Lippincott's Biochemistry Chapter 21 - Amino Acids (Conversion to Specialized Products)

An enzyme involved in porphyrin metabolism found in all tissues.

An enzyme involved in porphyrin metabolism, specifically in erythroid cells.

A genetic disorder caused by mutations in ALAS2, leading to iron overload.

A molecule crucial for various functions, produced from porphyrin.

A form of heme resulting from the oxidation of iron.

The extent to which ALAS1 is active in catalyzing porphyrin production.

A system in the liver that metabolizes drugs using heme-proteins.

The biochemical pathway for producing porphyrins, which go on to make heme.

Variable, adjusting to fluctuating needs for hemeproteins in the cell.

Relatively constant, matching the rate of globin synthesis.

Mitochondria are involved in the initial and final three steps of porphyrin building.

The intermediate stages of porphyrin synthesis occur in the cytosol of the cell.

A crucial building block of porphyrins, formed from glycine and succinyl CoA.

Enzyme catalyzing the formation of 6-aminolevulinic acid (the committed step of porphyrin synthesis).

The activity of ALAS is regulated by the amount of iron available .

A coenzyme needed for the synthesis of 6-Aminolevulinic acid (ALA).

The creation of CYP proteins, which are enzymes involved in metabolic processes, is stimulated by certain drugs.

Increased CYP protein synthesis consumes more heme, resulting in lower heme levels in liver cells.

Lower intracellular heme levels trigger the production of ALAS1, a vital enzyme in heme synthesis.

Increased ALAS1 production leads to a corresponding rise in the synthesis of another molecule needed for heme formation, ALA.

Two molecules of ALA combine to create PBG, a crucial step in heme biosynthesis, catalyzed by ALA dehydratase.

The enzyme that forms PBG is very sensitive to heavy metal ions, like lead, which can block its function.

Lead poisoning blocks PBG synthesis, resulting in elevated ALA levels and anemia.

Four PBG molecules condense to form uroporphyrinogen III, a crucial tetrapyrrole.

Methyl and vinyl groups derived from decarboxylation of acetate and propionate side chains.

Four different arrangements (I-IV) of side chains around the porphyrin nucleus.

The only physiologically important porphyrin type in humans.

A type III porphyrin.

Reduced, colorless precursors to protoporphyrins in heme biosynthesis.

Primarily the liver and bone marrow erythrocyte-producing cells.

Synthesis of a variety of enzymes crucial for biological processes.

Precursor in heme biosynthesis.

Starting material for heme synthesis

A porphyrin precursor that is generated from a cyclic tetrapyrrole by the decarboxylation of its acetate groups.

Enzyme that catalyzes the decarboxylation of acetate groups in the cyclic tetrapyrrole to produce coproporphyrinogen III.

A porphyrin precursor, generated from Coproporphyrinogen III by decarboxylation of propionate side chains, that is oxidized to protoporphyrin IX in the mitochondria.

Conversion of protoporphyrinogen IX to protoporphyrin IX, followed by the incorporation of iron (Fe2+) to create heme.

Inherited or acquired defects in heme synthesis leading to accumulation of porphyrins or precursors in the body.

The removal of a carboxyl group (-COOH) from a molecule.

Amino acids are converted into many important biological compounds like porphyrins, neurotransmitters, hormones, etc.

Porphyrins are cyclic, planar molecules built from 4 pyrrole rings linked by methenyl bridges.

Heme is a crucial component for hemoglobin, myoglobin, cytochromes, and other vital molecules.

The rate of heme synthesis in the liver adjusts to the body's needs for different hemeproteins.

The biochemical pathway for producing porphyrins that are necessary to form heme and other important compounds

Different chemical groups attached to the pyrrole rings in porphyrin molecules, influencing their properties and function.

The only biologically important porphyrin type in humans, distinguished by their specific arrangement of side chains.

A porphyrin with acetate and propionate side chains.

A specific type III porphyrin crucial for forming heme, the most common type of heme.

Porphyrins are flat, ring-like molecules with four pyrrole rings linked together.

A porphyrin with methyl and propionate side chains.

Specific patterns in how side chains are positioned around the porphyrin molecule.

The reduced, colorless forms of protoporphyrins.

Methyl and vinyl groups formed from the decarboxylation of acetate and propionate side chains.

Four different arrangements (I-IV) of side chains around the porphyrin nucleus.

The only physiologically important porphyrin type in humans.

A type III porphyrin.

Reduced, colorless precursors to protoporphyrins in heme biosynthesis.

Primarily the liver and bone marrow erythrocyte-producing cells.

A crucial building block of porphyrins, formed from glycine and succinyl CoA.

The removal of a carboxyl group (-COOH) from a molecule.

Two molecules of ALA combine to create PBG, a crucial step in heme biosynthesis, catalyzed by ALA dehydratase.

The enzyme that forms PBG is very sensitive to heavy metal ions, like lead, which can block its function.

Highly variable, adapting to cellular demands for hemeproteins.

Relatively constant, matching globin synthesis rate.

Initial and final three steps of porphyrin production happen in mitochondria..

Intermediate steps in porphyrin synthesis occur in the cytosol.

Building block for porphyrins, formed from glycine and succinyl CoA.

Enzyme creating 6-Aminolevulinic acid (ALA), the committed step.

ALAS activity is controlled by iron levels.

Coenzyme needed for ALA synthesis.

Enzyme in porphyrin synthesis, found in all tissues.

Enzyme in porphyrin synthesis, specifically in red blood cells.

Genetic defect in ALAS2, leading to iron overload.

Hemin reduces ALAS1 activity by repressing its gene expression.

Some drugs increase liver ALAS1 activity via CYP monooxygenase.

Liver system using hemeproteins to metabolize some drugs.

Variable rate, adjusted to meet the body's needs for hemeproteins.

Relatively constant, matching the rate of hemoglobin synthesis.

Initial and final stages happen in mitochondria; intermediate in the cytosol.

Amino acids are transformed into various biologically important compounds like porphyrins, neurotransmitters, and hormones.

Porphyrins are cyclic, planar molecules formed by linking four pyrrole rings with methenyl bridges.

Heme is a vital component of hemoglobin, myoglobin, cytochromes, and other crucial molecules.

The rate of heme synthesis in the liver is variable, adapting to the body's needs for different hemeproteins.

The biochemical pathway for producing porphyrins to make heme and other important compounds.

Chemical groups attached to porphyrin rings, influencing their function and properties.

The only significant porphyrin type in humans, distinguished by a specific side-chain arrangement.

A crucial type III porphyrin essential for heme formation.

Reduced, colorless precursors to protoporphyrins in heme biosynthesis.

A key building block of porphyrins, created from glycine and succinyl CoA.

The removal of a carboxyl group (-COOH) from a molecule.

Two ALA molecules combine to form PBG, a crucial step in heme biosynthesis, catalyzed by ALA dehydratase.

The enzyme that forms PBG is extremely sensitive to heavy metal ions like lead, hindering its function.

Different chemical groups attached to the pyrrole rings in porphyrin molecules, influencing their properties and function.

The only biologically important porphyrin type in humans, distinguished by their specific arrangement of side chains.

A porphyrin with acetate and propionate side chains.

A specific type III porphyrin crucial for forming heme, the most common type of heme.

A porphyrin with methyl and propionate side chains.

Specific patterns in how side chains are positioned around the porphyrin molecule.

The reduced, colorless forms of protoporphyrins.

Porphyrins are flat, ring-like molecules with four pyrrole rings linked together.

Methyl and vinyl groups formed from the decarboxylation of acetate and propionate side chains.

Four different arrangements (I-IV) of side chains around the porphyrin nucleus.

The only physiologically important form of porphyrin in humans. They have a specific arrangement of side chains.

A type III porphyrin, and crucial for the formation of heme.

Reduced, colorless precursors in heme biosynthesis leading to protoporphyrins.