MindMap Gallery Protein digestion and absorption and amino acid metabolism
Biochemistry and Molecular Biology 9th Edition Chapter 8 Protein digestion and absorption and amino acid metabolism, ammonia is transported to the liver or kidneys in the form of alanine and glutamine in the blood.
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This is a mind map about bacteria, and its main contents include: overview, morphology, types, structure, reproduction, distribution, application, and expansion. The summary is comprehensive and meticulous, suitable as review materials.
This is a mind map about plant asexual reproduction, and its main contents include: concept, spore reproduction, vegetative reproduction, tissue culture, and buds. The summary is comprehensive and meticulous, suitable as review materials.
This is a mind map about the reproductive development of animals, and its main contents include: insects, frogs, birds, sexual reproduction, and asexual reproduction. The summary is comprehensive and meticulous, suitable as review materials.
Protein digestion and absorption and amino acid metabolism
Nutritional value of protein and digestion and absorption
Ammonia balance: the relationship between ammonia intake and ammonia excretion
Total balance: intake = output
Positive balance: intake > excretion
Negative balance: intake<output
Significance: Reflects the overview of protein synthesis and catabolism in the body
Essential amino acids (9 types: a family wrote two books to rent)
The nutritional value of protein depends on the type and proportion of essential amino acids
Proteins are digested into oligopeptides and amino acids in the stomach and small intestine
In the stomach: pepsin
Activation: pepsinogen - (gastric acid, pepsin) → pepsin
Optimum pH of pepsin: 1.5~2.5
Pepsin milk coagulation
Small intestine:
Pancreatic juice: pancreatic enzymes
Endopeptidases: specifically hydrolyze peptide bonds within proteins, such as trypsin, chymotrypsin, and elastase
Exopeptidase: starting from the end of the peptide chain, hydrolyzing one amino acid at a time, such as carboxypeptidase A and B
significance:
1. Protect pancreatic tissue from the digestive action of proteases themselves
2. Ensure that the enzyme plays a catalytic role in its specific site and environment
3. Enzyme can also be regarded as the storage form of enzyme
Amino acids and oligopeptides are absorbed from the small intestine via active transport mechanisms
Corruption
Definition: Undigested proteins and unabsorbed digestive products are broken down by intestinal bacteria in the lower colon.
Deamination produces ammonia: lowers intestinal pH and reduces ammonia absorption (based on acid enema)
Most of the products are harmful, such as amines, ammonia, phenol, indole, etc.
Hepatic encephalopathy—pseudoneurotransmitter theory
General metabolism of amino acids
Protein breaks down into amino acids in the body
Two degradation pathways of proteins in eukaryotic cells
Lysosomes: ATP-independent pathway
Proteasome: ATP-dependent ubiquitin pathway
Exogenous amino acids and endogenous amino acids constitute the amino acid metabolic pool
The amino acids absorbed by digestion and absorption of food proteins (exogenous) are mixed with the amino acids produced by the degradation of tissue proteins in the body and the non-essential amino acids synthesized in the body (endogenous)
Amino acid catabolism begins with deamination
Deamination: refers to the process of removing the α-amino group from amino acids to generate the corresponding α-keto acid.
Way:
1. Transamination
2. L-glutamic acid dehydrogenase catalyzes the oxidative deamination of L-glutamic acid
combined deamination
3. Amino acid oxidase catalyzes deamination
Transamination: Under the action of transaminase (aminotransferase), a certain amino acid removes the α-amino group to form the corresponding α-keto acid, and another α-keto acid obtains this amino group to form the corresponding amino acid.
Transaminase: highly specific, with L-glutamic acid and α-keto acid transaminases being the most important
Alanine aminotransferase (ALT) is also known as glutamic alanine aminotransferase (GPT)
acute hepatitis
Aspartate aminotransferase (AST) is also known as aspartate aminotransferase (GOT)
myocardial infarction
Prosthetic group of transaminase: phosphate ester of vitamin B6, namely pyridoxal phosphate
L-glutamate dehydrogenase catalyzes the oxidative deamination of L-glutamate to generate α-ketoglutarate and ammonia
Combined deamination: transamination is coupled to oxidative deamination of L-glutamic acid
Amino acids are deaminated through the purine nucleotide cycle
The amino acid carbon chain skeleton can be converted or decomposed
Alpha-keto acids can be completely oxidized and decomposed to release energy
Amination of alpha-keto acids produces nutritionally non-essential amino acids
Alpha-keto acids can be converted into sugars and lipids
Glucogenic and ketogenic amino acids (a faded book)
Ammonia metabolism
Three main sources of blood ammonia
Amino acid deamination and amine breakdown
Intestinal bacterial putrefaction
Renal tubular epithelial cell secretion
Ammonia is transported in the blood to the liver or kidneys 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
Glutamine is both the detoxification product of ammonia and the storage and transportation form of ammonia.
The metabolic route of ammonia is the synthesis of urea in the liver
Urea is synthesized via the ornithine cycle (urea cycle)
Location: Mainly in mitochondria and cytoplasm of liver cells, trace amounts in brain and kidney
process:
①NH₃, CO₂ and ATP condense to form carbamoyl phosphate
Key enzyme: carbamoyl phosphate synthase-1 (CPS-1, priming)
Key enzyme activator: N-acetylglutamic acid (AGA)
②Carbamoyl phosphate ornithine → citrulline
Mitochondria
③citrulline aspartic acid → argininosuccinic acid
Key enzyme: argininosuccinate synthase (lowest activity, rate limiting)
④Argininosuccinic acid→arginine fumaric acid
⑤Arginine → Urea Ornithine
Cytoplasm
summary:
Raw materials: 2 molecules of ammonia, 1 free ammonia, aspartic acid
Process: Through the ornithine cycle, now in the mitochondria and then in the cytoplasm
Energy consumption: 3 ATP, 4 high-energy phosphate bonds
Regulation of urea synthesis
High-protein meals increase urea synthesis
AGA activates CPS-1 to initiate urea synthesis
Regulation of argininosuccinate synthase (least active, rate-limiting)
Urea synthesis disorder, elevated blood ammonia concentration
Hyperammonemia
Hepatic encephalopathy (ammonia poisoning)
Metabolism of individual amino acids
Decarboxylation of amino acids (decarboxylase) produces amines
Decarboxylation of glutamic acid produces γ-aminobutyric acid (GABA, an inhibitory neurotransmitter, which has an inhibitory effect on the central nervous system)
Decarboxylation of histamine produces histamine (a strong vasodilator that can increase capillary permeability, smooth muscle contraction, and stimulate pepsinogen and gastric acid secretion)
Tryptophan is hydroxylated and then decarboxylated to generate 5-hydroxytryptamine (5-HT, which acts as an inhibitory neurotransmitter in the brain and constricts blood vessels in peripheral tissues)
Decarboxylation of certain amino acids can produce polyamines (regulate cell growth)
Certain amino acids produce one-carbon units during catabolism
Tetrahydrofolate (FH4) participates in one-carbon unit metabolism as a one-carbon unit carrier
One-carbon unit concept: a group containing one carbon atom produced during the catabolism of certain amino acids
Methyl -CH₃
Methylene -CH₂-
Methine =CH-
formyl-CHO
Imidomethyl -CH=NH
The one-carbon unit is usually bound to the N4 and N10 positions of the FH4 molecule.
One-carbon units produced from amino acids can be converted into each other
The main function of the one-carbon unit is to participate in the synthesis of purine and pyrimidine
Metabolism of sulfur-containing amino acids can produce a variety of biologically active substances
Methionine is involved in methyl transfer
Methionine provides methyl group for creatine synthesis
Cysteine is related to the production of various physiologically active substances
Cysteine←→Cystine
Cysteine → Taurine
Cysteine → active sulfate
The metabolism of aromatic amino acids (phenylpropanol, phenol, color) requires oxygenase catalysis
Phenylalanine → tyrosine
Phenylketonuria, phenylalanine hydroxylase deficiency, in which phenylalanine cannot be metabolized normally into tyrosine. Phenylpyruvic acid, phenylpropanoic acid, etc. are generated through transamination and are excreted in the urine, causing hereditary metabolic diseases.
Tyrosine→Melanin Catecholamine
Reduced dopamine production in Parkinson's disease
The human body lacks tyrosinase, melanin synthesis is impaired, and the skin and hair become white, which is called albinism.
Other metabolic pathways of tyrosine: When the enzyme that metabolizes homogentisate in the body is congenitally defective, the decomposition of melanin is blocked, resulting in alkaptonuria.
Catabolism of tryptophan produces pyruvate and acetoacetyl CoA
The catabolism of branched-chain amino acids has a similar metabolic process