Chapter 4 lecture 2/23

If two enzymes that are in different ____________ compete for the same __________, the enzyme with the _________ affinity will get the substrate.

If two enzymes that are in different ____________ compete for the same __________, the enzyme with the _________ affinity will get the substrate.

pathways, substrate, higher

an enzyme with ____ affinity won’t become ________.

less, active

glucose enters cells and becomes _______________ to form glucose-_-_______________.

phosphorylated, 6-phosphate

______________ can function in preventing ___________ from leaving the cell, and ____________ glucose to help further ______________.

phosphorylation, glucose, destabilizing, metabolism

Glucose has no ________, G-6-P is ___________ charged.

charge, negatively

Two enzymes (isozymes) that can _____________ glucose are _____knase and _____kinase

phosphorylate, hexo, gluco

Glucose always moves ____ to ____.

high, low

_____kinase is found in all ________, and _____ ___ require insulin, and is __________ by its product G-6-p

hexo, tissues, does not, inhibited

_____kinase has a _____ affinity for glucose (low Km) and opperates efficiently at normal _______ glucose levels.

hexo, high, blood

______kniase has adapted for utillizing _________ as an _________ source, example: cellular respiration for ATP production.

hexo, glucose, energy

_______kinase is found in the ______, pancrease, (gut and brain), and is activated by ________ and _________.

gluco, liver, insulin, glucose

Insulin ____________ transcription of GK gene in the _____ for glucoknase, and is ___ inhibited by G-6_P

increases, liver, not

_____kinase has a ____ affinity for glucose, and acts as a glucose ________.

gluco, low, sensor

________kinase regulates _____________ metabolism, and has a ____ response when _______ glucose levels are high. glucose stored as glycogen or fat.

Gluco, carbohydrate, high, blood,

_______kinase has a high ________ where the liver removes __________ from _________ to prevent hyperglycemia

Gluco, Vmax, glucose, blood

_____ is the rate at which ____________ molecules are converted to __________ by a single statured enzyme at ___________ velocity, (moles of product/sec).

Kcat, substrate, product, maximum.

The ________ the kcat, the more ____________ produce/sec. turnover numbers vary greatly among __________.

larger, product, enzymes

___ Km does not necessarily mean _____ Kcat.

high affinity could _________ rate of reaction

catalysis might require other _________ that are present in limited amounts

________ might require many steps.

Low, high, reduce, molecules, catalysis

Enzyme efficiency is a measure of how __________ and enzyme converts __________ into __________. (also a measure of preference)

efficiently, substrates, products

enzyme ___________ - Kcat/Km

efficiency

Either a ______ value of Kcat (rapid turnover) or a ______ value of Km (high affinity for substrate) makes Kcat/Km _______.

large, small, large

within a ____ protein and enzyme _________ is tightly controlled. The ___________ of protein activity occurs at many _______.

cell, activity, regulations, levels

The ____________ of protein activities can consist of:

control of _____ ____________

________ degradation rates,

confining protein activity to particular _________ compartment/vesicle

adjusting protein activity by __________ with other molecules.

regulation, gene expression, protein, cellular, interacting

factors that can affect or conrol enzyme/protein function:

1. ___ and _______

2. __________ and coenzyme

3. __________ regulation

pH, temp, cofactors, allosteric

proteins and enzymes have two different binding sites, _______ and ______________.

active, allosteric

____________ sites are have one or more ______ at a different location that recognize regulatory ___________.

allosteric, sites, molecules

the __________ of regulatory molecule/s affect _________ site and ___________.

binding, active, catalysis

____________ and ______________ can regulate other ____________ by either increasing or reducing their activity.

activators, inhibitors, molecules

enzyme ____________ decrease activity. They have two major types, _________ and ___________

inhibitors, reversible, irreversible

_________________ inhibitors bind enzyme __________ by modifying amino acid residues, can cause permanent loss of __________ activity, and are generally ______ to cells, Examples heavy metal ions, nerve gas, poisons, some insecticided.

irreversible, covalently, catalytic, toxic.

__________ inhibitors bind enzymes non-covalently and can __________ from the enzyme. There are two types, ____________ and _______________.

reversible, dissociate, competitive, noncompetitive

______________ inhibitor binds to an _______ site, which stops the activeness of an enzyme until it falls off.

competive, active,

______________ inhibitor bonds to ___________ site, where it inhibits ___________ binding or reduced _________ activity at the active

noncompetitive, allosteric, substrate, catalytic

factors that can affect or control enzyme/protein function:

4. __________ regulation

5. ____________ activation/cleavage

6. __________ modification

7. ATP ____________

feedback, proteolytic, covalent, hydrolysis