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Literature summary for 3.2.1.14 extracted from

  • Zhao, Y.S.; Zheng, Q.C.; Zhang, H.X.; Chu, H.Y.; Sun, C.C.
    Analysis of a three-dimensional structure of human acidic mammalian chitinase obtained by homology modeling and ligand binding studies (2009), J. Mol. Model., 15, 499-505.
    View publication on PubMed

Application

Application Comment Organism
pharmacology hAMCase is a potential therapeutic target for anti-inflammatory therapy in Th2-mediated diseases such as asthma Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
allosamidin modelling of ligand binding at the active site, Glu119 forms hydrogen bond with allosamidin. Trp10, Glu49, Asp192, and Glu276 in hAMCase are four important determinant residues in binding as they form strong van der Waals and electrostatic interactions with the ligand, respectively Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9BZP6
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-

Source Tissue

Source Tissue Comment Organism Textmining
lung
-
Homo sapiens
-
stomach
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information modelling of (GlcNAc)2 ligand binding at the active site Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
More three-dimensional structure modelling using the crystal structure of the human chitotriosidase, EC 3.2.1.44, PDB ID 1HKK, and the molecular mechanics and molecular dynamics methods, overview Homo sapiens

Synonyms

Synonyms Comment Organism
acidic mammalian chitinase
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Homo sapiens
AMCase
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Homo sapiens