Phospholipase D as a catalyst: application in phospholipid synthesis, molecular structure and protein engineering

Area of Science:

• Biochemistry
• Enzymology

Background:

• Phospholipase D (PLD) enzymes are crucial for synthesizing phospholipids (PLs) via transphosphatidylation.
• PLD-catalyzed synthesis has evolved from plant to microbial sources, particularly actinomycetes.
• PLDs belong to a superfamily sharing conserved catalytic motifs (HxKxxxxD/HKD) and a common two-step reaction mechanism involving a phosphatidyl-enzyme intermediate.

Purpose of the Study:

• To review recent advancements in Phospholipase D enzymology.
• To highlight the synthesis of bioactive phospholipids using PLD.
• To explore substrate recognition, binding mechanisms, specificity alteration, and thermostability improvements.

Main Methods:

• Review of existing literature on PLD-catalyzed synthesis.
• Analysis of PLD superfamily structure and catalytic mechanisms.
• Incorporation of recent research findings and author's own results.

Main Results:

• PLD engineering efforts focus on enhancing activity, stability, and specificity.
• Understanding of PLD substrate binding and recognition mechanisms has deepened.
• Advances in modifying PLD for tailored phospholipid production are discussed.

Conclusions:

• Phospholipase D is a versatile enzyme with significant potential for synthesizing functional phospholipids.
• Ongoing research continues to expand our knowledge of PLD's catalytic capabilities and applications.
• Engineering PLD holds promise for developing novel bioactive lipids and improving enzymatic synthesis processes.