Scyllo-inosamine-4-phosphate amidinotransferase

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scyllo-inosamine-4-phosphate amidinotransferase
Identifiers
EC no. 2.1.4.2
CAS no. 52227-63-1
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ExPASy NiceZyme view
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MetaCyc metabolic pathway
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In enzymology, a scyllo-inosamine-4-phosphate amidinotransferase (EC 2.1.4.2) is an enzyme that catalyzes the chemical reaction

L-arginine + 1-amino-1-deoxy-scyllo-inositol 4-phosphate L-ornithine + 1-guanidino-1-deoxy-scyllo-inositol 4-phosphate

Thus, the two substrates of this enzyme are L-arginine and 1-amino-1-deoxy-scyllo-inositol 4-phosphate, whereas its two products are L-ornithine and 1-guanidino-1-deoxy-scyllo-inositol 4-phosphate.

This enzyme belongs to the family of transferases that transfer one-carbon groups, specifically the amidinotransferases. The systematic name of this enzyme class is L-arginine:1-amino-1-deoxy-scyllo-inositol-4-phosphate amidinotransferase. Other names in common use include L-arginine:inosamine-P-amidinotransferase, inosamine-P amidinotransferase, L-arginine:inosamine phosphate amidinotransferase, and inosamine-phosphate amidinotransferase. This enzyme participates in streptomycin biosynthesis.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1BWD.

Related Research Articles

The urea cycle (also known as the ornithine cycle) is a cycle of biochemical reactions that produces urea (NH2)2CO from ammonia (NH3). Animals that use this cycle, mainly amphibians and mammals, are called ureotelic.

<span class="mw-page-title-main">Ornithine</span> Chemical compound

Ornithine is a non-proteinogenic α-amino acid that plays a role in the urea cycle. Ornithine is abnormally accumulated in the body in ornithine transcarbamylase deficiency. The radical is ornithyl.

<span class="mw-page-title-main">Pyridoxal phosphate</span> Active form of vitamin B6

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.

Biosynthesis, i.e., chemical synthesis occurring in biological contexts, is a term most often referring to multi-step, enzyme-catalyzed processes where chemical substances absorbed as nutrients serve as enzyme substrates, with conversion by the living organism either into simpler or more complex products. Examples of biosynthetic pathways include those for the production of amino acids, lipid membrane components, and nucleotides, but also for the production of all classes of biological macromolecules, and of acetyl-coenzyme A, adenosine triphosphate, nicotinamide adenine dinucleotide and other key intermediate and transactional molecules needed for metabolism. Thus, in biosynthesis, any of an array of compounds, from simple to complex, are converted into other compounds, and so it includes both the catabolism and anabolism of complex molecules. Biosynthetic processes are often represented via charts of metabolic pathways. A particular biosynthetic pathway may be located within a single cellular organelle, while others involve enzymes that are located across an array of cellular organelles and structures.

<span class="mw-page-title-main">Cerebral creatine deficiency</span> Medical condition

Cerebral creatine deficiencies are a small group of inherited disorders that result from defects in creatine biosynthesis and utilization. Commonly affected tissues include the brain and muscles. There are three distinct CCDs. The most common is creatine transporter defect (CTD), an X-linked disorder caused by pathogenic variants in SLC6A8. The main symptoms of CTD are intellectual disability and developmental delay, and these are caused by a lack of creatine in the brain, due to the defective transporter. There are also two enzymatic defects of creatine biosynthesis, arginine:glycine amidinotransferase deficiency, caused by variants in GATM and guanidinoacetate methyltransferase deficiency, caused by variants in GAMT. The single enzyme defects are both inherited in an autosomal recessive manner.

The enzyme guanidinodeoxy-scyllo-inositol-4-phosphatase (EC 3.1.3.40) catalyzes the reaction

The enzyme streptomycin-6-phosphatase (EC 3.1.3.39) catalyzes the reaction

In enzymology, a glutamate N-acetyltransferase (EC 2.3.1.35) is an enzyme that catalyzes the chemical reaction

In enzymology, a 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol transaminase 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, a glutamine-scyllo-inositol transaminase is an enzyme that catalyzes the chemical reaction

In enzymology, a scyllo-inosamine 4-kinase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Aldehyde dehydrogenase 18 family, member A1</span> Protein-coding gene in the species Homo sapiens

Delta-1-pyrroline-5-carboxylate synthetase (P5CS) is an enzyme that in humans is encoded by the ALDH18A1 gene. This gene is a member of the aldehyde dehydrogenase family and encodes a bifunctional ATP- and NADPH-dependent mitochondrial enzyme with both gamma-glutamyl kinase and gamma-glutamyl phosphate reductase activities. The encoded protein catalyzes the reduction of glutamate to delta1-pyrroline-5-carboxylate, a critical step in the de novo biosynthesis of proline, ornithine and arginine. Mutations in this gene lead to hyperammonemia, hypoornithinemia, hypocitrullinemia, hypoargininemia and hypoprolinemia and may be associated with neurodegeneration, cataracts and connective tissue diseases. Alternatively spliced transcript variants, encoding different isoforms, have been described for this gene. As reported by Bruno Reversade and colleagues, ALDH18A1 deficiency or dominant-negative mutations in P5CS in humans causes a progeroid disease known as De Barsy Syndrome.

<span class="mw-page-title-main">Ribostamycin</span> Aminoglycoside antibiotic

Ribostamycin is an aminoglycoside-aminocyclitol antibiotic isolated from a streptomycete, Streptomyces ribosidificus, originally identified in a soil sample from Tsu City of Mie Prefecture in Japan. It is made up of 3 ring subunits: 2-deoxystreptamine (DOS), neosamine C, and ribose. Ribostamycin, along with other aminoglycosides with the DOS subunit, is an important broad-spectrum antibiotic with important use against human immunodeficiency virus and is considered a critically important antimicrobial by the World Health Organization., Resistance against aminoglycoside antibiotics, such as ribostamycin, is a growing concern. The resistant bacteria contain enzymes that modify the structure through phosphorylation, adenylation, and acetylation and prevent the antibiotic from being able to interact with the bacterial ribosomal RNAs.

Scyllo may refer to:

<span class="mw-page-title-main">Homoarginine</span> Chemical compound

Homoarginine is an nonproteinogenic alpha-amino acid. It is structurally equivalent to a one-methylene group-higher homolog of arginine and to the guanidino derivative of lysine. L-Homoarginine is the naturally-occurring enantiomer. Physiologically, homoarginine increases nitric oxide (NO) supply and betters endothelial functions in the body, with a particular correlation and effect towards cardiovascular outcome and mortality. At physiological pH, homoarginine is cationic: the guanidino group is protonated.

2-deoxy-scyllo-inosamine dehydrogenase (EC 1.1.1.329, neoA (gene name), kanK (gene name)) is an enzyme with systematic name 2-deoxy-scyllo-inosamine:NAD(P)+ 1-oxidoreductase. This enzyme catalyses the following chemical reaction

2-deoxy-scyllo-inosamine dehydrogenase (SAM-dependent) is an enzyme with systematic name 2-deoxy-scyllo-inosamine:S-adenosyl-L-methionine 1-oxidoreductase. This enzyme catalyses the following chemical reaction

2-deoxy-scyllo-Inosose synthase is an enzyme with systematic name D-glucose-6-phosphate phosphate-lyase (2-deoxy-scyllo-inosose-forming). This enzyme catalyses the following chemical reaction

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.

References