更新于：2024-11-01

CYB5A

更新于：2024-11-01

基本信息

别名

CYB5、CYB5A、Cytochrome b5

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简介

Cytochrome b5 is a membrane-bound hemoprotein functioning as an electron carrier for several membrane-bound oxygenases.

关联

100 项与 CYB5A 相关的临床结果

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100 项与 CYB5A 相关的转化医学

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0 项与 CYB5A 相关的专利（医药）

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2,196

项与 CYB5A 相关的文献（医药）

2024-10-01·Metabolic Engineering

Not all cytochrome b5s are created equal: how a specific CytB5 boosts forskolin biosynthesis in Saccharomyces cerevisiae

Article

作者: Kampranis, Sotirios ; Møller, Birger Lindberg ; Pateraki, Irini ; Stærk, Dan ; Luo, Dan ; Forman, Victor

Cytochrome B5s, or CytB5s, are small heme-binding proteins, ubiquitous across all kingdoms of life that serve mainly as electron donors to enzymes engaged in oxidative reactions. They often function as redox partners of the cytochrome P450s (CYPs), a superfamily of enzymes participating in multiple biochemical processes. In plants, CYPs catalyze key reactions in the biosynthesis of plant specialized metabolites with their activity dependent on electron donation often from cytochrome P450 oxidoreductases (CPRs or PORs). In eukaryotic microsomal CYPs, CytB5s frequently participate in the electron transfer process although their exact role remains understudied, especially in plant systems. In this study, we assess the role of CytB5s in the heterologous biotechnological production of plant specialized metabolites in yeast. For this, we used as a case-study the biosynthesis of forskolin - a bioactive diterpenoid produced exclusively from the plant Coleus forskohlii. The complete biosynthetic pathway for forskolin is known and includes three CYP enzymes. We reconstructed the entire forskolin pathway in the yeast Saccharomyces cerevisiae, and upon co-expression of the three CytB5s - identified in C. forskohlii transcriptomes - alleviation of a CYP-related bottleneck step was noticed only when a specific CytB5, CfCytB5A, was used. Co-expression of CfCytB5A in yeast, in combination with forskolin pathway engineering, resulted in forskolin production at titers of 1.81 g/L in a bioreactor. Our findings demonstrate that CytB5s not only play an important role in plant specialized metabolism but also, they can interact with precision with specific CYPs, indicating that the properties of CytB5s are far from understood. Moreover, our work highlights how CytB5s may act as indispensable components in the sustainable microbial production of plant metabolites, when their biosynthetic pathways involve CYP enzymes.

2024-09-01·Journal of Fish Biology

Proteomic analysis of exosomes derived from fatty hepatocytes of grass carp

Article

作者: Sun, Jian ; Zhang, Yuru ; Yang, Lulu ; Cao, Xianglin ; Jia, Shenzong ; Lu, Ronghua ; Xu, Xinxin

AbstractExosomes participate in intercellular communication by carrying proteins, messenger RNA, microRNAs, and non‐coding RNA. Fatty liver is a common phenomenon in farmed fish, but there has been little study of fatty hepatocytes‐derived exosomes. Here, we successfully isolated exosomes from hepatocytes of grass carp, named Exos (hepatocytes‐derived exosomes) and OA‐Exos (fatty hepatocytes‐derived exosomes), from which 617 differentially expressed proteins were identified using liquid chromatography tandem mass spectrometry. Of these, 320 proteins were promoted and 297 proteins were restrained, which were gathered in biological processes and cellular components (cellular processes, cells, and intracellular structures). The results of kyoto encyclopedia of genes and genomes (KEGG) analysis revealed that the differential expression proteins were gathered in “carbohydrate transport and metabolism”, “translation, ribosomal structure and biogenesis”, “posttranslational modification, protein turnover, chaperones”, and “intracellular trafficking, secretion, and vesicular transport”. In addition, five differentially expressed exosomal proteins were further confirmed by parallel reaction monitoring, including 2‐phospho‐D‐glycerate hydrolyase, cytochrome b5, fatty acid‐binding protein domain‐containing protein, metallothionein, and malate dehydrogenas, which were downregulated. These findings provided evidence that exosomes derived from fatty hepatocytes of grass carp may be biomarkers for the early diagnosis, treatment, and prevention of fatty liver in fishery development.

2024-07-02·The Plant Cell

Cytochrome b5 diversity in green lineages preceded the evolution of syringyl lignin biosynthesis

Article

作者: Liu, Chang-Jun ; Zhao, Yunjun ; Zeng, Qing-Yin ; Zhao, Xianhai

AbstractLignin production marked a milestone in vascular plant evolution, and the emergence of syringyl (S) lignin is lineage specific. S-lignin biosynthesis in angiosperms, mediated by ferulate 5-hydroxylase (F5H, CYP84A1), has been considered a recent evolutionary event. F5H uniquely requires the cytochrome b5 protein CB5D as an obligatory redox partner for catalysis. However, it remains unclear how CB5D functionality originated and whether it coevolved with F5H. We reveal here the ancient evolution of CB5D-type function supporting F5H-catalyzed S-lignin biosynthesis. CB5D emerged in charophyte algae, the closest relatives of land plants, and is conserved and proliferated in embryophytes, especially in angiosperms, suggesting functional diversification of the CB5 family before terrestrialization. A sequence motif containing acidic amino residues in Helix 5 of the CB5 heme-binding domain contributes to the retention of CB5D function in land plants but not in algae. Notably, CB5s in the S-lignin–producing lycophyte Selaginella lack these residues, resulting in no CB5D-type function. An independently evolved S-lignin biosynthetic F5H (CYP788A1) in Selaginella relies on NADPH-dependent cytochrome P450 reductase as sole redox partner, distinct from angiosperms. These results suggest that angiosperm F5Hs coopted the ancient CB5D, forming a modern cytochrome P450 monooxygenase system for aromatic ring meta-hydroxylation, enabling the reemergence of S-lignin biosynthesis in angiosperms.