Phospholipase D mechanism using Streptomyces PLD.
Phospholipase D (PLD) plays various roles in important biological processes and physiological functions, including cell signaling. Streptomyces PLDs show significant sequence similarity and belong to the PLD superfamily containing two catalytic HKD motifs. These PLDs have conserved catalytic regions and are among the smallest PLD enzymes. Therefore, Streptomyces PLDs are thought to be suitable models for studying the reaction mechanism among PLDs from other sources. Furthermore, Streptomyces PLDs present advantages related to their broad substrate specificity and ease of enzyme preparation. Moreover, the tertiary structure of PLD has been elucidated only for PLD from Streptomyces sp. PMF. This article presents a review of recently reported studies of the mechanism of the catalytic reaction, substrate recognition, substrate specificity and stability of Streptomyces PLD using various protein engineering methods and surface plasmon resonance analysis.
Uesugi
Yoshiko
Y
Research Institute for Biological Sciences (RIBS), Kaga-gun, Okayama, Japan.
Hatanaka
Tadashi
T
D000595:Amino Acid Sequence; D000818:Animals; D055162:Biocatalysis; D004795:Enzyme Stability; D006801:Humans; D008969:Molecular Sequence Data; D010739:Phospholipase D / Q000737:chemistry / Q000378:metabolism*; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity
D010739:Phospholipase D