cooked biochem

what is the common oxidized product in citric acid cycle

acetyl coa

product of glycolysis

pyruvate

which molecule provides a C skeleton for nonessential amino acids

pyruvate

what happens in anaerobic respiration

pyruvate to lactate

triose phosphate

an intermediate in the Calvin cycle, also known as glyceraldehyde-3-phosphate.

precursor for fatty acids and cholesterol

acetyl coa

how many AAs must be in diet

8 (arg semi essential)

main product of catabolism

acetyl coa

transamination

The process by which an amino group from one amino acid is transferred to a carbon compound to form a new amino acid.

what does pyruvate transamination give

alanine

Oxaloacetate

molecule the combines with alanine to deaminate it to form aspartate

Alanine aminotransferase (ALT) aspartate aminotransferase (AST)

(if spiked) indicates that liver cells or cells in other organs are damaged, and the enzymes have leaked into the bloodstream

what is formed by the reductive amination of ketoglutarate

glutamate

what enzyme catalyzes reductive amination of ketoglutarate

glutamate dehydrogenase (favors glutamate synthesis)

what enzymes involved in glutamate to glutamine

glutamine synthetase and lambda glutamyl phosphate

what provides N for aspartate --> arginine

glutamine

serine oxidation (what is oxidizing agent), what does it do

NAD+, changes OH to ketone

glycine formation (why special)

STRONGLY FAVORED

what reduces proline, what molecule cyclizes

NADPH, glutamyl phosphate

cysteine comes from what AA

methionine

what process is a disulfide bridge formed by

oxidation

phenylalanine hydroxylation

irriversible (done by phenylalanine hydroxylase and NADPH)

if diet has enough phenylalanine...

tyrosine nonessential, BUT tyrosine cant replace phenylalanine

Tetrahydrobiopterin

a cofactor needed to stabilize the enzyme phenylalanine hydroxylase (phenylalnine to tyrosine by NADPH)

mixed function oxidases

(AKA monooxygenase or hydroxylase) oxidize two different substrates simultaneously (REDOX) O2 to substrate and water

where does hydroxylation of proline and lysine occur

ONLY ON ACTAUAL COLLAGEN NOT SPEARATELY

oxidase

adds electrons to oxygen

p450s

ENZymes capable of bio transforming drugs in the liver mostly

Lock- Key Model

Complementarity in size, shape, charge, lipophilicity

Induced Fit

Conformational change upon binding that allows for higher affinity and tighter binding

Transfer amino group of one molecule to another (often AA to keto group)

Transaminases

Which of the following enzymes is a mix-function oxidase?

Phenylalanine hydroxylase

Which amino acid will form disulfide bridges?

Cysteine

What type of enzyme are P450s?

Oxidases

Which statement is true about essential Amino acids?

They cannot be synthesized

Glutamate dehydrogenase catalyzes the reaction

Reductive amidation of ᵳ-ketoglutarate

Which transamination reaction is strongly energetically favored?

Glycine synthesis

Why can’t essential AA undergo transamination?

transamination only occurs with AA that can be synthesized

what cuts protein into peptides in stomach

pepsin

trypsin

an enzyme from the pancreas that digests proteins (SMALL TO SMALLER) in the small intestine

Chymotrypsin

One of the main pancreatic proteases; it is activated (from chymotrypsinogen) by trypsin. (cut up proteins in small intestine

Aminopeptidase + carboxypeptidase

in small intestine - degrade peptides into amino acids; splits off one amino acid at a time

2 fates of amino acid

oxidized for energy (remove amino group - urea cycle) (entry into central metabolism - glycolysis citric acid cycle)

recycled into proteins

Why do we have to metabolize amino acids?

All of the above

some animals excrete nitrogen as

uric acid

trafficable amino acid

glutamate

alpha ketoglutaric acid

an intermediate product of the citric acid cycle (accepts amino group) N scavenger)

what happens when you add an amine to alpha ketoglutarate

glutamate

pyridoxal phosphate

The major coenzyme form of vitamin B6

Schiiffbase

imine

Transfer of one amine to alpha-ketoglutarate results in synthesis of _________________. Transfer of a second amine results in

synthesis of _________________.

glutamate (e.g., transamination).

glutamine (e.g., glutaminesynthetase).

AST (aspartate aminotransferase) in bloodstream

sign of liver damage

what is ammonia captured in

glutamate

excess ammonium stored where

glutamine

glutaminase

Enzyme converting glutamine to glutamate; catalyzes the release of ammonia from glutamine in the mitochondria?

ammonia in glutamate removed by what

glutamate dehydrogenase

transdeamination

the combined action of aminotransferase and glutamate dehydrogenase (transamination + oxidative deamination); pathway for ammonia excretion

Oxidative Deamination

removes an ammonia molecule directly from the amino acid

Transamination

The process by which an amino group from one amino acid is transferred to a carbon compound to form a new amino acid.

Acts as temporary storage of nitrogen

glutamine

glutamate dehydrogenase

catalyzes the reversible oxidative deamination (removes ammonia from glutamate) of glutamate and makes intermediate α-ketoglutarate

where does ammonia get removed from glutamate

mitochondria

Where do the two nitrogens in urea come from?

Carbamoyl phosphate and aspartate.

Carbamoyl phosphate synthetase I

1st step of nitrogen acquiring (needs ATP)

Rate Limiting Enzyme of Urea Cycle / initiates

Converts CO2 and NH3 to Carbamoyl Phosphate

where do most urea cycle reactions occur

cytosol followed by the mitochondrial matrix

Ornithine

Amino acid involved in urea cycle combines with carbamoyl phosphate (acts as a carrier molecule that accepts an ammonia group to become citrulline)

Citrulline

Intermediate formed from ornithine and carbamoyl phosphate.

when does citrulline go to the cytosol

when the phosphate of carbamoyl phosphate goes into mitochondrial matrix

citrulline

kidneys convert to L arginine

how does one amino group enter the urea cycle

as carbamoyl phosphate

how does the second amino group enter the urea cycle

in the form of aspartate

Oxaloacetate

A four-carbon molecule that binds with the two-carbon acetyl unit of acetyl-CoA to form citric acid in the first step of the Krebs cycle.

How does ammonia from glutamine enter the urea cycle?

after glutamine is broken down by the enzyme glutaminase inside liver cells, releasing both ammonia and glutamate

argininosuccinate

Intermediate formed from citrulline and aspartate.

citrullyl - AMP

Intermediate formed during argininosuccinate synthesis.

2 sources of N for urea

aspartate and carbamoyl phosphate

Ketogenic

Describes amino acids that can be converted into intermediates that then turn into acetyl coa (USED FOR ENERGY)

AAs to pyruvate

Trp, Ala, Ser, Gly, Thr, Cys

CAT GSS

another name for niacin

Vitamin B3

what can tryptophan be used to make

niacin (vitB3)

what do e coli produce in gut (good for gut)

indole derivatives

serotonin

feel good (made from TRYPTOPHAN) sleep, mood, pain, digestion

what is the first drug to combat serotonin deficiency

serotonin reuptake inhibitor (SSRI) prozac (block/ inhibit the reuptake of serotonin so it can stay around longer

enzyme for pyruvate to acetyl coa

pyruvate dehydrogenase

AAs metabolized to alpha ketoglutarate

Pro, His, Arg, Glu, Gln

PHAGG

alpha-ketoglutarate

a compound that participates in the formation of nonessential amino acids during transamination

what amino acid goes directly to aketoglutarate but others must be converted to it

glutamate

what is folate

Aka vit B9 -required for hemoglobin and amino acid synthesis (CRUCIAL DURING EARLY PREGNANCY) reduce birth defects in brain and spine

Succinyl-CoA (AA's)

Threonine

Isoleucine

Methionine

Valine

TIM V

succinyl coa

used for energy, made from alpha ketoglutarate

AAs metabolized to fumarate

tyrosine, phenylalanine

Phenylketonuria

phenylalanine hydroxylase is missing--> cant metabolize phenylalanine

is a disease leading to toxic accumulation of phenylalanine

AAs metabolized to oxaloacetate

aspartate,

asparagine

oxaloacetate function

acetyl group acceptor to carry intro citric acid cycle for oxidation

oxaloacetate pathway

asparagine-->aspartate-->oxaloacetate

asparaginase use

treatment of Acute Lymphoblastic Leukemia

Acute lymphoblastic leukemia

a type of blood cancer that affects the bone marrow, where blood cells are produced

citrate formed by

condensation of acetyl coa and oxaloacetate

citrate

A compound that is an intermediate in the citric acid cycle (krebs cycle)

Citrate chelates (binds) calcium ions, preventing blood clotting and thus is an effective anticoagulant

asparaginase

treatment for leukemia