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o'=rnx is INDEPENDENT of (sub)

1'=rnx rate depends on the (sub)

speudo 1'=2 subs, only one of them is limiting

2'=2 subs, rnx rate depends on the (2 subs)

G<0

rnx is spontaneous

G>0

rxn is NOT spontaneous

Flavins: FMN>FMNH2

FAD>FADH2

involved in redox of C=C

NIcotinamides: NAD+>NADH

NADP+>NADPH

involved in redox of C=O

All types of protein are extremly sensitive to Temp. at a certain point, the enzymes or proteins are denatured and so the rate drops drastically. it is the same with pH

Vmax= max processing rate of the enzyme ( when all the active site are filled)

Km= concentration  of sub at which 1/2 of the active sites are filled

  than dissociation reaction

what could we do to increase the rate of a rnx

(besides adding a catalyst)

add more enzyme

engineer a bettere active site

add an activator

same shape as sub

compete for the Active site

 if you increase the sub, you decrease the I

Vmax does not change

Km decreases (so that binding affinitiy decreases b/t S and E)

I and sub have different shapes

don't bind to the active site

Vmax decrases and Km does not change

mimis the natural sub

bonds to active site IRREVERSIBLY so it deactivates it

both Vmax and Km decrease

whats the mechanism of action of lysosyme)

Lysozyme digests bacterial cell walls by breaking b(1- 4) glycosidic bonds between (N- acetylmuramic acid (NAM) and N-acetylglucosamine (NAG)

Exemples of  comp inhibitors

serine protease family

chymotrypin

carbonate anhydrase

H2C03<CA>H20+Co2

HMG-CoA Reductase

cholesterol biosynthesis

stimulate gluconeogenesis by allosteric activation of pyruvate carboxylase

inhibits pyruvate dehydrogenage complex

G>G6P (hexokinase)

F6P>F1,6-BP (PFK-1)

PEPyruvate>pyruvate (pyruvate kinase)

glucokinase is found in the liver. 

It has much higher Km for glucose

 not inhibited by glucose 6-phosphate

**    is absent in muscle and is deficient in patients

    with diabetes

also, at normal blood glucose, hexo is saturated completely whereas gluco is not

PFK-1 is an important allosteric enzyme regulating the rate of glucose catabolism and plays a role in integrating metabolism.

 its the 1st unite irreversible step of glycolysis

 1,3BPG >>> 3-P-GI

(PGK)

How is NAD+ supplied under anaerobic conditions in glycolysis

from pyruvate to lactate

(lactate dehydrogenase rxn)

the liver furnishes glucose to contracting skeletal muscle,

which derives ATP from the glycolytic conversion of glucose into lactate.

Contracting skeletal muscle supplies lactate to the liver, which use it

to synthesize glucose.

GI-3-P>>> 1,3BPG

(GI-3P dehydrogenase)

**so The NADH that is produced in the glyceraldehyde 3-phosphate reaction is consumed in the lactate DH reaction.  Thus, redox balance is maintained

Overconsumption of alcolhol> high level of NADH>> inhibits gluconeogenesis>> lactate increase

ATP

* remember : hexokinase, PFK1, pyruvate kinase

During exercise, what is needed to activate PFK1

in the liver. 

Insulin.

it is synthesized  from F6P by PFK2

the level of F2,6-BP is regulated by the phosphorylation of PFK2

PFK2 kinase and phosphatase regulate PFK2

when the body is fasting (hungry), insulin is low so PFK2 kinase will target PFK2 to make more f2,6-BF>> stimulate PFK1>>stimulate glycolysis

when the body is full (fed), insulin is high so PFK2 phosphate will target PFK2 to make less f2,6-BF>> to stop PFK1>>to slow down glycolysis

Abnormal RBC shape a result of inadequate ion pumping

•Excessive RBC destruction in spleen