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Literature summary for 2.7.1.39 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
Search for more literature for 2.7.1.39

Application

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

Inhibitors

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Leishmania major Q4Q6Y2
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

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

Subunits

Subunits Comment Organism
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

Synonyms Comment Organism
HSK
-
 Leishmania major

General Information

General Information Comment Organism
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