In this paper, the binding relationship between oligopeptides of edible fungi and monoamine oxidase A (MAO-A) was explored by computer simulation. The frequency of high affinity oligopeptides (F value) was calculated, and the MAO-A inhibitory peptide was screened. By simulating the hydrolysis of 27 proteins from 8 common edible fungi in China, the oligopeptides obtained by hydrolysis were docked with MAO-A to screen high affinity oligopeptides (docking fraction ≤ -120) and ultra-high affinity oligopeptides (docking fraction ≤ -160). At the same time, the F value was calculated to predict the inhibitory effect of edible fungi protein on MAO-A. A total of 430 high-affinity oligopeptides and 32 ultra-high-affinity oligopeptides were obtained by molecular docking after 27 proteins were simulated hydrolysis. Among them, the three oligopeptides with the highest docking were PQSTW (-195.952), PTSGW (-187.942) and QCQW (-180.007). In addition, the simulated hydrolyzed edible fungi all contained oligopeptides with strong inhibitory effect on MAO-A. In summary, this paper aims to screen MAO-A inhibitory peptides, provide new possibilities for high-speed screening of MAO-A inhibitory peptides, and provide a theoretical basis for exploring the potential value of edible fungi.
Research Article
Screening of Monoamine Oxidase A Inhibitory Peptides from Proteins of Edible Fungi
https://doi.org/10.21203/rs.3.rs-1436744/v1
This work is licensed under a CC BY 4.0 License
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edible fungi
monoamine oxidase A
computer simulation
molecular docking
Depression is an affective disorder with a high morbidity and disability rate, which is expected to become the highest disability rate in the world by 2030(Wen et al., 2021). In recent years, the incidence of depression has increased year by year, accounting for about 10% of the total global population(Siu et al., 2016). In China, the incidence of depression is as high as 6 .1%(Song & Jiang, 2020) and the lifetime prevalence is 3.4%(Huang et al., 2019b). However, the current number of drugs that have obvious reactions to depression patients is limited, indicating that more effective and safer drugs are needed to cure the disease or idiopathic diseases(Blackburn, 2019). It is necessary to explore the prevention and treatment of depression.
Monoamine oxidase (MAO, EC1.4.3.4) is a flavin adenine dinucleotide enzyme, which is mainly located on the outer membrane of mitochondria of tissue cells such as brain, liver and intestinal mucosa. Clinically, MAO is an important drug target for the treatment of neuropsychiatric and neurodegenerative diseases. Meanwhile, MAO inhibitors are mature drugs for the treatment of depression and Parkinson's disease(Panova et al., 2021). This enzyme has two forms, with 70% similarity, namely MAO-A and MAO-B(Cakir et al., 2016; Huang et al., 2016). MAO-A inhibitors are used to treat anxiety and depression, while MAO-B inhibitors could potentially be used as therapeutic agents in Parkinson’s and Alzheimer’s diseases(Özdemir et al., 2021).
This paper mainly studies MAO-A, one of the subtypes of MAO. MAO-A inhibitors refer to a class of drugs that selectively inhibit MAO-A and are mainly used for the treatment of depression. Their mechanism of action is that they can reversely and selectively inhibit MAO-A, prevent the degradation of 5-HT and NE in the brain, and increase the concentration of 5-HT and NE in the synaptic space of the brain, thus playing an anti-depressive role(Yamada & Yasuhara, 2004). At present, artificial synthesis and natural product screening are the mainly preparation methods of MAO-A inhibitors. The synthesis of MAO-A inhibitors is simple and straightforward, but the use of MAO-A inhibitors as antidepressants may lead to adverse reactions such as hypertensive crisis, hepatotoxicity and bleeding(Yang et al., 2020). MAO-A inhibitors of natural origin can be screened from plants, animals and microorganisms, and natural products are safer than synthetic methods (Huang et al., 2016). This is important for finding safe and effective MAO-A inhibitors and avoiding adverse reactions caused by the process of synthesis. The development of a new generation of MAO-A inhibitors is attracting the attention of scholars, aiming to provide a theoretical basis for the development of safer and more tolerant drugs for depression(Tripathi et al., 2018).
Edible fungi are not only diverse, but also their metabolites contain a variety of active ingredients, which are natural carriers for screening MAO-A inhibitors. Hu et al. separated and purificated the metabolites of Beauveria bassiana strains, and finally obtained the inhibitory substance osporin on MAO(Hu et al., 2006). Takeuchi et al. isolated and purified a MAO inhibitor harman from mushroom(Takeuchi et al., 1973). Li et al. found that the inhibitory effects of extracts from different strains or solvents on MAO were significantly different by studying Cordyceps and its related fermentation broth extracts(Li et al., 2006). Huang et al. found that (R) − 5 - Methylmellein was a selective inhibitor for MAO-A during the study on the active chemical components and antidepressant mechanism of the mycelia fermented by fungus Xylaria nigripes(Huang et al., 2019a). As a large edible filamentous fungus, edible fungi contain abundant proteins, and their amino acids are complete and balanced. Moreover, most species contain eight essential amino acids that cannot be synthesized by human body. In addition, edible fungi possess high medicinal value and play an important role in antibacterial, antiviral, antitumor, digestive aid, and adjuvant treatment of cardiovascular( Kang, 2010).
China is the world’s largest producer and consumer of edible fungi. In 2017, China’ s edible fungi production accounted for more than 70% of the world’s total production, and it is the fifth largest industry after grain, vegetables, fruits and oil. Among them, the yields of Pleurotus ostreatus, Auricularia auricula and Flammulina velutipes are at the forefront(Yang et al., 2019). The yield of edible fungi in China is huge, but it is still dominated by primary processing. The research on the medicinal value of edible fungi mainly focuses on polysaccharides and triterpenoids. The research on protein resources of edible fungi needs to be further carried out(Li et al., 2017). In this study, the protein in eight edible fungi such as Flammulina velutipes and Auricularia auricula was hydrolyzed by simulated gastrointestinal protease, and the obtained oligopeptide was docked with MAO-A. The inhibitory effect of edible fungi on MAO-A was evaluated by scoring, and the core value of edible fungi was further explored to better play the characteristics of high nutrition and high value of edible fungi, thus to improve the development potential of edible fungi as medicinal and health products.
2.1 Simulated proteolysis in the gastrointestinal tract
According to the method adopted by Yao et al. amino acid sequences of proteins from edible fungi such as Pleurotus eryngii, Cordyceps, Boletus, Tremella, Flammulina velutipes, Ganoderma lucidum, Volvariella volvacea and Auricularia auricula were obtained from NCBI database (https://www.ncbi.nlm.nih.gov/)(Yao et al., 2020a; Zhou et al., 2018). Proteins from edible fungi were simulated hydrolyzed by three gastrointestinal enzymes (pepsin, trypsin, and chymotrypsin) in BIOPEP-UWM database (https://biochemia.uwm.edu.pl/biopep-uwm/).
The formula of theoretical hydrolysis degree (TDH) is(Yao et al., 2020b):
Note: D is the total number of peptide bonds in protein, d is the number of hydrolyed peptide bonds.
2.2 Molecular docking and its capability evaluation
According to the methods adopted by Luo et al., oligopeptides containing 2–5 amino acids were screened out from the protein of edible fungi after gastrointestinal hydrolysis(Luo et al., 2020). The oligopeptides containing 2 ~ 5 amino acids were released from the protein of edible fungi after gastrointestinal hydrolysis. The oligopeptides were docked with the crystal structure of MAO-A (PDB code: 2BXR)(Amer et al., 2020) by HPEPDOCK website (http://huanglab.phys.hust.edu.cn/hpepdock/), and the oligopeptides with docking scores ≤ -120 were high affinity oligopeptides. The frequency of high-affinity oligopeptides (F value) in the protein is used to evaluate the ability of the protein in edible fungi as monoamine oxidase inhibitors (
, where F is the frequency of occurrence and N is the quantity of high-affinity oligopeptide in the protein chain, L is the length of the protein chain.)(Yao et al., 2020b).
After the docking model was obtained, the ultra-high affinity oligopeptides were screened, and PyMol(Delano, 2002) was used to deal with the receptors and ligands, and LigPlot + (Laskowski & Swindells, 2011) was used to detect the hydrogen bonds and residues of the docking results between the high affinity oligopeptide and MAO-A.
3.1 Results of simulated proteolysis in the gastrointestinal tract
In order to simulate the digestive function of gastrointestinal tract, three gastrointestinal enzymes were used to hydrolyze the protein of edible fungi, and the degree of hydrolysis (THD) was obtained (see Table 1 for details). The TDH of edible fungi protein is 29%~41%. The hydrolysates were mainly amino acids and oligopeptides (2 ≤ peptide length ≤ 5), and a few polypeptides (peptide length > 5). The results showed that among the selected proteins in edible fungi, the protein with the highest degree of hydrolysis was squalene synthase (40.95%) in Ganoderma lucidum, followed by phosphoglycerate mutase-like protein (40.62%) and MFS general substrate transporter (38.87%) in Pleurotus eryngii (See Fig. 1 for details). These proteins have a good TDH value, but it is worth mentioning that computer simulation of protein hydrolysis is to assume that all peptide bond hydrolysis in the protein chain, its degree of hydrolysis of theory and experimental results may be different. The computer simulation of hydrolysis does not consider the complexity, which may hinder the protein structure of its interaction with proteolytic enzymes. Under experimental conditions, the hydrolysis will become very complex(Szerszunowicz & Klobukowski, 2020).
3.2 Binding ability of hydrolyzed oligopeptides to MAO-A
Molecular docking, a reliable in silico approach to screen potent bioactive compounds for drug discovery and design, has been widely applied to screen enzyme inhibitors in a high-throughput way based on binding interactions between the ligand and protein(Yang et al., 2020). HPEPDOCK is a new type of web server that realizes protein-peptide blind docking by hierarchical algorithm(Zhou et al., 2018). Using molecular docking technology can quickly calculate the protein-peptide complex structure, thereby improving the screening efficiency of enzyme inhibitors.
On the HPEPDOCK, MAO-A was docked with oligopeptides released from proteins screened from edible fungi after gastrointestinal enzyme hydrolysis. Oligopeptides with docking scores ≤ -120 were high affinity oligopeptides. The F value was used to evaluate the ability of corresponding proteins to inhibit MAO-A protease. The docking scores and F value were shown in table S1. The results showed that the F value of mitochondrial vector was the largest (0.069), followed by laccase (0.064), glutamate dehydrogenase (0.059), ascorbate peroxidase (0.058), and MFS general substrate transporter (0.055). Among them, the F value of oxalate decarboxylase was 0.022, and that of phosphotyrosine protein phosphatase was the lowest, which was only 0.018. F values of other proteins ranged from 0.03 to 0.05. Oligopeptides with docking scores ≤-120 were high affinity oligopeptides. All 27 proteins hydrolysates contain high affinity oligopeptides with MAO-A. There were 430 high-affinity oligopeptides after simulated hydrolysis of 27 proteins, of which 27 oligopeptides sequences were repeated (see Fig. 2), and 32 oligopeptides are super-affinity oligopeptides with docking scores ≤ -160 (see table 2). Among the high affinity oligopeptides, the three oligopeptides with the highest docking scores were PQSTW (− 195.952), PTSGW (− 187.942) and QCQW (− 180.007), respectively. Combined with the 2D structure diagram after docking (made by LigPlot + software, version number: V.1.4.5) analysis (see Fig. 3 for details). The main interaction modes between oligopeptides and MAO-A were hydrogen bond and hydrophobic interaction. Furthermore, the affinity between oligopeptide and enzyme is different because of the different kinds, quantity, and arrangement of amino acids. It can be seen from Fig. 3a that MAO-A and PQSTW formed two pairs of hydrogen bonds between Arg424 and Trp5, Arg454 and Ser3.In addition, there were 13 non-covalent bond residues in hydrophobic contact, which were Tyr35, Trp144, Pro426, Glu458, Arg457, Asn462, Asp141, Thr439, Asp141, Arg457, Thr439, Leu461.It can be seen from Fig. 3b that MAO-A and PTDGW formed three pairs of hydrogen bonds, which were Thr204 and Gly4, Thr205 and Gly4 (Two pairs).In addition, there were 11 non-covalent bond residues with hydrophobic contact, which were Asn117, Trp116, Tyr124, Gly110, Trp128, Phe177, Phe208, Phe173, Val210, Asn125 and Tyr121.It can be seen from Fig. 3c that four pairs of hydrogen bonds were formed between MAO-A and QCQW. The hydrogen bonds were connected between Thr204 and Trp4, and between Thr205 and Trp4 (three pairs). The non-covalent bond residues in hydrophobic contact were Trp116, Tyr124, Phe173, Val201, Phe208, Phe117, Trp128, Asn125, Tyr121, Gln110, a total of 10. The remaining 29 super-affinity oligopeptides have hydrogen bonds and hydrophobic non-covalent bond residues, as detailed in table S2.
4.1 Comparison of degree of hydrolysis among edible fungi proteins
Three gastrointestinal enzymes were used to simulate the hydrolysis of 27 proteins in edible fungi. The highest degree of hydrolysis was squalene synthase (40.95%) in Ganoderma lucidum, followed by phosphoglycerate mutase-like protein (40.62%) in Pleurotus eryngii, and the other proteins see (Table 1, Fig. 1). The TDH of these proteins were similar to those of 28 plant proteins simulated by Luo et al.(Luo et al., 2020), indicating that these proteins were within the range of theoretical values, and the TDH of squalene synthase and phosphoglycerol ester mutant-like proteins were more than 40%, which were high-quality proteins derived from peptides in the gastrointestinal tract. Otherwise, squalene synthase and Phosphoglycerate mutase-like proteins are widely present in organisms, and the F values of MAO-A docking are 0.049 and 0.045, respectively. Through docking, it is found that they have good inhibitory effect on MAO-A, and high hydrolysis degree indicates that they are more conducive to the absorption and utilization of human body.
4.2 Frequency of high affinity oligopeptides
After simulated docking, F value was used to evaluate the ability of these edible fungi proteins to inhibit MAO-A. The F value was used to evaluate the ability of proteins from edible fungi to inhibit MAO-A. Among the high affinity oligopeptides, the highest F value was the mitochondrial carrier (0.069) in Pleurotus eryngii, followed by laccase (0.064) in Auricularia auricula and glutamate dehydrogenase (0.059) in Flammulina velutipes. The F value of mitochondrial carrier, laccase and glutamate dehydrogenase was higher than that of other proteins (enzymes), indicating that the inhibitory effect on MAO-A activity was relatively better than that of other proteins studied in this paper, and it was easier to obtain high affinity oligopeptides after hydrolysis. Since these three proteins are widely present in edible fungi and have high relative content, they are a major advantage for screening MAO inhibitory peptides from edible fungi.
4.3 Super high affinity oligopeptides
MAO-A inhibitors are currently used to treat refractory depression and some specific types of depression(Shulman et al., 2013). Computer simulation is helpful to reasonably explore the selection of more valuable compounds from a series of compounds with inhibitory potential, so as to screen inhibitors more reasonably, reduce the experimental cost and reduce the experimental burden.
After HPEPDOCK docking, the oligopeptides with docking scores≤-160 were called ultra-high affinity oligopeptides. There were 27 proteins involved in hydrolysis. After hydrolysis, 32 oligopeptides with ultra-high affinity were obtained by molecular docking. Among them, there were 20 oligopeptides with − 170 ≤ docking scores≤-160, which were PSTSY, PVVY, SISW, IIDAY, GPQW, PIPF, PGW, PPQH, PTATH, SGITY, TTSW, SSTAW, SAIW, GTICF, TITIL, PSW, VIW, SIPQF, PGVW, PEW. There were 9 oligopeptides with − 180 ≤ docking scores < − 170, which were ISDVW, QTGGW, PAAW, TIQVF, IIAEW, PTW, QETIY, SIVAW and IQIIH. There were 2 oligopeptides with − 190 ≤ docking scores < − 180, which were PTSGW and QCQW. And 1 oligopeptide with − 200 ≤ docking scores< -190, which was PQSTW (see table 2 for details). The results showed that the docking scores of ultra-high affinity oligopeptides was mainly between-170 and-160.These oligopeptides not only had low molecular weight and good inhibitory effect on MAO-A, but also had good bioavailability and were more likely to play a role through the intestine.
Bioactive peptides from food proteins are increasingly considered as a useful tool for improving health and preventing chronic diseases, and have attracted great attention from food manufacturers and consumers. Peptides are one of many food compounds with the ability to display biological activities in vivo. The application of bioactive peptides in functional foods, nutrients and therapeutic formulations has attracted more and more attention from the academic community(Acquah et al., 2019; Lammi et al., 2019). So far, researchers have found some antidepressant-active peptides. As Veyssiere et al.(Veyssiere et al., 2015) have shown, a peptide named spadin, consisting of 17 amino acids, works faster than classical antidepressants and does not induce side effects. Kimura et al.(Kimura et al., 2018) identified that the three peptides obtained from the hydrolysis of spinach green leaf protein showed strong anti-anxiety effects after oral administration. As a new therapeutic tool, food-derived peptides have shown outstanding advantages in finding new safe and effective antidepressants. In summary, these ultra-high affinity oligopeptides are the main target peptides for further exploring the inhibitory effect of MAO-A in vivo and in vitro.
4.4 Repeated high affinity oligopeptides
All 27 proteins hydrolysates contain high affinity oligopeptides with MAO-A. There were 430 high-affinity oligopeptides after simulated hydrolysis of 27 proteins, of which 27 oligopeptides sequences were repeated (see Fig. 2 for details). In the repeat oligopeptides, PY has 9 and repeats the most. Followed by AW, there are 7. The peptides with 4 repeats were IAF, PW, EW, VW, and SW. There were 3 repeats in ISR, and 2 repeats in the remaining 19 oligopeptides. Among the repeatable high affinity oligopeptides, there are 8 oligopeptides containing 2 amino acid sequences, namely PY, AW, CW, VW, PW, QW, SW, and EW. There are 16 kinds of oligopeptides with 3 amino acid sequences, namely VQF, IAF, VVR, ISR, PEY, ATW, TVY, QPR, VEW, SVF, PSW, PGF, VAY, CIH, ITY, and PGR. There are 3 kinds of oligopeptides containing 4 amino acids, namely QPSL, VSPR and TQSL. Thus, the same high affinity oligopeptide sequence can be obtained after different protein hydrolysis. These oligopeptides may have special effects on inhibiting MAO-A activity, which can be further tested in vitro and in vivo.
Edible fungi are a kind of large fungi with many varieties, full nutrition, delicious taste, rich in various active substances, and their potential value needs to be explored together. In this study, oligopeptides were obtained by computer simulation of protein hydrolysis. These oligopeptides were docked with the MAO-A through HPEPDOCK website. The results showed that oligopeptides obtained by hydrolysis of edible fungi protein (enzyme) had good inhibitory effect on MAO-A. Among them, the oligopeptides from the mitochondrial carrier of Pleurotus eryngii had the best inhibitory effect on MAO-A, with the maximum F value of 0.069, and the PQSTW oligopeptide obtained by hydrolysis had the highest docking scores (− 195.952). After hydrolysis of 27 proteins, 32 peptides with super high affinity were obtained by molecular docking. There were 430 high-affinity oligopeptides after simulated hydrolysis of 27 proteins, of which 27 oligopeptide sequences were repeated,. After simulated hydrolysis and docking, the proteins from common edible fungi were found to contain oligopeptides with high affinity to MAO-A. The results showed that the proteins from edible fungi were the high-quality source of MAO-A inhibitory peptides. The oligopeptides released by gastrointestinal water were closely related to the treatment of depression.
The results of this study are obtained by computer simulation, which has important scientific guiding significance for the development of functional food ingredients and drugs for the treatment of depression. In the future, in vitro and in vivo experiments will be carried out to further study its mechanism in cells or animal models. In-depth exploration and development of peptides in food as MA0 - A inhibitors will benefit the population of patients with mood disorders.
| Abbreviation | Meaning |
|---|---|
| MAO | Monoamine Oxidase |
| MAO-A | Monoamine Oxidase A |
| MAO-B | Monoamine Oxidase B |
| TDH | Theoretical Hydrolysis Degree |
• Ethics approval and consent to participate
Not applicable.
• Consent to publish
Not applicable.
• Availability of data and materials
Not applicable.
• Competing interests
The authors declare that they have no competing interests
• Funding
This research was supported by the Guangdong Basic and Applied Basic Research Foundation (2020A1515110326) and the academic Foundation Project for students of Foshan University in 2021 (xsjj202108kjb07).
• Authors' Contributions
Cansheng Ou: Wrote the original manuscript of the paper, made the molecular docking between the hydrolyzed peptide and monoamine oxidase A, and made the diagram.
Xianmin Zhou: Writing papers - reviewing and editing, screening of edible fungus proteins, sorting out tables.
Songbin Liu: Screening edible fungus proteins and simulating protein hydrolysis in gastrointestinal tract.
Huan Lu: Molecular docking was performed between the hydrolyzed peptide and monoamine oxidase A.
Ruijuan Wang: Molecular docking was performed between the hydrolyzed peptide and monoamine oxidase A.
* Corresponding author: Qiaohui Zeng: Doctor, supervised the design and implementation of the project.
All authors read and approved the final manuscript.
• Acknowledgements
Not applicable.
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Table 1 Degree of protein hydrolysis of edible fungi
|
Edible fungi |
Protein |
Hydrolysis % |
Edible fungi |
Protein |
Hydrolysis % |
|
Pleurotus mushroom |
Alpha/beta-hydrolase |
36.76 |
Ganoderma lucidum |
Squalene synthase |
40.95 |
|
Phosphotyrosine protein phosphatase |
32.51 |
PacC |
29.98 |
||
|
DigA protein |
36.99 |
CreA |
32.49 |
||
|
Phosphoglycerate mutase-like protein |
40.62 |
Cytochrome P450 reductase |
35.38 |
||
|
Mitochondrial carrier |
33.54 |
Glutathione peroxidase |
38.61 |
||
|
MFS general substrate transporter |
38.87 |
Ascorbate peroxidase |
36.28 |
||
|
Needle mushroom |
Glutamate dehydrogenase |
35.91 |
Superoxide dismutase |
38.32 |
|
|
Oxalate decarboxylase |
31.44 |
β-actin |
36.95 |
||
|
Immunomodulatory Protein Fip-fve |
31.44 |
Black fungus |
Dye-decolorizing peroxidase |
30.21 |
|
|
Straw mushroom |
Ran family protein |
38.63 |
Laccase |
31.52 |
|
|
Arf family protein |
34.47 |
Cordyceps fungi |
Ribosome-inactivating protein |
32.74 |
|
|
Ras family protein |
33.75 |
Boletes |
Lectin |
37.67 |
|
|
Rab family protein |
33.33 |
Golden tremella |
Glyceraldehyde-3-phosphate dehydrogenase |
30.43 |
|
|
Rho family protein |
33.81 |
|
|||
Table 2 Ultra-high affinity oligopeptides bound to MAO-A from edible fungus protein
|
Peptide |
Amino acids and hydrogen bond lengths between hydrogen bonds |
Noncovalent bond residues in hydrophobic contact |
|
PSTSY |
Pleurotus eryngii-Alpha/beta-hydrolase |
-166.171 |
|
PQSTW |
Pleurotus eryngii-Mitochondrial carrier |
-195.952 |
|
ISDVW |
Pleurotus eryngii-MFS general substrate transporter |
-173.514 |
|
PVVY |
Pleurotus eryngii-MFS general substrate transporter |
-163.573 |
|
SISW |
Pleurotus eryngii-MFS general substrate transporter |
-161.211 |
|
IIDAY |
Pleurotus eryngii-MFS general substrate transporter |
-165.119 |
|
GPQW |
Pleurotus eryngii-MFS general substrate transporter |
-161.160 |
|
PIPF |
Pleurotus eryngii-MFS general substrate transporter |
-161.959 |
|
QTGGW |
Flammulina velutipes-Squalene synthase |
-173.242 |
|
PAAW |
Flammulina velutipes-Squalene synthase |
-173.247 |
|
TIQVF |
Flammulina velutipes-Squalene synthase |
-175.172 |
|
IIAEW |
Flammulina velutipes-Squalene synthase |
-171.299 |
|
PTSGW |
Ganoderma Lucidum Karst-Squalene synthase |
-187.942 |
|
PGW |
Ganoderma Lucidum Karst-Squalene synthase |
-164.214 |
|
QCQW |
Ganoderma Lucidum Karst-PacC |
-180.007 |
|
PTW |
Ganoderma Lucidum Karst-PacC |
-170.110 |
|
PPQH |
Ganoderma Lucidum Karst-PacC |
-161.765 |
|
PTATH |
Ganoderma Lucidum Karst-CreA |
-160.186 |
|
SGITY |
Ganoderma Lucidum Karst-Cytochrome P450 reductase |
-161.143 |
|
TTSW |
Ganoderma Lucidum Karst-Cytochrome P450 reductase |
-163.129 |
|
QETIY |
Ganoderma Lucidum Karst-Cytochrome P450 reductase |
-174.550 |
|
SSTAW |
Ganoderma Lucidum Karst-Ascorbate peroxidase |
-163.446 |
|
SAIW |
Ganoderma Lucidum Karst-Superoxide dismutase |
-162.982 |
|
GTICF |
Volvariella volvacea-Ran family protein |
-161.729 |
|
TITIL |
Volvariella volvacea-Arf family protein |
-162.496 |
|
SIVAW |
Volvariella volvacea-Arf family protein |
-177.602 |
|
PSW |
Volvariella volvacea-Arf family protein, Auricularia auricula-Dye-decolorizing peroxidase |
-166.293 |
|
IQIIH |
Volvariella volvacea-Arf family protein |
-172.927 |
|
VIW |
Volvariella volvacea-Rho family protein |
-160.293 |
|
SIPQF |
Auricularia auricula-Dye-decolorizing peroxidase |
-166.991 |
|
PGVW |
Auricularia auricula-Laccase |
-169.860 |
|
PEW |
Cordyceps-Ribosome-inactivating protein |
-160.266 |
Note: ( ) Internally expressed hydrogen bond length
