Asymchem Laboratories (tianjin) Co., Ltd.

Asymchem Life Science (tianjin) Co., Ltd

Lemon Inc.

Asymchem Life Science Co., Ltd.

Rui Li

Jiangping Lu

Na Zhang

Kejian Zhang

Xuecheng Jiao

Hao Hong

Yu Xuan Zhang

Gage James

Yiming Yang

Bin Liu

Zheng Chen

Yuan Gao

Hongyu Xiong

Han Wang

Yiqi Feng

James Gage

Xiangyu Zeng

Qingyi Lu

Yu Zhang

Yihan Yang

Tianyu Zhang

An amino acid sequence of the monooxygenase mutant is obtained by mutation of an amino acid sequence shown in SEQ ID NO: 1, and the mutation at least includes one of the following mutation sites: 45-th site, 95-th site, 106-th site, 108-th site, 114-th site, 186-th site, 190-th site, 191-th site, 249-th site, 257-th site, 393-th site, 436-th site, 499-th site, 500-th site, 501-th site, 503-th site, 504-th site, 559-th site, and 560-th site.

Monooxygenase mutant and use thereof

The present application relates to the technical field of genetic engineering, and provides a monooxygenase mutant, a preparation method and application thereof. The monooxygenase mutant has any one of the amino acid sequences shown in (I) and (II): (I) an amino acid sequence having at least 80% identity with the amino acid sequence shown in SEQ ID NO. 1; and (II) an amino acid sequence obtained by modifying, substituting, deleting, or adding one or several amino acids to the amino acids at 23 to 508 positions of the amino acid sequence shown in SEQ ID NO. 1, the substituting referring to a substitution of 1 to 34 amino acids, wherein the mutant has the activity of monooxygenase.

Monooxygenase mutant, preparation method and application thereof

There are provided methods, devices, and computer program products for similarity determination. In a method, first and second access data are obtained for a first and a second group of users who access a first and a second website, respectively. A first and a second jump path are generated for the first and second groups of users based on the first and second access data, respectively. The first and second jump paths describe access history for the first and second groups of users among webpages in the first and second websites, respectively. A similarity is determined between the first and second websites based on the first and second jump paths. Here, access data are used for similarity determination and unvisited webpages are not considered in the similarity determination. Therefore, the computation workload may be lowered, and the noise caused by the unvisited webpages may be reduced.

Website similarity determination

Provided is an amino acid dehydrogenase mutant. The amino acid sequence of the mutant is obtained by mutating the amino acid sequence shown in SEQ ID NO:1. The mutation includes at least one of the following mutation sites: 64th, 94th, 133rd, 137th, 148th, 168th, 173rd, 183 rd, 191st, 207th, 229th, 248th, 255th and 282nd sites; or the amino acid sequence of the amino acid dehydrogenase mutant is an amino acid sequence having the mutation sites in the mutated amino acid sequence and having a 80% or more homology with the mutated amino acid sequence. The mutant enzyme activity is more than 50 times higher than that of wild amino acid dehydrogenase, and the enzyme specificity is also correspondingly improved.

Amino acid dehydrogenase mutant and use thereof

Disclosed are transaminase mutants and use thereof. The amino acid sequence of the transaminase mutant is obtained by the mutation of the amino acid sequence as shown in SEQ ID NO: 1, and the mutation at least comprises one of the following mutation sites: the 19-th site, the 41-th site, the 43-th site, the 72-th site, the 76-th site, the 92-th site, the 107-th site, the 125-th site, the 132-th site, the 226-th site, the 292-th site, the 295-th site, the 308-th site, and the 332-th site; and the 19-th site is mutated into a serine, the 41-th site is mutated into a serine, the 43-th site is mutated into an asparagine, a glycine in the 72-th site is mutated into a leucine, etc.; or the amino acid sequence of the transaminase mutant has the mutation sites in the mutanted amino acid sequence, and has more than 80% homology to the mutanted amino acid sequence.

Transaminase mutant and use thereof

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Tianjin, China

Rui Li