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 |
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 |
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 |
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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.2.6 | Serratia marcescens | P52699 | - |
- |
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 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.2.6 | MBL | - |
Serratia marcescens |
3.5.2.6 | metallo-beta-lactamase | - |
Serratia marcescens |
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 |