TY - JOUR
T1 - Biochemical Investigation of 3-Sulfopropionaldehyde Reductase HpfD
AU - An, Junwei
AU - Wei, Yifeng
AU - Liu, Jiayi
AU - Lui Ang, Ee
AU - Zhao, Huimin
AU - Zhang, Yan
N1 - Funding Information:
This work was supported by the National Key R&D Program of China 2020YFA0907900 (Y. Zhang), 31870049 (Y. Zhang), the Agency for Science, Technology and Research of Singapore Visiting Investigator Program Grant 1535j00137 (H.Z.) and Advanced Manufacturing and Engineering Programmatic Grant A18 A9b0060 (Y.W., E.L.A. and H.Z.).
Publisher Copyright:
© 2021 Wiley-VCH GmbH
PY - 2021/10/1
Y1 - 2021/10/1
N2 - Sulfoquinovose is the polar headgroup of plant sulfolipids and is a globally abundant organosulfur compound, and its degradation by bacteria is an important component of the sulfur cycle. Sulfoquinovose degradation by certain bacteria, including Escherichia coli, produces dihydroxypropanesulfonate (DHPS), which is further converted by anaerobic bacteria into 3-hydroxypropanesulfonate (3-HPS), through the catalytic action of DHPS dehydratase (a member of the glycyl radical enzyme family), and sulfopropionaldehyde reductase HpfD (a member of the metal-dependent alcohol dehydrogenase family). Here we report biochemical investigation of Hungatella hathewayi HpfD. In addition to 3-HPS, HpfD also displayed high catalytic activities for NAD+-dependent oxidation of 4-hydroxybutanesulfonate (4-HBS) and γ-hydroxybutyrate (GHB). The highest activity was obtained with Fe2+ or Mn2+ as the divalent metal cofactor. Bioinformatics studies suggest that, in addition to DHPS degradation, 3-HPS and γ-aminobutyrate (GABA) degradations also involve HpfD homologs.
AB - Sulfoquinovose is the polar headgroup of plant sulfolipids and is a globally abundant organosulfur compound, and its degradation by bacteria is an important component of the sulfur cycle. Sulfoquinovose degradation by certain bacteria, including Escherichia coli, produces dihydroxypropanesulfonate (DHPS), which is further converted by anaerobic bacteria into 3-hydroxypropanesulfonate (3-HPS), through the catalytic action of DHPS dehydratase (a member of the glycyl radical enzyme family), and sulfopropionaldehyde reductase HpfD (a member of the metal-dependent alcohol dehydrogenase family). Here we report biochemical investigation of Hungatella hathewayi HpfD. In addition to 3-HPS, HpfD also displayed high catalytic activities for NAD+-dependent oxidation of 4-hydroxybutanesulfonate (4-HBS) and γ-hydroxybutyrate (GHB). The highest activity was obtained with Fe2+ or Mn2+ as the divalent metal cofactor. Bioinformatics studies suggest that, in addition to DHPS degradation, 3-HPS and γ-aminobutyrate (GABA) degradations also involve HpfD homologs.
KW - alcohol dehydrogenase
KW - hydroxybutyrate
KW - sulfoglycolysis
KW - sulfonate
KW - sulfoquinovose
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U2 - 10.1002/cbic.202100316
DO - 10.1002/cbic.202100316
M3 - Article
C2 - 34410031
AN - SCOPUS:85114195098
SN - 1439-4227
VL - 22
SP - 2862
EP - 2866
JO - ChemBioChem
JF - ChemBioChem
IS - 19
ER -