The GxSxG motif of Arabidopsis monoacylglycerol lipase (MAGL6 and MAGL8) is essential for their enzyme activities

Kim, Ryeo Jin; Suh, Mi Chung

doi:10.1007/s13765-016-0232-1

Cited by 5 publications

(1 citation statement)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The motif of CaPLA1 is also located in the same position and has the same sequence as in AtDSEL ( Figure 2 A,C). It has been reported that the two Gly residues of the GXSXG motif are also essential for the lipase activity [ 24 ]. The lipase activities of MGLs in Arabidopsis thaliana were completely lost when the researchers applied the following mutagenesis to the lipases: GXAXG, GXSXS, or SXSXG [ 24 ], which demonstrates that Gly to the Ser mutant as well as Ser to the Ala mutant causes severe deactivation of the lipases.…”

Section: Resultsmentioning

confidence: 99%

Crystal Structures of the Plant Phospholipase A1 Proteins Reveal a Unique Dimerization Domain

et al. 2022

View full text Add to dashboard Cite

Phospholipase is an enzyme that hydrolyzes various phospholipid substrates at specific ester bonds and plays important roles such as membrane remodeling, as digestive enzymes, and the regulation of cellular mechanism. Phospholipase proteins are divided into following the four major groups according to the ester bonds they cleave off: phospholipase A1 (PLA1), phospholipase A2 (PLA2), phospholipase C (PLC), and phospholipase D (PLD). Among the four phospholipase groups, PLA1 has been less studied than the other phospholipases. Here, we report the first molecular structures of plant PLA1s: AtDSEL and CaPLA1 derived from Arabidopsis thaliana and Capsicum annuum, respectively. AtDSEL and CaPLA1 are novel PLA1s in that they form homodimers since PLAs are generally in the form of a monomer. The dimerization domain at the C-terminal of the AtDSEL and CaPLA1 makes hydrophobic interactions between each monomer, respectively. The C-terminal domain is also present in PLA1s of other plants, but not in PLAs of mammals and fungi. An activity assay of AtDSEL toward various lipid substrates demonstrates that AtDSEL is specialized for the cleavage of sn-1 acyl chains. This report reveals a new domain that exists only in plant PLA1s and suggests that the domain is essential for homodimerization.

show abstract

Section: Resultsmentioning

confidence: 99%

Crystal Structures of the Plant Phospholipase A1 Proteins Reveal a Unique Dimerization Domain

et al. 2022

View full text Add to dashboard Cite

show abstract

Microbial production of butyl butyrate, a flavor and fragrance compound

Noh

Lee

Jang

2019

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Metabolic engineering of Clostridium acetobutylicum for the production of butyl butyrate

Noh

Woo

Lee

et al. 2018

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Butyl butyrate is widely used as a fragrance additive for foods and beverages. The first step in the currently used process is the production of precursors, including butanol and butyrate, from petroleum using chemical catalysts, followed by the conversion of precursors to butyl butyrate by immobilized lipase. In this work, we engineered Clostridium acetobutylicum for the selective, one-step production of butyl butyrate from glucose. C. acetobutylicum ATCC 824, possessing a strong carbon flux that yields butanol and butyryl-CoA, was selected as a host and was engineered by introducing alcohol acyltransferases (AATs) from Fragaria x ananassa (strawberry) or Malus sp. (apple). Batch culture of the engineered C. acetobutylicum strain CaSAAT expressing the strawberry SAAT gene produced 50.07 mg/L of butyl butyrate with a selectivity of 84.8% of total esters produced. Also, the engineered C. acetobutylicum strain CaAAAT expressing the apple AAAT gene produced 40.60 mg/L of butyl butyrate with a selectivity of 87.4%. This study demonstrated the feasibility of the one-step fermentation of butyl butyrate from glucose in the engineered C. acetobutylicum, as a proof of concept.

show abstract

The GxSxG motif of Arabidopsis monoacylglycerol lipase (MAGL6 and MAGL8) is essential for their enzyme activities

Cited by 5 publications

References 26 publications

Crystal Structures of the Plant Phospholipase A1 Proteins Reveal a Unique Dimerization Domain

Crystal Structures of the Plant Phospholipase A1 Proteins Reveal a Unique Dimerization Domain

Microbial production of butyl butyrate, a flavor and fragrance compound

Metabolic engineering of Clostridium acetobutylicum for the production of butyl butyrate

Contact Info

Product

Resources

About