(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Firmicutes: NE > Bacilli: NE > Lactobacillales: NE > Lactobacillaceae: NE > Lactobacillus: NE > Lactobacillus rhamnosus: NE
No mutation 4 structures(e.g. : 4N5H, 4N5I, 4OUK... more)(less) 4N5H: Crystal structure of esterase B from Lactobacillus rhamnosis (HN001), 4N5I: Crystal Structure of a C8-C4 Sn3 Inhibited Esterase B from Lactobacillus Rhamnosis, 4OUK: Crystal structure of C6-C4 SN3 inhibited esterase B from Lactobacillus rhamnosis, 4PO3: Crystal structure of C4-C4 SN3 tributyrin phosphonate inhibited esterase B from Lactobacillus rhamnosis No kinetic
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MADEEAMLAKVQASWAQTAARDKARYADERVPEDVHWETEYRYEQSADPQ QTLNLYYPAKRRNATMPTVIDIHGGGWFYGDRNLNRNYCRYLASQGYAVM GMGYRLLPDVDLRGQIQDIFASLRWLSHFGPQRGFDLDHVLLTGDSAGGH LASLVACIQQSAELQELFGVSRVNFNFTLVALVCPVAEPSKLPEAAGDMS DMAAFYLDKLSGGDQALVDHLNFSQVVKGLDLPPFMLIGGQNDSFYLQSQ ALLKVFDANHVTYTTKLWPASAGPHLKHVFNVQHWEWPESIETNLEMLRT FDALSKQQDQAEENEFE
References
Title: Role of N-Terminal Extensional Long alpha-Helix in the Arylesterase from Lacticaseibacillus rhamnosus GG on Catalysis and Stability Li BC, Guo T, Li X, Hou X, Ding GB Ref: Catalysts, 13:441, 2023 : PubMed
In the alpha/beta hydrolases superfamily, the extra module modulated enzymatic activity, substrate specificity, and stability. The functional role of N-terminal extensional long alpha-helix (Ala2-Glu29, designated as NEL-helix) acting as the extra module in the arylesterase LggEst from Lacticaseibacillus rhamnosus GG had been systemically investigated by deletion mutagenesis, biochemical characterization, and biophysical methods. The deletion of the NEL-helix did not change the overall structure of this arylesterase. The deletion of the NEL-helix led to the shifting of optimal pH into the acidity and the loss of thermophilic activity. The deletion of the NEL-helix produced a 10.6-fold drop in catalytic activity towards the best substrate pNPC10. NEL-Helix was crucial for the thermostability, chemical resistance, and organic solvents tolerance. The deletion of the NEL-helix did not change the overall rigidity of enzyme structure and only reduced the local rigidity of the active site. Sodium deoxycholate might partially replenish the loss of activity caused by the deletion of the NEL-helix. Our research further enriched the functional role of the extra module on catalysis and stability in the alpha/beta hydrolase fold superfamily.
Free fatty acids (FFAs) and esters derived from FFAs are important flavour compounds in cheese. Evidence is provided that esterases of lactic acid bacteria (LAB) catalyse not only hydrolysis of milk fat glycerides to release FFAs, but also synthesis of esters from glycerides and alcohols via a transferase reaction. The esterases of LAB prefer di- and monoglycerides for both hydrolysis and ester synthesis and are, in fact, alcohol acyltransferases that use both water (hydrolysis) and alcohol (alcoholysis) as acyl acceptors. Therefore, esterases of LAB can impact on both the lipolytic and ester flavours of cheese. The impact of esterases of LAB on cheese flavour can be controlled by manipulating the amount of the esterase, by regulating alcohol availability and/or by increasing the mono- and diglyceride composition of milk fat. In addition, esterification may play a role in ester synthesis in hard cheeses (e.g. Italian type) where water activity is low.
Lactobacillus rhamnosus (LMS2-1) (HN001) Esterase BLRH_10360
