biochem cool 2

oxidative deam of glutamate - localisation, main function,

regulation (main one and then allosteric activators/inhibitors)

OX DEAM

• mitochondria

• main function = only deg of AA where energy is obtained

• glutamate dehydrogenase

• allosteric act = ADP,

• allosteric inhibitors = ATP and GTP

oxidative deam of remaining AAs

enzymes, what do these enzymes act together with

what is the released H2 transferred to

REMAINING = GIMME NOW = IMINO

transamination

what interacts with what?

the start - is converted into a new what? (two things)

cofactor of transaminase?

role ?

AA (donor of amino group) interacts with acceptor of amino group (keto acid)

keto into new l amino acid and vice cersa

cofactor = PLP (pyrodixal phosphate - derivative of b6)

role = to make NON ESSENTIAL amino acids

AST GOT and ALT GPT

what are they?

used for what disease? how do they work?

what other disease?

draw aspartate

aspartate = COO- at the end

ast/alt = TRANSAMINASES WITH BIO IMPORTANCE

DIAGNOSTIC MARKER FOR LIVER DISEASE (inc proportionately depending on disorfer)

myocardial infarction = increase in AST serum.

transdeamination:

what two things is it a combination of - what enzyme does it use?

what is it the main route of?

what does it allow AA’s to have done to them?

which direction is it in? leading to the synthesis of?

cmobo of transamintion of AA with a aloha ketoglutarate and subsequent oxidative deamination of the resulting glutamate

under glyutamate dehydrogenase

main route for nitrogen release from AA’s

a way to degrade the other AA’s with energy gain

in the refuction direction = synthesis of non essential AAs

decarboxylation

WHAT ARE BIOGENIC AMINES NEUTRALISED BY

what are biogenic amines

what are they neutralised by

mono amine oxidases, di amine oxidases

reductive animation of ketoglut

WHICH ENZYME IS INVOLVED

what is it and what does it cause?

reduces the level of what required for what?

reverse ox deam of glut -

high level of glutam dehydrogenase in the brain

reduces amount of aKG REQUIRED!!!!! FOR CITRATE and glutamate synthesis

glutamine synthesis

requires ATP

causes high levels of glutamine synthetase in the brain

reduces level of glutamate which is a neurotransmitter required for synthesis of FABA

glutamine is used for ammonia depot = degraded by glutaminase

ammoneogenesis 9METABOLISM OF GLUTAMINE)

location, main function (3 points)

what is obtained and what is it used for?

KIDNEYS

neutralisaiton of ammonia

-obtained from degredation of glutamine

• by its conversion into ammonium ion and excretion through urine

glutamate obtained from deg of glutamine is used as a substrate for GNG

urea cycle

localisation

main function

regulation - main regulatory enzyme, the two allosteric activators

energy balance?

enzyme defects

4 macroergic bonds for 2 AA groups - ammonia and aspartate and bicarbonate ion to urea

enzyme defects = ammonia posion = vomiting, mental retard

synthesis of SAM

main function? what is SAM a cofactor in

SAM is active form of?

what happens in methionine deficiency?

what is needed as a cofactor?

what parts do you forget of the scheme

atp and pPP on meth ad. transf. serine, glycine, hsitide, tryptophan goes to c1 group

degradation of phenylalanine and tyrosine

products:

enzyme defects: 4

parts of scheme you forget

phenylketonuria

tyrosinemia

alkaptonuria

albinism

phenylalanine hydroxylase (o2 to H20) (BH4 to BH2)

tyrosine transaminase = akg and glutamate

pOH phenylpyruvate hydroxylase again = O2 to CO2 (Cu2+)

dihydroprotein reductase - draw it

what does it do?

requires what?

defect in this enzyme leads to what?

synthesis by transamination OF A KETO ACIDS- what is obtained?

hint - its the stuff from ast and alt action

synthesis by reductive amination - what is obtained under action of what

synthesis by amidation (making it an AMINE)

what is obtained from twhat (2 things)

under action of what?

synthesis by hydroxylation

hydroxylation of what obtains what

by hydroxylation of phenyl alanine, tyrosine is obtained

ESSENTIAL AA

synthesis by cyclation (of what?) produces what

what does it require

CYCLATION of glutamate gives proline = a cycler is a proathelete

requires nadph for lots of energy

synthesis by exchange of c1 fragments

ontained from what through what ?

c1 fragment = C AND C (from methionine) through methyl transferases

creatine phosphate  - forgot

loc !!!!!!!!!!!!!!!!!!!!

main function?

main tip?

aas involved?

things i forget in the scheme:

arginine to guanoacetate - amidino transferase GLYCINE _ ORTHININE

creatine phosphokinase - atp to adp

h20+P

THE LOCATIONS KIDNEY, LIVER, MUSCLE + BRAIN

cituline formation?

what is under the enxyme

structure of citruine

what is not involved therefore what cant happen?

what is it obtained from by what?

what do you froget?

NO also produced = 2nd mediator for vasodilation

NADPH to NADP

citruline = CO=O and NH2

synthesis of acetylcholine

localisation 

main function?

AA substrate for synthesis?

cytosol of neruons

formatiion of acetyle choline, a neurotransmitter,

serine

synthesis of serotonin and melatonin? forgot what

TRIP

AA substrate for synthesis of it?

serotonin localisation?

what does it participate in?

what does it activate?

melatonin?

localisation?

obtained from what?

synthesis and what else increases at night? what does it affect?

what does it inhibit?

melatonin/seratonin = hormones that make u trip out

therefore tryptophan

CLEAN THEN DIRTY AT THE TOP

plain 6 pyramid then pentagon with n at the top

catecholamines = tyrone the cat

acetylcholine

sam S A)AETYL) - hes neuro divergent therefore neurons

melatonin = secrete at night - affects circadian rhythm = inhibits other neurotransmitters

(where n acetyltransferase is in pineal gland)

synthesis of catecholamines - what to remember

name the catecholamines:

substrate:

location:

regulation: main regulatory enzyme?

disease?

WHAT DO YOU FORGET?

NEED TO FEED THE CAT WATER

dopamine, adrenaline, noradrenaline

tyrosine

location:

noradrenaline/dopamine = neurotransmitt. in NS

adren/noradren = made in medulla of adrenal gland = for stress

main reg enzyme = tyrosine hydroxylase

parkinsons

DOPAMINE B HYDROXYLAASE

degradation of pruine nucleotides - starts with what preoduct?

location

final profuct?

regulation?

what is a suicide subtrate for the regulatory enzyme? and what is it used for?

eynzme defects?

parts you forget

IF YOURE PURE YOU WANT PROTEIN AND GOUT

adenosine deaminase = h20 to nh4+

guanase = h20 to nh3+

origin of the constituent atoms of the purine ring

synthesis of pruine nucleotides do the CORRECT SCHEME PLEASE

subtrate?

final product?

how many reactions form IMP?

why does it not accumulate?

REGULATION!!! ?

enzyme defects

5

what syndrome is caused and how?

enzymes on the diagram you forget = ?

enzyme defects:

PRPP synthase or PRPP glutamyl amidotransferase increase = gout

hypoxanthine phopsphoribosoyl transferase deficiency = gout

defeciency in this = lesch nyhan syndrome

glutamate to glutamine in glutamyl thingy

and again in transamidinase

and atp to p + pp in prpp synthesis

regulation of purine nycelotide synthesis

part i forget =

what provides energy for synth of AMP and GMP

ADP / GDP = INHIBITORS

main regulatory enzyme?

allosteric activator?

allosteric inhibiotrs?

final products?

name the competitive inhibitors and how they work here

main reg enzyme = glutamyl PRPP amidotransferase

allosteric activator - PRPP

alloesteric inhibitors: - ADP AND GDP

allosteric inhibitors - final products: ATP<AMP>ADP< GDP< GTP< GMP

PRPP SYNTHETASE

AMP AND GMP = competitive inhibitors of iIMP AND EACH INHIBITS THEIR OWN SYNTHESIS

ATP provides energy synth for GMP and GTP for AMP

synthesis of pyrimidine nucleotides - miastkaes

what is built first before the next part is added?

substrates?

final product?

how many reactions is UMP synth in? what is obtained from it?

regulation - main reg enzyme?

enzyme defects?

2

aspartate = c-O- and COO,

no nh for ctp

the base is first built then the ribose phosphate residue is added

substrates: glutamine + bicarbonate

final product: tmp, ctp, ump

6, other pyrmaidines

regulation: aspartate transcarbamoulase

enzyme defects =

orotidine monophosphate decarboxylase and orotate phosphoribosyl transferase = orotaturia = type 1

orotidinedecarboxylisasae = type 2

regulation of pyrimidine nucleotide synthesis

main reg enzyme

alloesteric activator

allosteric inhibitor

which enzyme regulaties it in the cytosol? (at the start)

alloesteric activtor and inhibitor?

what does TDP do here?

free iron (non heme) - intake of iron by enterocytes

what do you forget

removal of iron from enterocyte

deposition of iron in liver and release into circulation again

on luminal surface of cells it is reduced from fe3 to fe2 by ferrireductase (duodenal cyt b), transported into enterocyte by divalent metal transporter

iron crosses membrane through ferroportin (crosses basolateral membrane) and hephaestin oxidses it from fe2 to fe3 again

and then fe3+ binds to transferrin and passes into liver + released into circulation again

• hepatocytes absorb fe3+ + transferrin after it binds to tfr (transferrin receptor)

• fe2 is released into blood and oxidised to fe3+ by ceruloplasmin and binds to transferring again

heme iron - intake of iron by enterocytes

transported by HCP 1 (hemetransporting protein)

iron is released by heme oxygenase and fe2+ binds to ferretin again

porphoryn synthesis

location

main function

substrates

regulation: main reg enzyme

allosteric inhibitor (what else is this substance)?

inductors:

repressors?

enyzyme defects

mainly liver and bone marrow

main fynction: fomation of porphoryns, pros groups, hemeoglbin myoglonin etc

succinyl coA and glycine

main reg enzyme = ALA synthase

allosteric inhib = heme (is also a repressor)

inductorsL anaesthetics, xenobiotics, steroids

repressors: glucose, hemin, hematin

enzyme defectsL

decreased ALA dehydratase activity

porphoryn - mutation in gene 3 and 8

intermittent acute porphyn - iroporphyrinogen 1 synthase

degradation of hemoglobin

localisaiton

main function

macrophages: how is hemohlobim degraded here, what is obtained

in liver?

describe the indirect/direct bilirubin again

macrophages and hepatocytes in the liver

main funct: erythrocutes live for 120 days - after this they degrade

• globin = into AA (reused)

• heme = bilirubin )and iron is released which is recycled)

MACROPHAFES:

• under heme oxygenase, green biliverdin is produced

• indirect bilirubin is produced (conjugated, blood, hydrophobic)

in liver, it is converted to bilirubin diglucoronide after it is conjugated with udp glucoronic acid to form bilirubin diglucoronide (bile, hydrophilic, direct)

metabolism of bilirubin

• in macrophage, heme is converted to indirect bilirubin

• is bound to albumin, transported to liver by blood

• indirect bilirubin = taken up by parenchymal cells, conjugated to direct bilirubin and secreted into bile

• in intestines, bilirubin is reduced to urobillonogen

• in colon, it is oxidised to urobilins (gives poo normal colour)

• some of urobilinogen enter kidneys and exit via blood stream, while some are reabsorbed by intestines, enter liver and re exreted (enterohepatic circulation)

haemolytic jaundice

reason?

degradation of large amounts of erythrocytes exceeding the capacity of a healthy liver

• bilirubin in the blood increased (indirect)

• no bilirubin in urine

• urobillnogen IS, as dark as beer urine, DARK feces

hepatic jaundice

hepatocytes = destroyed due to liver damage (cirrohosis/hepatitis)

bilirubin in the bloos - yes (increased indirect and direct)

bilirubin in urine = yes

urobillinogen = not increased

feces colour = normal

obstructive (post hepatic jaundice)

disorder name?

reason - due to complete obstruction of bile duct due to tumour / gall stones

bilirubin in the blood = increased direct bilirubun

bilirubin in urine = yes, dark urine

urobilinogen in urine, no

feces color = acholic (pale)

cysteine synthesis