mutase$51058$ - ορισμός. Τι είναι το mutase$51058$
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Τι (ποιος) είναι mutase$51058$ - ορισμός

MAMMALIAN PROTEIN FOUND IN HOMO SAPIENS
Methylmalonyl Coenzyme A mutase; Methylmalonyl-coa mutase; Methylmalonyl mutase; Methylmalonyl-coenzyme A mutase; Methylmalonyl coenzyme A mutase; MUT (gene); EC 5.4.99.2; (R)-methylmalonyl-CoA CoA-carbonylmutase
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Methylmalonyl-CoA mutase         
Methylmalonyl-CoA mutase (, MCM), mitochondrial, also known as methylmalonyl-CoA isomerase, is a protein that in humans is encoded by the MUT gene. This vitamin B12-dependent enzyme catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA in humans.
5-(carboxyamino)imidazole ribonucleotide mutase         
CLASS OF ENZYMES
N5-carboxyaminoimidazole ribonucleotide mutase; EC 5.4.99.18; 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole carboxymutase
In enzymology, a 5-(carboxyamino)imidazole ribonucleotide mutase () is an enzyme that catalyzes the chemical reaction
Squalene-hopene cyclase         
  • Suggested active residues in squalene-hopene cyclase
  • Chemical structure of hopene
  • Space-filling model of the squalene molecule
  • Numerous tightly linked surface helices
CLASS OF ENZYMES
EC 5.4.99.17; Squalene mutase (cyclizing, hop-22(29)-ene-forming); Squalene—hopene cyclase
Squalene-hopene cyclase (SHC) () or hopan-22-ol hydro-lyase is an enzyme in the terpene cyclase/mutase family. It catalyzes the interconversion of squalene into a pentacyclic triterpenes, hopene and hopanol.

Βικιπαίδεια

Methylmalonyl-CoA mutase

Methylmalonyl-CoA mutase (EC 5.4.99.2, MCM), mitochondrial, also known as methylmalonyl-CoA isomerase, is a protein that in humans is encoded by the MUT gene. This vitamin B12-dependent enzyme catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA in humans. Mutations in MUT gene may lead to various types of methylmalonic aciduria.

MCM was first identified in rat liver and sheep kidney in 1955. In its latent form, it is 750 amino acids in length. Upon entry to the mitochondria, the 32 amino acid mitochondrial leader sequence at the N-terminus of the protein is cleaved, forming the fully processed monomer. The monomers then associate into homodimers, and bind AdoCbl (one for each monomer active site) to form the final, active holoenzyme form.