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Literature summary extracted from

  • Meshram, R.J.; Shirsath, A.; Aouti, S.; Bagul, K.; Gacche, R.N.
    Molecular modeling and simulation study of homoserine kinase as an effective leishmanial drug target (2020), J. Mol. Model., 26, 218 .
    View publication on PubMed

Application

EC Number Application Comment Organism
2.7.1.39 drug development molecular modeling and simulation study of homoserine kinase as an effective leishmanial drug target Leishmania major

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.39 (1R,3r,5S)-8-[(1-cyclohexyl-1H-tetrazol-5-yl)methyl]-3-(pyridin-3-yl)-8-azabicyclo[3.2.1]octan-3-ol
-
 Leishmania major
2.7.1.39 (2S)-1-(9H-carbazol-9-yl)-3-(piperazin-1-yl)propan-2-ol
-
 Leishmania major
2.7.1.39 (naphthalen-1-yl)(1,3,5-triazatricyclo[3.3.1.13,7]decan-7-yl)methanone
-
 Leishmania major
2.7.1.39 1-(3,4-dihydroquinolin-1(2H)-yl)-2-[[1-(4-methylphenyl)-1H-tetrazol-5-yl]sulfanyl]ethan-1-one
-
 Leishmania major
2.7.1.39 1-[(2R,6S)-2,6-dimethylpiperidin-1-yl]-2-[([1,2,4]triazolo[4,3-a]pyrimidin-3-yl)sulfanyl]ethan-1-one
-
 Leishmania major
2.7.1.39 1-[(2R,6S)-2,6-dimethylpiperidin-1-yl]-2-[4-(4-methylbenzoyl)piperidin-1-yl]ethan-1-one
-
 Leishmania major
2.7.1.39 2-[(5-amino-4-phenyl-4H-1,2,4-triazol-3-yl)sulfanyl]-N-(naphthalen-1-yl)acetamide
-
 Leishmania major
2.7.1.39 L-threonine competitive inhibition Leishmania major
2.7.1.39 additional information virtual screening of a compound library and docking study, binding free energies, overview Leishmania major
2.7.1.39 N,N'-(pyridine-2,5-diyl)dicyclohexanecarboxamide
-
 Leishmania major
2.7.1.39 N-[(3r)-adamantan-1-yl]-2-[3-(2-methylphenyl)-6-oxopyridazin-1(6H)-yl]acetamide
-
 Leishmania major

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.39 Mg2+ required, binding structure, modelling Leishmania major

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.39 ATP + L-homoserine Leishmania major
-
 ADP + O-phospho-L-homoserine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.39 Leishmania major Q4Q6Y2
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.39 ATP + L-homoserine = ADP + O-phospho-L-homoserine possible catalytic mechanism of leishmanial homoserine kinase from molecular simulations Leishmania major
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.39 ATP + L-homoserine
-
 Leishmania major ADP + O-phospho-L-homoserine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.39 More the predicted HSK structure contains two distinct domains, the N-terminal domain (1-161, 280-285) and remaining residues constitute the C-terminal domain. The N-terminal domain is formed by two beta-sheets that enclose a core formed of four helices. The active site of HSK is located at the interface of N- and C-domains Leishmania major

Synonyms

EC Number Synonyms Comment Organism
2.7.1.39 HSK
-
 Leishmania major

General Information

EC Number General Information Comment Organism
2.7.1.39 additional information molecular modeling and simulation study of homoserine kinase (HSK) as an effective leishmanial drug target. Two MD simulations are performed on HSK enzyme without substrate (for reference), and on the enzyme in complex with the substrate, prosthetic group, and the magnesium ion using the NAMD program with CHARMM all-atom force field. The topology and parameters for the ligands used in this study are obtained from the MATCH web server. Virtual screening of a compound library and docking study. Homology modeling using several templates, overview. The active site of HSK mainly constitutes of two aspartates, two asparagine residues, and an arginine. All these residues are found to be optimally placed in the predicted model (Asn23, Asp29, Asp144, Asn145, and Arg241). Substrate recognition and structure-function analysis Leishmania major