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MindMap Gallery Protein digestion and absorption and amino acid metabolism mind map

Protein digestion and absorption and amino acid metabolism mind map

This is a mind map about protein digestion and absorption and amino acid metabolism, the nutritional value of protein and digestion, absorption, ammonia metabolism, etc.

Edited at 2023-11-16 17:39:12

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Protein digestion and absorption and amino acid metabolism mind map

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Outline

Protein digestion and absorption and amino acid metabolism

Ammonia metabolism

There are three important sources of blood ammonia

Ammonia can be produced by both amino acid deamination and amine decomposition

Intestinal bacteria produce ammonia

Ammonia secreted by renal tubular epithelial cells mainly comes from glutamine

Ammonia is transported in the blood as alanine and glutamine

Ammonia is transported from skeletal muscle to the liver via the alanine-glucose cycle

Ammonia is transported from tissues such as the brain and skeletal muscles to the liver or kidneys via glutamine

effect

Glutamine is both the detoxification product of ammonia and the storage and transportation form of ammonia.

Glutamine provides the amino group to convert aspartic acid into asparagine

The main metabolic route of ammonia is the synthesis of urea in the liver

Urea is synthesized via the ornithine cycle (urea cycle)

Reaction steps in the ornithine cycle in the liver

NH3, CO2, ATP condense to form carbamoyl phosphate

Carbamoyl phosphate reacts with ornithine to form citrulline

Citrulline reacts with aspartic acid to form argininosuccinic acid

Argininosuccinic acid is cleaved to produce arginine and fumaric acid

Arginine is hydrolyzed to release urea and regenerated into ornithine

overall response

Urea synthesis is regulated by dietary protein and two key enzymes

High-protein meals increase urea production

AGA activates CPS-I to initiate urea synthesis

Argininosuccinic acid synthesis

Impairment of urea production can cause hyperammonemia or ammonia poisoning

Metabolism of individual amino acids

Decarboxylation of amino acids requires decarboxylase catalysis

Glutamic acid decarboxylates to gamma-aminobutyric acid

Decarboxylation of histidine to produce histamine

Tryptophan is hydroxylated and decarboxylated to form 5-hydroxytryptamine

Decarboxylation of certain amino acids can produce polyamines

key enzyme

ornithine decarboxylase

Certain amino acids produce one-carbon units during catabolism

Tetrahydrofolate participates in one-carbon unit metabolism as a carrier of one-carbon units

one carbon unit

An organic group containing one carbon atom produced during the catabolism of certain amino acids

One-carbon units produced from amino acids can be converted into each other

Nutritional Value of Protein and Digestion and Absorption

The metabolic status of proteins in the body can be described by nitrogen balance

nitrogen balance

The relationship between daily nitrogen intake and excretion

The average nitrogen content of protein is 16%

way

ingest

food

discharge

urine and feces

balance

Total nitrogen balance (nitrogen intake = nitrogen output)

normal person

Positive balance of nitrogen (nitrogen intake > nitrogen output)

Children, pregnant women, convalescent patients

Negative nitrogen balance (nitrogen intake < nitrogen output)

Starvation, severe burns, bleeding

Physiological requirements for protein

Nutritional essential amino acids determine the nutritional value of protein

"Bring one or two light-colored books to the group"

Niacin deficiency

nutritional value of protein

Utilization of food protein in the body

Metrics

Types and proportions of essential amino acids in food

Animal protein has relatively high nutritional value

Complementary effects of food proteins

When a variety of proteins with low nutritional value are mixed and eaten, the essential amino acids can complement each other, thereby improving the nutritional value of the protein.

Cereal proteins contain more tryptophan and less lysine

Bean protein contains more lysine and less tryptophan

Exogenous proteins are digested into oligopeptides and amino acids and then absorbed

Proteins are digested into oligopeptides and amino acids in the stomach and small intestine

Physiological significance of protein digestion

Large molecules are converted into small molecules for easy absorption

Eliminate species specificity and antigenicity to prevent allergic and toxic reactions

Proteins are hydrolyzed into peptides and amino acids in the stomach

Proteins are hydrolyzed into oligopeptides and amino acids in the small intestine (the main site of protein digestion)

Digestive effect of pancreatic juice on protease

Protease

Endopeptidase

effect

Specifically hydrolyzes some peptide bonds within proteins

include

Trypsin

chymotrypsin

elastase

exopeptidase

effect

Specific hydrolysis of peptide bonds at the ends of proteins or polypeptides

include

Carboxypeptidase (main)

carboxypeptidase A

carboxypeptidase B

Aminopeptidase

Activation of zymogens in intestinal fluid

Protein digestion by intestinal mucosal cells

Oligopeptidase

Aminopeptidase

dipeptidase

Amino acids and oligopeptides are absorbed through active transport mechanisms

amino acid absorption carrier

Peptide absorption mechanism and significance

Undigested and absorbed proteins become putrid in the lower colon

protein putrefaction

Undigested proteins and unabsorbed digestive products are broken down by intestinal bacteria in the lower colon

product

Mostly harmful

Amine, ammonia, phenol, indole

few useful

fatty acids, vitamins

Gut bacteria produce amines through decarboxylation

pseudoneurotransmitter

Gut bacteria produce ammonia through deamination

Corruption produces other harmful substances

Tyrosine→phenol

Cysteine → hydrogen sulfide

Tryptophan→indole

General metabolism of amino acids

Protein breaks down into amino acids in the body

Proteins degrade at different rates

Half-life (t1/2)

The time required to reduce its concentration to 50% of the starting value

There are two important pathways for protein degradation in eukaryotic cells

Proteins are degraded in lysosomes through an ATP-independent pathway

Features

cathepsin

Degrade exogenous proteins, membrane proteins and intracellular long-lived proteins

Proteins are degraded in the proteasome through the ATP-dependent ubiquitin pathway

Features

Proteasome is responsible for degradation

Dependent on ubiquitin

Ubiquitin

A small molecule protein composed of 76 amino acids, widely present in eukaryotic cells

Primary structure is highly conserved

Degrade abnormal proteins and short-lived proteins

process

ubiquitination

Ubiquitin forms a covalent linkage to proteins selected for degradation, allowing them to be labeled and then degraded by the proteasome

Three enzymes involved in consuming ATP

proteasomal degradation

structure

26S protein complex

20S core particles (CP)

19S Regulating Particles (RP)

Exogenous amino acids and endogenous amino acids constitute the amino acid metabolic pool

Amino acid catabolism begins with deamination

Way

transaminase

transamination

Under the catalysis of aminotransferase, the amino group of an a-amino acid is reversibly transferred to an a-keto acid. The result is that the amino acid is deaminated to form the corresponding a-keto acid, and the original a-keto acid is converted into another amino acid.

type

Aspartate aminotransferase (GOT)/aspartate aminotransferase (AST)

More myocardium

Glutamate aminotransferase (GPT)/alanine aminotransferase (ALT)

Excess liver

Transaminase has the same coenzyme and mechanism of action

coenzyme

Pyridoxal Phosphate

effect

transfer amino

L-glutamate dehydrogenase

allosteric enzyme

allosteric inhibitor

ATP,GTP

allosteric activator

ADP, GDP

transamination/deamination/combined deamination

amino acid oxidase

prosthetic base

FMN,FAD

The amino acid carbon chain skeleton can be converted or decomposed

a-keto acid can completely oxidize and decompose and provide energy

way

Tricarboxylic acid cycle and biological oxidation system→CO2 H2O energy

a-Keto acids undergo amination to form nutritionally non-essential amino acids

Pyruvate → alanine

Oxaloacetate → Aspartic acid

a-ketoglutarate→glutamic acid

a-Keto acids can be converted into sugars and lipids