aminoacylase

All Noun Verb
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  • Many scientific studies throughout the past half century have used porcine aminoacylase as their model aminoacylase enzyme.
  • The amino acid sequence and primary structure of porcine aminoacylase have been determined.
  • The nucleophilic attack by water is the rate-limiting step of aminoacylase's catalytic mechanism.
  • It is this dimerization that allows catalysis to occur, since aminoacylase's active site lies between its two Zinc binding domains.
  • Porcine aminoacylase differs from human aminoacylase in structure but replicates its function.
  • Aminoacylase 2 is known for the fact that it can hydrolyze N-acetylaspartate while aminoacylase 1 cannot.
  • Aminoacylase is involved in the regulation of the urea cycle.
  • The diagnosis can be confirmed by sequencing of the aminoacylase 1 gene.
  • Additionally, N-acyl-L-amino acids cannot be used directly as building blocks for proteins and must first be converted to L-amino acids by aminoacylase.
  • Of the N-actyl amino hydrolyzing enzymes, aminoacylase 1 is the most common.
  • Other names in common use include long-chain aminoacylase, long-chain-fatty-acyl-glutamate deacylase, long-chain acylglutamate amidase, and N-acyl-D-glutamate deacylase.
  • The Zinc ions inside of aminoacylase are each coordinated to histidine, glutamate, aspartate, and water.
  • Aminoacylase-1 is an enzyme that in humans is encoded by the ACY1 gene.
  • Aminoacylase 1 deficiency is a rare inborn error of metabolism.
  • Porcine aminoacylase 1 is composed of two identical heterodimeric subunits each consisting of 406 amino acids, with acetylalanine at the N-terminus of each.
  • Aminoacylase is up-regulated during times of nutrient deficit or starvation, causing N-acetyl-L-glutamate breakdown, which down-regulates carbamoyl phosphate synthetase and the rest of the urea cycle.
  • Aminoacylase 1 exists in a heterotetrameric structure, meaning 2 Zinc binding domains and 2 dimerization domains come together to make aminoacylase 1's quaternary structure.
  • The lack of functional aminoacylase 1 caused by A1D results in a dysfunctional urea cycle, causing an array of neurological disorders including seizures, muscular hypotonia, mental retardation, and impaired psychomotor development.
  • Canavan disease, also called Canavan-Van Bogaert-Bertrand disease, aspartoacylase deficiency or aminoacylase 2 deficiency, is an autosomal recessive degenerative disorder that causes progressive damage to nerve cells in the brain.
  • Aminoacylase 2 Deficiency - also known as Canavan's Disease - is another rare disease caused by a mutation in the ASPA gene (on chromosome 17) that leads to a deficiency in the enzyme aminoacylase 2.
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Words starting with aminoacylase