Question

which of the following aminoacids is involved in the formation of Heme ?
A) Tryptophan
B) Tyrosine
C) Glycine
D) Histidine

First person to answer correctly with explaination will be marked as brainliest.​

Answer 1

Answer:

i think i am the first person plzz mark as brainliest

A) your answer is Glycine!

Heme synthesis starts in mitochondria with the condensation of succinyl-CoA with the amino acid glycine, activated by pyridoxal phosphate. ALA synthase is the rate-limiting enzyme of heme synthesis.

Explanation:

its from google :Heme synthesis starts in mitochondria with the condensation of succinyl-CoA with the amino acid glycine, activated by pyridoxal phosphate. ALA synthase is the rate-limiting enzyme of heme synthesis. ALA molecules enter the cytoplasm, where their union in the presence of ALA dehydratase yields porphobilinogen (PBG) and water molecules. Four PBG molecules are joined by uroporphyrinogen I synthase (PBG deaminase) as linear tetrapyrrole called hydroxymethylbilane. Linear tetrapyrrole cyclizes to form a ring known as uroporphyrinogen III (UPG) with the participation of uroporphyrinogen III synthase. All acetyl groups of UPG are converted to methyl groups by decarboxylation and coproporphyrinogen III (CPG) is generated. CPG is acted upon in mitochondria by CPG oxidase, which decarboxylates and oxidizes two propionic side chains to vinyl groups. Protoporphyrinogen thus formed is further oxidized to protoporphyrins. Molecular oxygen is required for conversion of CPG to protoporphyrins. Finally, iron is incorporated to generate heme.

Metabolism of Iron and Heme

N.V. Bhagavan, Chung-Eun Ha, in Essentials of Medical Biochemistry (Second Edition), 2015

Formation of δ-Aminolevulinic Acid

δ-Aminolevulinic acid (ALA) formation is catalyzed by mitochondrial ALA synthase, which condenses glycine and succinyl-CoA to ALA:

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The ALA synthase is located on the matrix side of the inner mitochondrial membrane. It is encoded by a nuclear gene.

Heme synthesis also requires a functional tricarboxylic acid (TCA) cycle and an oxygen supply. The primary regulatory step of heme synthesis in the liver is apparently that catalyzed by ALA synthase. The regulatory effects are multiple. The normal end product, heme, when in excess of that needed for production of heme proteins, is oxidized to hematin, which contains a hydroxyl group attached to the Fe3+ atom. Replacement of the hydroxyl group by a chloride ion produces hemin. Hemin and heme inhibit ALA synthase allosterically. Induction of ALA synthase is suppressed by hemin and increased by a variety of xenobiotics (e.g., environmental pollutants) and natural steroids. In erythropoietic tissues, where the largest amount of heme is synthesized, regulation of heme biosynthesis may also involve the process of cell differentiation and proliferation of the erythron, which occurs to meet a change in the requirements for synthesis of heme. The differentiation and proliferation are initiated by erythropoietin