Current Advances on Structure-Function Relationships of Pyridoxal 5′-Phosphate-Dependent Enzymes
Pyridoxal 5′-phosphate (PLP) functions as a coenzyme in many enzymatic processes, including decarboxylation, deamination, transamination, racemization, and others. Enzymes, requiring PLP, are commonly termed PLP-dependent enzymes, and they are widely involved in crucial cellular metabolic pathways i...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2019-03-01
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| Series: | Frontiers in Molecular Biosciences |
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| Online Access: | https://www.frontiersin.org/article/10.3389/fmolb.2019.00004/full |
| _version_ | 1818229477730156544 |
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| author | Jing Liang Qian Han Yang Tan Haizhen Ding Jianyong Li |
| author_facet | Jing Liang Qian Han Yang Tan Haizhen Ding Jianyong Li |
| author_sort | Jing Liang |
| collection | DOAJ |
| description | Pyridoxal 5′-phosphate (PLP) functions as a coenzyme in many enzymatic processes, including decarboxylation, deamination, transamination, racemization, and others. Enzymes, requiring PLP, are commonly termed PLP-dependent enzymes, and they are widely involved in crucial cellular metabolic pathways in most of (if not all) living organisms. The chemical mechanisms for PLP-mediated reactions have been well elaborated and accepted with an emphasis on the pure chemical steps, but how the chemical steps are processed by enzymes, especially by functions of active site residues, are not fully elucidated. Furthermore, the specific mechanism of an enzyme in relation to the one for a similar class of enzymes seems scarcely described or discussed. This discussion aims to link the specific mechanism described for the individual enzyme to the same types of enzymes from different species with aminotransferases, decarboxylases, racemase, aldolase, cystathionine β-synthase, aromatic phenylacetaldehyde synthase, et al. as models. The structural factors that contribute to the reaction mechanisms, particularly active site residues critical for dictating the reaction specificity, are summarized in this review. |
| first_indexed | 2024-12-12T10:19:14Z |
| format | Article |
| id | doaj.art-bd3ece015d414979a6e6b26d90440748 |
| institution | Directory Open Access Journal |
| issn | 2296-889X |
| language | English |
| last_indexed | 2024-12-12T10:19:14Z |
| publishDate | 2019-03-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Molecular Biosciences |
| spelling | doaj.art-bd3ece015d414979a6e6b26d904407482022-12-22T00:27:36ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2019-03-01610.3389/fmolb.2019.00004387990Current Advances on Structure-Function Relationships of Pyridoxal 5′-Phosphate-Dependent EnzymesJing Liang0Qian Han1Yang Tan2Haizhen Ding3Jianyong Li4Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, VA, United StatesLaboratory of Tropical Veterinary Medicine and Vector Biology, Hainan Key Laboratory of Sustainable Utilization of Tropical Bioresources, Institute of Agriculture and Forestry, Hainan University, Haikou, ChinaInstitute of Synthetic Biology, Shenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen, ChinaDepartment of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, VA, United StatesDepartment of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, VA, United StatesPyridoxal 5′-phosphate (PLP) functions as a coenzyme in many enzymatic processes, including decarboxylation, deamination, transamination, racemization, and others. Enzymes, requiring PLP, are commonly termed PLP-dependent enzymes, and they are widely involved in crucial cellular metabolic pathways in most of (if not all) living organisms. The chemical mechanisms for PLP-mediated reactions have been well elaborated and accepted with an emphasis on the pure chemical steps, but how the chemical steps are processed by enzymes, especially by functions of active site residues, are not fully elucidated. Furthermore, the specific mechanism of an enzyme in relation to the one for a similar class of enzymes seems scarcely described or discussed. This discussion aims to link the specific mechanism described for the individual enzyme to the same types of enzymes from different species with aminotransferases, decarboxylases, racemase, aldolase, cystathionine β-synthase, aromatic phenylacetaldehyde synthase, et al. as models. The structural factors that contribute to the reaction mechanisms, particularly active site residues critical for dictating the reaction specificity, are summarized in this review.https://www.frontiersin.org/article/10.3389/fmolb.2019.00004/fullpyridoxal 5′-phosphatestructure-function relationshipreaction mechanismamino acid residuesreaction specificity |
| spellingShingle | Jing Liang Qian Han Yang Tan Haizhen Ding Jianyong Li Current Advances on Structure-Function Relationships of Pyridoxal 5′-Phosphate-Dependent Enzymes Frontiers in Molecular Biosciences pyridoxal 5′-phosphate structure-function relationship reaction mechanism amino acid residues reaction specificity |
| title | Current Advances on Structure-Function Relationships of Pyridoxal 5′-Phosphate-Dependent Enzymes |
| title_full | Current Advances on Structure-Function Relationships of Pyridoxal 5′-Phosphate-Dependent Enzymes |
| title_fullStr | Current Advances on Structure-Function Relationships of Pyridoxal 5′-Phosphate-Dependent Enzymes |
| title_full_unstemmed | Current Advances on Structure-Function Relationships of Pyridoxal 5′-Phosphate-Dependent Enzymes |
| title_short | Current Advances on Structure-Function Relationships of Pyridoxal 5′-Phosphate-Dependent Enzymes |
| title_sort | current advances on structure function relationships of pyridoxal 5 phosphate dependent enzymes |
| topic | pyridoxal 5′-phosphate structure-function relationship reaction mechanism amino acid residues reaction specificity |
| url | https://www.frontiersin.org/article/10.3389/fmolb.2019.00004/full |
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