Porphobilinogen is a porphyrin precursor, specifically the organic compound intermediate in the biosynthesis of heme and chlorophyll, formed by the condensation of two pyrrole molecules in the liver and other tissues.

An enzyme that catalyzes the tetrapolymerization of the monopyrrole PORPHOBILINOGEN into the hydroxymethylbilane preuroporphyrinogen (UROPORPHYRINOGENS) in several discrete steps. It is the third enzyme in the 8-enzyme biosynthetic pathway of HEME. In humans, deficiency in this enzyme encoded by HMBS (or PBGD) gene results in a form of neurological porphyria (PORPHYRIA, ACUTE INTERMITTENT). This enzyme was formerly listed as EC 4.3.1.8

An enzyme that catalyzes the formation of porphobilinogen from two molecules of 5-aminolevulinic acid. EC 4.2.1.24.

Enzymes that catalyze the formation of a carbon-carbon double bond by the elimination of AMMONIA. EC 4.3.1.

An autosomal dominant porphyria that is due to a deficiency of HYDROXYMETHYLBILANE SYNTHASE in the LIVER, the third enzyme in the 8-enzyme biosynthetic pathway of HEME. Clinical features are recurrent and life-threatening neurologic disturbances, ABDOMINAL PAIN, and elevated level of AMINOLEVULINIC ACID and PORPHOBILINOGEN in the urine.

A diverse group of metabolic diseases characterized by errors in the biosynthetic pathway of HEME in the LIVER, the BONE MARROW, or both. They are classified by the deficiency of specific enzymes, the tissue site of enzyme defect, or the clinical features that include neurological (acute) or cutaneous (skin lesions). Porphyrias can be hereditary or acquired as a result of toxicity to the hepatic or erythropoietic marrow tissues.

Keto acids that are derivatives of 4-oxopentanoic acids (levulinic acid).

A compound produced from succinyl-CoA and GLYCINE as an intermediate in heme synthesis. It is used as a PHOTOCHEMOTHERAPY for actinic KERATOSIS.

A group of compounds containing the porphin structure, four pyrrole rings connected by methine bridges in a cyclic configuration to which a variety of side chains are attached. The nature of the side chain is indicated by a prefix, as uroporphyrin, hematoporphyrin, etc. The porphyrins, in combination with iron, form the heme component in biologically significant compounds such as hemoglobin and myoglobin.

Porphyrinogens which are intermediates in heme biosynthesis. They have four acetic acid and four propionic acid side chains attached to the pyrrole rings. Uroporphyrinogen I and III are formed from polypyrryl methane in the presence of uroporphyrinogen III cosynthetase and uroporphyrin I synthetase, respectively. They can yield uroporphyrins by autooxidation or coproporphyrinogens by decarboxylation.

Salts and esters of the 7-carbon saturated monocarboxylic acid heptanoic acid.

A group of metabolic diseases due to deficiency of one of a number of LIVER enzymes in the biosynthetic pathway of HEME. They are characterized by the accumulation and increased excretion of PORPHYRINS or its precursors. Clinical features include neurological symptoms (PORPHYRIA, ACUTE INTERMITTENT), cutaneous lesions due to photosensitivity (PORPHYRIA CUTANEA TARDA), or both (HEREDITARY COPROPORPHYRIA). Hepatic porphyrias can be hereditary or acquired as a result of toxicity to the hepatic tissues.

Porphyrins with four acetic acid and four propionic acid side chains attached to the pyrrole rings.

Liquid substances produced by living organisms to fulfill specific functions or excreted as waste.

A colorless compound formed in the intestines by the reduction of bilirubin. Some is excreted in the feces where it is oxidized to urobilin. Some is reabsorbed and re-excreted in the bile as bilirubin. At times, it is re-excreted in the urine, where it may be later oxidized to urobilin.

The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.

An enzyme that catalyzes the decarboxylation of UROPORPHYRINOGEN III to coproporphyrinogen III by the conversion of four acetate groups to four methyl groups. It is the fifth enzyme in the 8-enzyme biosynthetic pathway of HEME. Several forms of cutaneous PORPHYRIAS are results of this enzyme deficiency as in PORPHYRIA CUTANEA TARDA; and HEPATOERYTHROPOIETIC PORPHYRIA.

An enzyme of the transferase class that catalyzes condensation of the succinyl group from succinyl coenzyme A with glycine to form delta-aminolevulinate. It is a pyridoxyal phosphate protein and the reaction occurs in mitochondria as the first step of the heme biosynthetic pathway. The enzyme is a key regulatory enzyme in heme biosynthesis. In liver feedback is inhibited by heme. EC 2.3.1.37.

A mitochondrial enzyme found in a wide variety of cells and tissues. It is the final enzyme in the 8-enzyme biosynthetic pathway of HEME. Ferrochelatase catalyzes ferrous insertion into protoporphyrin IX to form protoheme or heme. Deficiency in this enzyme results in ERYTHROPOIETIC PROTOPORPHYRIA.

An enzyme that catalyzes the cyclization of hydroxymethylbilane to yield UROPORPHYRINOGEN III and water. It is the fourth enzyme in the 8-enzyme biosynthetic pathway of HEME, and is encoded by UROS gene. Mutations of UROS gene result in CONGENITAL ERYTHROPOIETIC PORPHYRIA.

Porphyrins with four methyl, two vinyl, and two propionic acid side chains attached to the pyrrole rings. Protoporphyrin IX occurs in hemoglobin, myoglobin, and most of the cytochromes.

Organic compounds that contain the (-NH2OH) radical.

Four PYRROLES joined by one-carbon units linking position 2 of one to position 5 of the next. The conjugated bond system results in PIGMENTATION.

Flammable, amorphous, vegetable products of secretion or disintegration, usually formed in special cavities of plants. They are generally insoluble in water and soluble in alcohol, carbon tetrachloride, ether, or volatile oils. They are fusible and have a conchoidal fracture. They are the oxidation or polymerization products of the terpenes, and are mixtures of aromatic acids and esters. Most are soft and sticky, but harden after exposure to cold. (From Grant & Hackh's Chemical Dictionary, 5th ed & Dorland, 28th ed)

Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.

Chloro(7,12-diethenyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-dipropanoato(4-)-N(21),N(22),N(23),N(24)) ferrate(2-) dihydrogen.

A species of fresh-water, flagellated EUKARYOTES in the phylum EUGLENIDA.

'Lead poisoning' is a type of heavy metal toxicity caused by increased levels of lead in the body, typically resulting from exposure to lead-containing substances or environments, and potentially leading to neurological issues, anemia, and developmental delays, especially in children.

A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.

Colorless reduced precursors of porphyrins in which the pyrrole rings are linked by methylene (-CH2-) bridges.

Azoles of one NITROGEN and two double bonds that have aromatic chemical properties.

Dicarboxylic acids are organic compounds containing two carboxyl (-COOH) groups in their structure, making them capable of forming salts and esters by losing two hydrogen ions.

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.