glutamate-1-semialdehyde 2,1-aminomutase | |||||||||
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Identifiers | |||||||||
EC no. | 5.4.3.8 | ||||||||
CAS no. | 68518-07-0 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a glutamate-1-semialdehyde 2,1-aminomutase (EC 5.4.3.8) is an enzyme that catalyzes the chemical reaction
Hence, this enzyme has one substrate, L-glutamate-1-semialdehyde, and one product, 5-aminolevulinate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The systematic name of this enzyme class is (S)-4-amino-5-oxopentanoate 4,5-aminomutase. This enzyme is also called glutamate-1-semialdehyde aminotransferase. This enzyme participates in porphyrin and chlorophyll biosynthesis. It employs one cofactor, pyridoxal phosphate.
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 2CFB, 2E7U, 2EPJ, 2GSA, 2HOY, 2HOZ, 2HP1, 2HP2, 3GSB, and 4GSA.
Pyridoxal phosphate (PLP, pyridoxal 5'-phosphate, P5P), the active form of vitamin B6, is a coenzyme in a variety of enzymatic reactions. The International Union of Biochemistry and Molecular Biology has catalogued more than 140 PLP-dependent activities, corresponding to ~4% of all classified activities. The versatility of PLP arises from its ability to covalently bind the substrate, and then to act as an electrophilic catalyst, thereby stabilizing different types of carbanionic reaction intermediates.
In molecular biology, biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism.
Homoserine (also called isothreonine) is an α-amino acid with the chemical formula HO2CCH(NH2)CH2CH2OH. L-Homoserine is not one of the common amino acids encoded by DNA. It differs from the proteinogenic amino acid serine by insertion of an additional -CH2- unit into the backbone. Homoserine, or its lactone form, is the product of a cyanogen bromide cleavage of a peptide by degradation of methionine.
Amino acid synthesis is the set of biochemical processes by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids. These 11 are called the non-essential amino acids).
Ornithine aminotransferase (OAT) is an enzyme which is encoded in human by the OAT gene located on chromosome 10.
1-Pyrroline-5-carboxylic acid is a cyclic imino acid. Its conjugate base and anion is 1-pyrroline-5-carboxylate (P5C). In solution, P5C is in spontaneous equilibrium with glutamate-5-semialdhyde (GSA).
In enzymology, a glutamate-5-semialdehyde dehydrogenase (EC 1.2.1.41) is an enzyme that catalyzes the chemical reaction
In enzymology, 4-aminobutyrate transaminase, also called GABA transaminase or 4-aminobutyrate aminotransferase, or GABA-T, is an enzyme that catalyzes the chemical reaction:
In enzymology, an acetylornithine transaminase (EC 2.6.1.11) is an enzyme that catalyzes the chemical reaction
In enzymology, an aminolevulinate transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, an aromatic-amino-acid transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, a D-amino-acid transaminase is an enzyme that catalyzes the chemical reaction:
In enzymology, a diaminobutyrate-2-oxoglutarate transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, glutamate-prephenate aminotransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a leucine transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, a L-lysine 6-transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, a succinylornithine transaminase (EC 2.6.1.81) is an enzyme that catalyzes the chemical reaction
The α-aminoadipate pathway is a biochemical pathway for the synthesis of the amino acid L-lysine. In the eukaryotes, this pathway is unique to the higher fungi and the euglenids. It has also been reported from bacteria of the genus Thermus.
Glutamate-5-semialdehyde is a non-proteinogenic amino acid involved in both the biosynthesis and degradation of proline and arginine, as well as in the biosynthesis of antibiotics, such as carbapenems. It is synthesized by the reduction of glutamyl-5-phosphate by glutamate-5-semialdehyde dehydrogenase.
Arginine and proline metabolism is one of the central pathways for the biosynthesis of the amino acids arginine and proline from glutamate. The pathways linking arginine, glutamate, and proline are bidirectional. Thus, the net utilization or production of these amino acids is highly dependent on cell type and developmental stage. Altered proline metabolism has been linked to metastasis formation in breast cancer.