Chinese Bulletin of Botany ›› 2024, Vol. 59 ›› Issue (2): 204-216.DOI: 10.11983/CBB23109 cstr: 32102.14.CBB23109
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Heping Wang1,2, Zhen Sun2, Yuchen Liu2, Yanlong Su2, Jinyu Du2,5, Yan Zhao5, Hongbo Zhao1, Zhaoming Wang6, Feng Yuan6, Yaling Liu6, Zhenying Wu2,3,4, Feng He2,3,4,*(), Chunxiang Fu2,3,4,*(
)
Received:
2023-08-09
Accepted:
2023-12-19
Online:
2024-03-10
Published:
2024-03-10
Contact:
* E-mail: Heping Wang, Zhen Sun, Yuchen Liu, Yanlong Su, Jinyu Du, Yan Zhao, Hongbo Zhao, Zhaoming Wang, Feng Yuan, Yaling Liu, Zhenying Wu, Feng He, Chunxiang Fu. Sequence Identification and Functional Analysis of Cinnamyl Alcohol Dehydrogenase Gene from Agropyron mongolicum[J]. Chinese Bulletin of Botany, 2024, 59(2): 204-216.
Sequence ID | Number of amino acid | Molecular weight (Da) | Theoretical pI | Instability index | Aliphatic index | Grand average of hydropathicity |
---|---|---|---|---|---|---|
PB.70108.1 | 360 | 38591.48 | 5.87 | 23.05 | 90.33 | 0.025 |
PB.82665.1 | 354 | 38437.86 | 6.66 | 24.94 | 84.75 | -0.098 |
PB.80567.1 | 358 | 38685.52 | 6.60 | 30.79 | 89.27 | 0.012 |
PB.80906.1 | 355 | 38256.89 | 5.68 | 31.84 | 88.42 | 0.037 |
PB.62308.1 | 269 | 28625.35 | 6.31 | 31.41 | 92.45 | 0.166 |
PB.17482.1 | 344 | 36802.76 | 5.86 | 31.22 | 86.13 | 0.103 |
PB.52032.1 | 373 | 38747.35 | 6.53 | 24.05 | 91.58 | 0.136 |
PB.47633.2 | 421 | 44353.00 | 6.42 | 31.04 | 84.28 | 0.092 |
PB.55683.1 | 421 | 44338.97 | 6.42 | 29.60 | 83.80 | 0.088 |
PB.83678.1 | 356 | 37359.82 | 5.40 | 25.49 | 92.25 | 0.146 |
PB.84043.1 | 356 | 37036.55 | 5.84 | 26.83 | 93.88 | 0.211 |
PB.84184.1 | 356 | 37019.73 | 6.08 | 23.61 | 92.25 | 0.195 |
Table 1 Analysis of physicochemical properties of AmCAD proteins from Agropyron mongolicum
Sequence ID | Number of amino acid | Molecular weight (Da) | Theoretical pI | Instability index | Aliphatic index | Grand average of hydropathicity |
---|---|---|---|---|---|---|
PB.70108.1 | 360 | 38591.48 | 5.87 | 23.05 | 90.33 | 0.025 |
PB.82665.1 | 354 | 38437.86 | 6.66 | 24.94 | 84.75 | -0.098 |
PB.80567.1 | 358 | 38685.52 | 6.60 | 30.79 | 89.27 | 0.012 |
PB.80906.1 | 355 | 38256.89 | 5.68 | 31.84 | 88.42 | 0.037 |
PB.62308.1 | 269 | 28625.35 | 6.31 | 31.41 | 92.45 | 0.166 |
PB.17482.1 | 344 | 36802.76 | 5.86 | 31.22 | 86.13 | 0.103 |
PB.52032.1 | 373 | 38747.35 | 6.53 | 24.05 | 91.58 | 0.136 |
PB.47633.2 | 421 | 44353.00 | 6.42 | 31.04 | 84.28 | 0.092 |
PB.55683.1 | 421 | 44338.97 | 6.42 | 29.60 | 83.80 | 0.088 |
PB.83678.1 | 356 | 37359.82 | 5.40 | 25.49 | 92.25 | 0.146 |
PB.84043.1 | 356 | 37036.55 | 5.84 | 26.83 | 93.88 | 0.211 |
PB.84184.1 | 356 | 37019.73 | 6.08 | 23.61 | 92.25 | 0.195 |
Figure 2 Phylogenetic tree of CADs in Agropyron mongolicum, Arabidopsis thaliana, Oryza sativa, and Brachypodium distachyon The red pentagram represents the functional CAD protein of A. mongolicum that may be involved in lignin synthesis; the pink dots represent the CAD protein of B. distachyon; the green dots represent the CAD protein of A. thaliana; and the blue dots represent the CAD protein of O. sativa.
Figure 3 Amplification of Agropyron mongolicum AmCAD and protein structure analysis (A) AmCAD gel map (M: DNA ladder; 1: Amplification sequence); (B) Comparison of CAD amino acid sequences among A. mongolicum and other species (the residue forming the substrate binding pocket is marked with a triangle (▲)); (C) Three-dimensional protein structure model and substrate binding pocket of AmCAD (the nucleotide binding and catalytic domains of the bottom subunit are colored yellow and blue, respectively, the corresponding compounds in the upper subunit are colored green and dark blue, while the zinc ions are indicated by gray spheres)
Figure 4 Heterologous expression (A) and enzymatic properties of AmCAD recombinant protein in Escherichia coli at different temperatures (B) and pH (C) 1: Marker; 2: Supernatant; 3: Precipitant; 4: Effluent; 5: Purified protein
Substract | Km (μmol·L-1) | Vmax (μmol·L-1·s-1) | Kcat (·s−1) | Kcat/Km (μmol·L-1·s-1) |
---|---|---|---|---|
Coniferylaldehyde | 8.94±0.15 | 6.87±0.008 | 441.37±0.53 | 49.35±0.90 |
Sinapaldehyde | 10.35±2.14 | 7.18±0.43 | 461.51±27.94 | 45.26±6.69 |
p-coumaraldehyde | 35.35±3.74 | 15.21±1.60 | 977.60±102.97 | 27.65±0.01 |
Table 2 Enzyme kinetic characteristics of different substrates catalyzed by recombinant AmCAD
Substract | Km (μmol·L-1) | Vmax (μmol·L-1·s-1) | Kcat (·s−1) | Kcat/Km (μmol·L-1·s-1) |
---|---|---|---|---|
Coniferylaldehyde | 8.94±0.15 | 6.87±0.008 | 441.37±0.53 | 49.35±0.90 |
Sinapaldehyde | 10.35±2.14 | 7.18±0.43 | 461.51±27.94 | 45.26±6.69 |
p-coumaraldehyde | 35.35±3.74 | 15.21±1.60 | 977.60±102.97 | 27.65±0.01 |
Figure 6 Expression analysis of AmCAD gene under drought stress at different time points and mannitol concentrations (A) 75 mmol∙L-1 mannitol treatment; (B) 150 mmol∙L-1 mannitol treatment; (C) 250 mmol∙L-1 mannitol treatment. * P<0.05; ** P<0.01; *** P<0.001
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