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B6db references: 31132312

type Journal Article
authors Devi S, Tarique KF, Ali MF, Abdul Rehman SAX, Gourinath S
title Identification and characterisation of Helicobacter pylori O-acetylserine-dependent cystathionine β-synthase, a distinct member of the PLP-II family
journal Mol Microbiol
Activity 2.5.1.134
Family 2.5.1.134
sel selected
ui 31132312
year (2019)
volume 112
number 2
pages 718-739
 
keywords Helicobacter pylori ; Cystathionine β-synthase; Hydrogen sulfide; O-acetylserine sulfhydrylase; pyridoxal 5-phosphate; reverse transsulfuration pathway
abstract O-acetylserine sulfhydrylase (OASS) and cystathionine β-synthase (CBS) are members of the PLP-II family, and involved in L-cysteine production. OASS produces L-cysteine via a de novo pathway while CBS participates in the reverse transsulfuration pathway. O-acetylserine-dependent CBS (OCBS) was previously identified as a new member of the PLP-II family, which are predominantly seen in bacteria. The bacterium Helicobacter pylori possesses only one OASS (hp0107) gene and we showed that the protein coded by this gene actually functions as an OCBS and utilizes L-homocysteine and O-acetylserine (OAS) to produce cystathionine. HpOCBS did not show CBS activity with the substrate L-serine and required OAS exclusively. The HpOCBS structure in complex with methionine showed a closed-cleft state, explaining the initial mode of substrate binding. Sequence and structural analyses showed differences between the active sites of OCBS and CBS, and explain their different substrate preferences. We identified three hydrophobic residues near the active site of OCBS, corresponding to one serine and two tyrosine residues in CBSs. Mutational studies were performed on HpOCBS and Saccharomyces cerevisiae CBS. A ScCBS double mutant (Y158F/Y226V) did not display activity with L-serine, indicating indispensability of these polar residues for selecting substrate L-serine, however did show activity with OAS.
last changed 2020/02/17 10:27

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