Abstract: 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.

Abstract: Provided are a transaminase mutant and a method for producing a chiral amine using the same. An amino acid sequence of the transaminase mutant is an amino acid sequence obtained by mutation occurred in an amino acid sequence as shown in SEQ ID NO: 1, and the mutation includes at least one of the following mutation sites: position 3, position 5, position 8, position 25, position 32, position 45, position 56, position 59, position 60, position 84, position 86, position 164, position 176, position 178, position 180, position 187, position 197, position 206, position 207, position 242, position 245, position 319 and position 324.

Abstract: The invention provides a transaminase mutant and application thereof, wherein the amino acid sequence of the transaminase mutant is formed after mutation of the amino acid sequence as shown in SEQ ID NO: 1, and mutated amino acid sites comprise T7C+S47C sites. The transaminase mutant having the mutation sites can be further prepared into an immobilized enzyme through an immobilization technology, the immobilized enzyme has relatively high activity and high stability, can be recycled for multiple times, and is applicable to continuous flow reaction in a packed bed.

Abstract: Disclosed are a monooxygenase mutant and use thereof. An amino acid sequence of a monooxygenase mutant is an amino acid sequence obtained by mutating an amino acid sequence as shown in SEQ ID NO: 1. Mutation includes at least one of the following mutation sites: site 49, site 60, site 61, site 144, site 145, site 146, site 147, site 167, site 169, site 189, site 246, site 247, site 280, site 284, site 285, site 286, site 287, site 328, site 330, site 332, site 382, site 427, site 428, site 429, site 430, site 431, site 432, site 433, site 434, site 435, site 436, site 438, site 441, site 493, site 494, site 508, site 509, site 510, site 511, site 512, and site 513 sites and the like. The monooxygenase mutant has the advantage of greatly improved stereoselectivity, and the enzyme activity is also improved correspondingly.

Abstract: 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.

Abstract: A ketoreductase mutant and use thereof are provided. The amino acid sequence of the ketoreductase mutant is an amino acid sequence obtained by mutation of the amino acid sequence shown in SEQ ID NO: 1, wherein the mutation at least comprises one of the following mutation sites: position 6, position 94, position 96, position 117, position 144, position 156, position 193, position 205, position 224, position 176, position 85 and position 108; alternatively, the amino acid sequence of the ketoreductase mutant has a mutation site in a mutated amino acid sequence and an amino acid sequence having 80% or more homology with the mutated amino acid sequence.

Abstract: 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.

Abstract: Provided are a proline hydroxylase and uses thereof. The proline hydroxylase comprises having the amino acid sequence of SEQ ID NO: 2 with the exception of a mutation of one or more amino acids; wherein the mutation of one or more amino acids must comprises E27K, and the mutation of one or more amino acids selected from the group consisting of: H14R, L16N, T25R, F26L, E27K, D30S, S33N, E34N, E34G, E34L, E34S, E34D, Y35W, Y35K, S37W, S37F, S37E, S37N, S37T, S37C, W40F, K41E, D54G, H55Q, S57L, I58T, I58Y, I58A, I58R, I58V, I58S, I58C, K86P, T91A, F95Y, C97Y, I98V, K106V, K106T, K106Q, F111S, K112E, K112R, S154A, K162E, L166M, I118F, I118V, I118R, H119R, H119F, I120V, K123D, K123N, K123Q, K123S, K123I, K123T, T130N, D134G, V135K, N165H, D173G, K209R, I223V and S225A, and having proline hydroxylase activity.

Abstract: Provided are a proline hydroxylase and uses thereof. The proline hydroxylase comprises (a) a protein having the amino acid sequence as shown in SEQ ID NO: 2; (b) a protein having an amino acid sequence of SEQ HD NO: 2 with a mutation of one or more amino acids and having a proline hydroxylase activity; or (c) a protein retaining the mutation of one or more amino acids as in (b), and having the proline hydroxylase activity and having at least 78% homology with the amino acid sequence of the protein in (b). Protein having the amino acid sequence as shown in SEQ HD NO: 2 and mutants obtained by genetically engineering have higher catalytic specificity or significantly increased catalytic activity when compared to proline hydroxylases in prior art.

Abstract: The invention provides a transaminase mutant and application thereof, wherein the amino acid sequence of the transaminase mutant is formed after mutation of the amino acid sequence as shown in SEQ ID NO: 1, and mutated amino acid sites comprise T7C+S47C sites. The transaminase mutant having the mutation sites can be further prepared into an immobilized enzyme through an immobilization technology, the immobilized enzyme has relatively high activity and high stability, can be recycled for multiple times, and is applicable to continuous flow reaction in a packed bed.

Abstract: 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.

Abstract: A ketoreductase mutant and use thereof are provided. The amino acid sequence of the ketoreductase mutant is an amino acid sequence obtained by mutation of the amino acid sequence shown in SEQ ID NO: 1, wherein the mutation at least comprises one of the following mutation sites: position 6, position 94, position 96, position 117, position 144, position 156, position 193, position 205, position 224, position 176, position 85 and position 108; alternatively, the amino acid sequence of the ketoreductase mutant has a mutation site in a mutated amino acid sequence and an amino acid sequence having 80% or more homology with the mutated amino acid sequence.

Abstract: A transaminase mutant and use hereof, the amino acid sequence of the transaminase mutant is an amino acid sequence in which the amino acid sequence as represented by SEQ ID NO: 1 is mutated, the mutated amino acid position being one or more selected from among F89, K193, P243, V234, I262, Q280, V379, R416, A417 and C418. The enzymatic activity and/or stability of the transaminase mutant is improved.

Abstract: Provided are a proline hydroxylase and uses thereof. The proline hydroxylase comprises (a) a protein having the amino acid sequence as shown in SEQ ID NO: 2; (b) a protein having an amino acid sequence of SEQ HD NO: 2 with a mutation of one or more amino acids and having a proline hydroxylase activity; or (c) a protein retaining the mutation of one or more amino acids as in (b), and having the proline hydroxylase activity and having at least 78% homology with the amino acid sequence of the protein in (b). Protein having the amino acid sequence as shown in SEQ HD NO: 2 and mutants obtained by genetically engineering have higher catalytic specificity or significantly increased catalytic activity when compared to proline hydroxylases in prior art.

Abstract: A polymer containing a carboxyl group, a preparation method and an application thereof, a supported catalyst and a preparation method thereof and preparation methods of penem antibiotic intermediate are disclosed. The polymer has high rigidity and hardness, thus the mechanical properties of the polymer is effectively improved. Meanwhile, in the polymer, the carboxyl group is used as a main functional group, and is used as a carrier to prepare, by means of a coordination reaction between the carboxyl group and a heavy metal, a supported metal catalyst which has better connection stability between the metal and the polymer. The above two factors can improve the stability of the supported metal catalyst, such that the catalyst can be recycled without losing the catalytic activity. Meanwhile, loss of a heavy metal active ingredient and production cost can be reduced.

Abstract: A method for preparing nilotinib includes the following steps: performing an aminocarbonylation reaction on a compound A and 3-(4-methyl-1H-imidazole-1-yl)-5-(trifluoromethyl) aniline to obtain an amination product; and performing deprotection treatment of an R group on the amination product to obtain the nilotinib, wherein the compound A has a structure shown in formula I, and in formula I, an R group is selected from benzyl, —COCF3, —CHO or —CO2R?, where an R? group is C1˜C10 alkyl, C1˜C3 alkoxy ethyl or C7˜C19 aralkyl.

Abstract: A method for preparing nilotinib includes the following steps: performing an aminocarbonylation reaction on a compound A and 3-(4-methyl-1H-imidazole-1-yl)-5-(trifluoromethyl) aniline to obtain an amination product; and performing deprotection treatment of an R group on the amination product to obtain the nilotinib, wherein the compound A has a structure shown in formula I, and in formula I, an R group is selected from benzyl, —COCF3, —CHO or —CO2R?, where an R? group is C1˜C10 alkyl, C1˜C3 alkoxy ethyl or C7˜C19 aralkyl.

Abstract: A polymer containing a carboxyl group, a preparation method and an application thereof, a supported catalyst and a preparation method thereof and preparation methods of penem antibiotic intermediate are disclosed. The polymer has high rigidity and hardness, thus the mechanical properties of the polymer is effectively improved. Meanwhile, in the polymer, the carboxyl group is used as a main functional group, and is used as a carrier to prepare, by means of a coordination reaction between the carboxyl group and a heavy metal, a supported metal catalyst which has better connection stability between the metal and the polymer. The above two factors can improve the stability of the supported metal catalyst, such that the catalyst can be recycled without losing the catalytic activity. Meanwhile, loss of a heavy metal active ingredient and production cost can be reduced.