transit time and prevents intermediate loss (diffusion, competing pathways)

Front 16

catabolic pathways converge to a few products. this differs from anabolic pathways because

Back 16

anabolic pathways diverge to synthesize many biomolecules. amphobolic intermediates have roles in catabolism and anabolism

Front 17

independent catabolism and anabolic pathways

Back 17

activation of one mode is accompanied by reciprocal inhibition of the other mode. For example, if enzyme 1 is turned on in the catabolic pathway (taking substrate A to create product P), enzyme 6 - which begins the anabolic pathway from P to A - gets turned off. Cell decides which to activate based on energy levels available to the cell

Front 18

micronutrients

Back 18

are required in diet, not synthesized by the organism. Are components or precursors of coenzymes (except vitamin c). they may be carriers of specific functional groups

Front 19

coenzyme

Back 19

required for certain enzymes to function. they are typically modified and then converted back by other enzymes.

Front 20

NAD+ and NADP+

Back 20

two-electron carrier coenzymes. transfer hydride anion (H- - 2 electrons) to and from substrates in redox reactions (usually dehydrogenase)

Front 21

riboflavin and the flavins (vitamin B12)

Back 21

micronutrient. helps convert carbohydrates (glucose) into energy. The active forms are flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD). Can carry 0 1 or 2 electrons.

Front 22

thiamine (vitamin B1)

Back 22

thiamine pyrophosphate (TPP) is the active form. it is involved in carbohydrate metabolism

Front 23

vitamin B6: pyridoxine and pyridoxal phosphate

Back 23

catalyzes rxns involving amino acids. Can form stable Schiff base adducts with alpha-amino acid groups - this allows the electron to move in a conjugated electron sink system & this is stabilizing for the intermediate of the rxn

Front 24

how does a schiff base work?

Back 24

Front 25

coenzyme A (vitamin b5 - panthothenic acid is a component of this)

Back 25

Serves two main functions: 1. activates acyl groups (Acyl refers to any group with thestructure R-(C=O) for transfer by nucleophilic attack, and 2. activation of the alpha-hydrogen of the acyl group to be abstracted as a proton. The reactive -SH group on CoA helps the reaction proceed (thioester bond) - makes it easier to grab something and release - does so with less energy

Front 26

What does the panthothenic acid help with? Adenine nucleotide?

Back 26

This acts as an arm to grab the substrate and move it to a different activation site on the enzyme.

Front 27

biotin

Back 27

a micronutrient. functions as a mobile carboxyl group (-COOH) carrier. Binds to lysine - when this occurs its called biocytin. The "tether" allows biotin to acquire a carboxyl group at one subsite of enzyme then deliver it to a substrate acceptor at another enzyme subsite

Front 28

lipoic acid (info)

Back 28

also a ring on a chain and gets linked to protein. This is an acyl group carrier, couples that transfer with an electron transfer during oxidation and decarboxylation of alpha-keto acids. This cofactor is used by pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase

Front 29

lipoic acid (picture)

Back 29

Front 30

vitamin B12: cyanocobalam

Back 30

Catalyzes: 1. intramolecular rearrangements. 2. reductions of ribonucleotides to deoxyribonucleotides 3. methyl group transfers (using tetrahydrofolate - see folic acid)

Front 31

folate

Back 31

Acceptors/donars of 1-C units for all oxidation levels of carbon except for CO2. Active form is THF (formed by 2 reductions of folate by duhydrofolate reductase)

Front 32

vitamin c

Back 32

reducing agent, electron scavenger. It helps to hydroxylate proline and lysine, metabolizes Tyr and Fe in the spleen. Prevents toxicity of metals, reduces allergic responses, and stimulates the immune system

Front 33

vitamin A

Back 33

important in development, cell differentiation. This is a prohormone, retinol from retinoic acid.

Front 34

vitamin D

Back 34

prohormone. produced in skin in response to sunlight. is a ligand for vitamin D receptor. this is important in bone maintenance and calciummetabolism

Front 35

which coenzymes are electron carriers?

Back 35

NADH, NADPH, FADH, FADH2 (vitamin C)

Front 36

which coenzymes are involved in (de)carboxylation reactions?

Back 36

thiamine, vitamin B6, biotin

Front 37

which coenzymes are involved in acyl group transfers?

Back 37

coA,lipoic acid (folic acid,vitamin B12)

Front 38

which coenzymes use a tethering mechanism?

Back 38

coA, biotin, lipoic acid