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Active site of T. thermophilus hpaB, showing hydrogen bonding of hpaB catalytic residues to 4-hydroxyphenylacetate and to the peroxide bound to FADH 2. (Note: this structure was generated using oxidized FAD in place of FADH 2; the magenta sphere representing oxygen here is actually a water molecule believed to occupy the space oxygen does when the flavin hydroxyperoxide is present.
In enzymology, a phenylalanine 2-monooxygenase (EC 1.13.12.9) is an enzyme that catalyzes the chemical reaction. L-phenylalanine + O 2 2-phenylacetamide + CO 2 + H 2 O. Thus, the two substrates of this enzyme are L-phenylalanine and O 2, whereas its 3 products are 2-phenylacetamide, CO 2, and H 2 O.
[9] French chemist Anselme Payen was the first to discover an enzyme, ... A key question is therefore whether and how enzymes can change their enzymatic activities ...
In enzymology, a phosphoamidase (EC 3.9.1.1) is an enzyme that catalyzes the chemical reaction. N-phosphocreatine + H 2 O creatine + phosphate. Thus, the two substrates of this enzyme are N-phosphocreatine and H 2 O, whereas its two products are creatine and phosphate.
Aralkylamine dehydrogenase (azurin) (EC 1.4.9.2, aromatic amine dehydrogenase, arylamine dehydrogenase, tyramine dehydrogenase) is an enzyme with the systematic name aralkylamine:azurin oxidoreductase (deaminating).
Heme oxygenase 1 (HMOX1, commonly HO-1) is a member of the heat shock protein (HSP) family identified as HSP32.HO-1 is a 32kDa enzyme which contains 288 amino acid residues encoded by the HMOX1 gene.
The active site is usually a groove or pocket of the enzyme which can be located in a deep tunnel within the enzyme, [3] or between the interfaces of multimeric enzymes. An active site can catalyse a reaction repeatedly as residues are not altered at the end of the reaction (they may change during the reaction, but are regenerated by the end ...
The distance between the enzyme residues and the enantiomers is 3.5 Å and 3.6 Å respectively. [4] Structural studies of enzyme complexes with a synthetic L-alanine analog, a tight binding inhibitor [5] and propionate [6] further validate that Tyr265 and Lys39 are catalytic bases for the reaction,. [5] [7]