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Literature summary for 1.1.1.25 extracted from

  • Skariyachan, S.; Manjunath, M.; Bachappanavar, N.
    Screening of potential lead molecules against prioritised targets of multi-drug-resistant-Acinetobacter baumannii - insights from molecular docking, molecular dynamic simulations and in vitro assays (2019), J. Biomol. Struct. Dyn., 37, 1146-1169 .
    View publication on PubMed
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Application

Application Comment Organism
drug development the enzyme is a target for drug development required for Acinetobacter baumannii, a member of ESKAPE pathogens, that has emerged as an extreme drug-resistant bacterium towards most of the current generation. Acinetobacter baumannii demonstrates resistance to nearly all major classes of antibiotics, including broad-spectrum penicillins, carbapenems, cephalosporins, fluoroquinolones, aminoglycosides, tetracyclines, chloramphenicol, and colistin, especially polymixin, creating a public health threat worldwide Acinetobacter baumannii

Inhibitors

Inhibitors Comment Organism Structure
ajmalicine (19alpha)-16,17-didehydro-19-methyloxayohimban-16-carboxylic acid methyl ester, from Rauwolfia serpentina leaves and roots, interacting residues are Asp131 and Arg130 Acinetobacter baumannii
limonin 7,16-dioxo-7,16-dideoxylimondiol, from Citrus sp. fruits, interacting residues are Thr75, Thr78, Val71, Gln101, and Pro103 Acinetobacter baumannii
additional information ten clinical isolates of Acinetobacter baumannii are used for inhibitor screening. Ajmalicine, strictamin, and limonin exhibit promising binding towards multiple drug targets of Acinetobacter baumannii in comparison with the binding between standard drugs and their targets. The tested isolates exhibit resistance to antibiotics clinafloxacin, imipenem and polymyxin-E, and the herbal preparations (crude extracts) demonstrate a significant antibacterial potential. Docking study and molecular dynamic simulations, model refinement and validation, overview. Acinetobacter baumannii exhibits resistance to a broad range of antibiotics due to the presence of a protective capsule, lipopolysaccharide, AbaR resistance islands, OmpA, efflux pumps, biofilms formation, and other mechanisms. Evaluation of drug targets in Acinetobacter baumannii. The toxicity prediction for ajmalicine (Rauvolfia serpentina) and strictamin (Alstonia scholaris) are predicted to be non-carcinogenic in both mouse and rat models making them potential leads Acinetobacter baumannii
strictamin akuammilan-17-oic acid methyl ester, from Alstonia scholaris leaves, interacting residues are Tyr129, Gln126, and Leu125 Acinetobacter baumannii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
shikimate + NADP+ Acinetobacter baumannii
-
 3-dehydroshikimate + NADPH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii
-
 ten clinical isolates, multi-drug resistant lines
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
shikimate + NADP+
-
 Acinetobacter baumannii 3-dehydroshikimate + NADPH + H+
-
 r

Synonyms

Synonyms Comment Organism
AroE
-
 Acinetobacter baumannii
HpSDH
-
 Acinetobacter baumannii

Cofactor

Cofactor Comment Organism Structure
NADP+
-
 Acinetobacter baumannii
NADPH
-
 Acinetobacter baumannii

General Information

General Information Comment Organism
metabolism shikimate dehydrogenase is one of the enzymes involved in the initial steps of the biosynthesis of amino acids such as histidine, tryptophan, tyrosine, phenylalanine, lysine, and aspartic acid Acinetobacter baumannii
additional information three-dimensional stucture homology modelling (PMDB ID PM0080741), model refinement and validation, overview Acinetobacter baumannii