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Qué (quién) es S-Adenozilmetionin:tRNA ribosyltransferase-isomerase - definición
S-Adenozilmetionin:tRNA ribosyltransferase-isomerase
CLASS OF ENZYMES
EC 2.4.99.17; QueA enzyme; Queuosine biosynthesis protein QueA; S-adenosyl-L-methionine:7-aminomethyl-7-deazaguanosine ribosyltransferase (ribosyl isomerizing; L-methionine, adenine releasing); S-adenozil-L-metionin:7-aminomethyl-7-deazaguanosine ribosyltransferase (ribosyl isomerizing; L-metionin, adenine releasing); S-adenozilmetionin:tRNA ribosyltransferase-isomerase
S-Adenosylmethionine:tRNA ribosyltransferase-isomerase (, QueA enzyme, queuosine biosynthesis protein QueA) is an enzyme with systematic name S-adenosyl-L-methionine:7-aminomethyl-7-deazaguanosine ribosyltransferase (ribosyl isomerizing; L-methionine, adenine releasing). This enzyme catalyses the following chemical reaction
Prolyl isomerase
CLASS OF ENZYMES
Peptidylprolyl isomerase; PPIase; Peptidyl prolyl cis/trans isomerase; Peptidyl prolyl cis-trans-isomerase; PPlase domain; PPlase; Peptidyl prolyl cis-trans isomerase; Peptidylprolylisomerase; Prolylisomerase; Peptidyl-prolyl cis-trans isomerase; EC 5.2.1.8; Peptidylproline cis-trans-isomerase; Peptidyl-prolyl isomerase; Cis-trans prolyl isomerase
Prolyl isomerase (also known as peptidylprolyl isomerase or PPIase) is an enzyme () found in both prokaryotes and eukaryotes that interconverts the cis and trans isomers of peptide bonds with the amino acid proline. Proline has an unusually conformationally restrained peptide bond due to its cyclic structure with its side chain bonded to its secondary amine nitrogen.
Methylitaconate Delta-isomerase
CLASS OF ENZYMES
Methylitaconate D-isomerase; EC 5.3.3.6; Methylitaconate Delta2-Delta3-isomerase
In enzymology, a methylitaconate Delta-isomerase () is an enzyme that catalyzes the chemical reaction
