General Information of the Molecule (ID: Mol01135)
Name
Virginiamycin B lyase (VGBB) ,Staphylococcus cohnii
Synonyms
Streptogramin B lyase
    Click to Show/Hide
Molecule Type
Protein
Gene Name
vgbB
Sequence
MNFYLEEFNLSIPDSGPYGITSSEDGKVWFTQHKANKISSLDQSGRIKEFEVPTPDAKVM
CLIVSSLGDIWFTENGANKIGKLSKKGGFTEYPLPQPDSGPYGITEGLNGDIWFTQLNGD
RIGKLTADGTIYEYDLPNKGSYPAFITLGSDNALWFTENQNNSIGRITNTGKLEEYPLPT
NAAAPVGITSGNDGALWFVEIMGNKIGRITTTGEISEYDIPTPNARPHAITAGKNSEIWF
TEWGANQIGRITNDKTIQEYQLQTENAEPHGITFGKDGSVWFALKCKIGKLNLNE
    Click to Show/Hide
Function
Inactivates the type B streptogramin antibiotics by linearizing the lactone ring at the ester linkage, generating a free phenylglycine carboxylate and converting the threonyl moiety into 2-amino-butenoic acid.
    Click to Show/Hide
Uniprot ID
O87275_9STAP
        Click to Show/Hide the Complete Species Lineage
Kingdom: N.A.
Phylum: Firmicutes
Class: Bacilli
Order: Bacillales
Family: Staphylococcaceae
Genus: Staphylococcus
Species: Staphylococcus cohnii
Type(s) of Resistant Mechanism of This Molecule
  DISM: Drug Inactivation by Structure Modification
Drug Resistance Data Categorized by Drug
Investigative Drug(s)
1 drug(s) in total
Click to Show/Hide the Full List of Drugs
Quinupristin/Dalfopristin
Click to Show/Hide
Drug Resistance Data Categorized by Their Corresponding Mechanisms
       Drug Inactivation by Structure Modification (DISM) Click to Show/Hide
Disease Class: Staphylococcus aureus infection [1]
Resistant Disease Staphylococcus aureus infection [ICD-11: 1B54.0]
Resistant Drug Quinupristin/Dalfopristin
Molecule Alteration Expression
Inherence
Experimental Note Identified from the Human Clinical Data
In Vitro Model Escherichia coli BL21(DE3) 469008
Experiment for
Molecule Alteration
PCR amplification and sequence alignments assay
Experiment for
Drug Resistance
Spectrophotometric and fluorometric assay
Mechanism Description Virginiamycin B lyase (Vgb) inactivates the quinupristin component of Synercid by lactone ring opening and the enzyme promotes this reaction by intramolecular Beta-elimination without the involvement of a water molecule. Replacement of the conserved active site residues His228, Glu268, or His270 with alanine reduces or abolishes S. cohnii Vgb activity. Residue Lys285 in S. cohnii Vgb is spatially equivalent to the S. aureus Vgb active site residue Glu284.
References
Ref 1 Crystal structure and mechanism of the Staphylococcus cohnii virginiamycin B lyase (Vgb). Biochemistry. 2008 Apr 8;47(14):4257-65. doi: 10.1021/bi7015266. Epub 2008 Mar 15.

If you find any error in data or bug in web service, please kindly report it to Dr. Sun and Dr. Zhang.