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Literature summary for 3.1.1.53 extracted from

  • Hayes, B.K.; Varki, A.
    O-Acetylation and de-O-acetylation of sialic acids. Sialic acid esterases of diverse evolutionary origins have serine active sites and essential arginine residues. (1989), J. Biol. Chem., 264, 19443-19448.
    View publication on PubMed
Search for more literature for 3.1.1.53

Inhibitors

Inhibitors Comment Organism Structure
2,3-Butanedione inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition Asterias rubens
2,3-Butanedione inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition Dicentrarchus labrax
2,3-Butanedione inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition Homo sapiens
2,3-Butanedione inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition influenza C virus
2,3-Butanedione inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition Rattus norvegicus
diisopropyl fluorophosphate
-
 Asterias rubens
diisopropyl fluorophosphate
-
 Dicentrarchus labrax
diisopropyl fluorophosphate
-
 Homo sapiens
diisopropyl fluorophosphate
-
 influenza C virus
diisopropyl fluorophosphate
-
 Rattus norvegicus
Phenylglyoxal inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition Asterias rubens
Phenylglyoxal inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition Dicentrarchus labrax
Phenylglyoxal inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition Homo sapiens
Phenylglyoxal inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition influenza C virus
Phenylglyoxal inhibited by this arginine-modifying reagents, an essential arginine residue in the active site is important for substrate recognition Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Asterias rubens
-
 starfish
-
Dicentrarchus labrax
-
 sea bass
-
Homo sapiens
-
-
-
influenza C virus
-
-
-
no activity in Dictyostelium discoideum
-
-
-
no activity in Glycine max
-
-
-
no activity in Hirudo medicinalis
-
 medicinal leech
-
no activity in Nicotiana tabacum
-
-
-
no activity in Spodoptera frugiperda
-
 fall armyworm, Sf-9 cells
-
Rattus norvegicus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification glycoprotein, partly resistant to endo-beta-N-acetylglycosaminidase H, but sensitive to peptide N-glycosidase Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Rattus norvegicus
-
brain
-
 Dicentrarchus labrax
-
erythrocyte
-
 Homo sapiens
-
gonad
-
 Asterias rubens
-
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-9-O-acetylneuraminate + H2O
-
 Homo sapiens N-acetylneuraminate + acetate
-
 ?
N-acetyl-9-O-acetylneuraminate + H2O
-
 Rattus norvegicus N-acetylneuraminate + acetate
-
 ?
N-acetyl-9-O-acetylneuraminate + H2O
-
 Dicentrarchus labrax N-acetylneuraminate + acetate
-
 ?
N-acetyl-9-O-acetylneuraminate + H2O
-
 influenza C virus N-acetylneuraminate + acetate
-
 ?
N-acetyl-9-O-acetylneuraminate + H2O
-
 Asterias rubens N-acetylneuraminate + acetate
-
 ?