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Literature summary extracted from

  • Gangadharappa, B.S.; Sharath, R.; Revanasiddappa, P.D.; Chandramohan, V.; Balasubramaniam, M.; Vardhineni, T.P.
    Structural insights of metallo-beta-lactamase revealed an effective way of inhibition of enzyme by natural inhibitors (2019), J. Biomol. Struct. Dyn., 38, 3757-3771 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.2.6 alizarin
-
 Serratia marcescens
3.5.2.6 apigenin
-
 Serratia marcescens
3.5.2.6 apocynin
-
 Serratia marcescens
3.5.2.6 beta-glucogallin
-
 Serratia marcescens
3.5.2.6 chrysophanol
-
 Serratia marcescens
3.5.2.6 eupalitin binding to the enzyme involves residues Leu176, Thr177, Leu196, Ile245, and Leu253 Serratia marcescens
3.5.2.6 Imipenem binding to the enzyme involves residues His72, His74, His150, His215, and Arg252 Serratia marcescens
3.5.2.6 kaempferol
-
 Serratia marcescens
3.5.2.6 L-captopril binding to the enzyme involves residues His72, His74, Asp76, His77, and His150 Serratia marcescens
3.5.2.6 luteolin binding to the enzyme involves residues His72, HIS74, Phe114, His150, and Pro216 Serratia marcescens
3.5.2.6 additional information dynamic behavior of the enzyme over simulation time with natural inhibitors using molecular dynamics studies, molecular docking, overview. The zinc ions are involved in inhibitor binding. Inhibitor binding alters the enzyme conformation. The natural inhibitors impairs the substrate binding by occupying a part of enzyme active site Serratia marcescens
3.5.2.6 rosmarinic acid binding to the enzyme involves residues Thr177, Ala178, Val179, Val218, and Ile245 Serratia marcescens
3.5.2.6 thiorphan
-
 Serratia marcescens
3.5.2.6 tiopronin
-
 Serratia marcescens
3.5.2.6 vitexin
-
 Serratia marcescens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.2.6 additional information
-
 additional information enzyme kinetics and thermodynamics Serratia marcescens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.2.6 Zn2+ a di-zinc enzyme, meropenem enzyme-bound structure with Zn2+, PDB ID 5AXO, overview. Zn1 and Zn2 at the active site pocket bind in a distance of 3.5A. The zinc ions are involved in inhibitor binding Serratia marcescens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.2.6 meropenem + H2O Serratia marcescens
-
 (4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.2.6 Serratia marcescens P52699
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.2.6 meropenem + H2O
-
 Serratia marcescens (4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
 ?
3.5.2.6 meropenem + H2O meropenem enzyme-bound structure with Zn2+, PDB ID 5AXO Serratia marcescens (4R,5S)-5-[(1S,2R)-1-carboxy-2-hydroxypropyl]-3-[[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl]-4-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.2.6 MBL
-
 Serratia marcescens
3.5.2.6 metallo-beta-lactamase
-
 Serratia marcescens

General Information

EC Number General Information Comment Organism
3.5.2.6 additional information structure-function analysis, molecular dynamics simulation and modeling, overview Serratia marcescens
3.5.2.6 physiological function metallo-beta-lactamase (MBL) is a class of enzyme that catalyzes the hydrolysis of a broad range of beta-lactam antibiotics leading to the development of drug resistance in bacteria Serratia marcescens