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Literature summary for 3.5.2.6 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
Search for more literature for 3.5.2.6

Inhibitors

Inhibitors Comment Organism Structure
alizarin
-
 Serratia marcescens
apigenin
-
 Serratia marcescens
apocynin
-
 Serratia marcescens
beta-glucogallin
-
 Serratia marcescens
chrysophanol
-
 Serratia marcescens
eupalitin binding to the enzyme involves residues Leu176, Thr177, Leu196, Ile245, and Leu253 Serratia marcescens
Imipenem binding to the enzyme involves residues His72, His74, His150, His215, and Arg252 Serratia marcescens
kaempferol
-
 Serratia marcescens
L-captopril binding to the enzyme involves residues His72, His74, Asp76, His77, and His150 Serratia marcescens
luteolin binding to the enzyme involves residues His72, HIS74, Phe114, His150, and Pro216 Serratia marcescens
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
rosmarinic acid binding to the enzyme involves residues Thr177, Ala178, Val179, Val218, and Ile245 Serratia marcescens
thiorphan
-
 Serratia marcescens
tiopronin
-
 Serratia marcescens
vitexin
-
 Serratia marcescens

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Serratia marcescens P52699
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
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

Synonyms Comment Organism
MBL
-
 Serratia marcescens
metallo-beta-lactamase
-
 Serratia marcescens

General Information

General Information Comment Organism
additional information structure-function analysis, molecular dynamics simulation and modeling, overview Serratia marcescens
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