Recent Progress in the Understanding and Engineering of Coenzyme B12-Dependent Glycerol Dehydratase

Nasır, Abdul; Ashok, S Patil; Shim, Jeung Yeop; Park, Sunghoon; Yoo, Tae Hyeon

doi:10.3389/fbioe.2020.500867

Cited by 10 publications

(5 citation statements)

References 83 publications

(128 reference statements)

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“…Two other pArg-bearing targets were metabolic enzymes: the multifunctional 2-oxoglutarate metabolism enzyme Kgd, involved in the tricarboxylic acid cycle (Wagner et al, 2011), and the glycerol dehydratase large subunit (Msmeg_1547), which potentially contributes to the catabolic pathway involving the glycerol dehydration reaction which yields 3-hydroxypropanal in the presence of adenosylcobalamin coenzyme ( Fig. 3A; Supplemental Figure S2 ) (Liu et al, 2010; Nasir et al, 2020). pArg may thus play a role in regulating cellular metabolic pathways.…”

Section: Resultsmentioning

confidence: 99%

Identification of arginine phosphorylation inMycolicibacterium smegmatis

Ogbonna

Schmitz

2021

Preprint

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Tuberculosis is a leading cause of worldwide infectious mortality. The prevalence of multidrug-resistant Mycobacterium tuberculosis (Mtb) infections drives an urgent need to exploit new drug targets. One such target is the ATP-dependent protease ClpC1P1P2, which is strictly essential for viability. However, few proteolytic substrates of mycobacterial ClpC1P1P2 have been identified to date. Recent studies in Bacillus subtilis have shown that the orthologous ClpCP protease recognizes proteolytic substrates bearing post-translational arginine phosphorylation. Several lines of evidence suggest that ClpC1P1P2 similarly recognizes phosphoarginine-bearing proteins, but the existence of phosphoarginine modifications in mycobacteria has remained in question. Here, we confirm the presence of post-translational phosphoarginine modifications in Mycolicibacterium smegmatis (Msm), a nonpathogenic surrogate of Mtb. Using a phosphopeptide enrichment workflow coupled with shotgun phosphoproteomics, we identify arginine phosphosites on a diverse collection of targets within the Msm proteome. Physicochemical and functional characterization of targets suggest that arginine phosphorylation is applied in a sequence-independent manner as part of a proteome-wide quality control pathway. Our findings provide new evidence supporting the existence of phosphoarginine-mediated proteolysis by ClpC1P1P2 in mycobacteria and other actinobacterial species.

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Section: Resultsmentioning

confidence: 99%

Identification of arginine phosphorylation inMycolicibacterium smegmatis

Ogbonna

Schmitz

2021

Preprint

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“…However, very little is known about the synthesis of coenzyme B 12 in C. beijerinckii DSM 6423. In many cases, supplementation of vitamin B 12 was necessary to produce 1,3-PDO when a coenzyme B 12 -dependent glycerol dehydratase was used [ 47 ]. In this study, even with supplementation of vitamin B 12 (2.5 mg/L), C. beijerinckii [pMTL83251_P thlA _dhaBCET.Cpas] was unable to produce 1,3-PDO.…”

Section: Discussionmentioning

confidence: 99%

Heterologous 1,3-Propanediol Production Using Different Recombinant Clostridium beijerinckii DSM 6423 Strains

et al. 2023

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1,3-propanediol (1,3-PDO) is a valuable basic chemical, especially in the polymer industry to produce polytrimethylene terephthalate. Unfortunately, the production of 1,3-PDO mainly depends on petroleum products as precursors. Furthermore, the chemical routes have significant disadvantages, such as environmental issues. An alternative is the biobased fermentation of 1,3-PDO from cheap glycerol. Clostridium beijerinckii DSM 6423 was originally reported to produce 1,3-PDO. However, this could not be confirmed, and a genome analysis revealed the loss of an essential gene. Thus, 1,3-PDO production was genetically reinstalled. Genes for 1,3-PDO production from Clostridium pasteurianum DSM 525 and Clostridium beijerinckii DSM 15410 (formerly Clostridium diolis) were introduced into C. beijerinckii DSM 6423 to enable 1,3-PDO production from glycerol. 1,3-PDO production by recombinant C. beijerinckii strains were investigated under different growth conditions. 1,3-PDO production was only observed for C. beijerinckii [pMTL83251_Ppta-ack_1,3-PDO.diolis], which harbors the genes of C. beijerinckii DSM 15410. By buffering the growth medium, production could be increased by 74%. Furthermore, the effect of four different promoters was analyzed. The use of the constitutive thlA promoter from Clostridium acetobutylicum led to a 167% increase in 1,3-PDO production compared to the initial recombinant approach.

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“…[28] Biocatalytic dehydration of glycerol to 3-hydroxypropanal is catalyzed by glycerol dehydra-tases, which can be dependent or independent of coenzyme B 12 . [88] A vicinal diol dehydration of paromamine catalyzed by AprD4, an enzyme dependent on S-adenosyl-l-methionine (SAM), leads to the deoxygenation of paromamine at C3' and is key for the biosynthetic route to C3'-deoxy-aminoglycosides. [89] Unsaturated sugars, which can be formed by novel biocatalytic dehydration reactions, open interesting opportunities for synthesizing bioactive natural products.…”

Section: Chemsuschemmentioning

confidence: 99%

“…The water elimination from glycerol can involve the primary alcohol functionality leading to hydroxyacetone, or the secondary alcohol group leading to 3‐hydroxypropanal, which can be converted by a subsequent dehydration reaction to acrolein, by oxidation to 3‐hydroxypropionic acid, or by reduction to 1,3‐propanediol [28] . Biocatalytic dehydration of glycerol to 3‐hydroxypropanal is catalyzed by glycerol dehydratases, which can be dependent or independent of coenzyme B 12 [88] …”

Section: Selective Biocatalytic O‐defunctionalizationmentioning

confidence: 99%

Selective Biocatalytic Defunctionalization of Raw Materials

Wohlgemuth

2022

ChemSusChem

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Biobased raw materials, such as carbohydrates, amino acids, nucleotides, or lipids contain valuable functional groups with oxygen and nitrogen atoms. An abundance of many functional groups of the same type, such as primary or secondary hydroxy groups in carbohydrates, however, limits the synthetic usefulness if similar reactivities cannot be differentiated. Therefore, selective defunctionalization of highly functionalized biobased starting materials to differentially functionalized compounds can provide a sustainable access to chiral synthons, even in case of products with fewer functional groups. Selective defunctionalization reactions, without affecting other functional groups of the same type, are of fundamental interest for biocatalytic reactions. Controlled biocatalytic defunctionalizations of biobased raw materials are attractive for obtaining valuable platform chemicals and building blocks. The biocatalytic removal of functional groups, an important feature of natural metabolic pathways, can also be utilized in a systemic strategy for sustainable metabolite synthesis.

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Recent Progress in the Understanding and Engineering of Coenzyme B12-Dependent Glycerol Dehydratase

Cited by 10 publications

References 83 publications

Identification of arginine phosphorylation inMycolicibacterium smegmatis

Identification of arginine phosphorylation inMycolicibacterium smegmatis

Heterologous 1,3-Propanediol Production Using Different Recombinant Clostridium beijerinckii DSM 6423 Strains

Selective Biocatalytic Defunctionalization of Raw Materials

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