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Chemical Structure| 54-47-7 Chemical Structure| 54-47-7
Chemical Structure| 54-47-7

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Pyridoxal phosphate is the active form of vitamin B6, acts as an inhibitor of reverse transcriptases, and is used for the treatment of tardive dyskinesia.

Synonyms: Pyridoxal 5′-phosphate; Pyridoxyl phosphate; MC-1

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Lara, Darwin Daniel ; Zeng, Bryan Tianzuo ; Hai, Yang ;

Abstract: β-Methylamino acids (β-MAAs) enhance the bioactivity of natural products and possess intrinsic pharmacological properties as free amino acids. While the biosynthetic capacity for this class of noncanonical amino acids has been established in certain bacterial lineages such as Gammaproteobacteria and Actinomycetes, other bacterial phyla remain largely unexplored. Here we report the genome-mining guided discovery of a novel biosynthetic gene cluster capable of producing β-methylarginine, from the phylum Planctomycetes. We provide both in vivo and in vitro evidence that Planctomycetes employ a transaminase (PlaA) and a methyltransferase (PlaB) to synthesize this β-MAA. Unlike previously described β-methylarginine biosynthetic pathways, PlaA and PlaB function as a self-sufficient enzyme cascade that operates without the need for additional keto acid and amino acid partners. These findings expand the catalytic repertoire for β-MAAs biosynthesis and establish Planctomycetes as a new source of secondary metabolites discovery.

Keywords: β-methyl-arginine ; PLP-dependent enzyme ; genome mining

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Humberto De Vitto ; Kafi K. J. Belfon ; Nandini Sharma ; Sarah Toay ; Jan Abendroth ; David. M. Dranow , et al.

Abstract: Thiamin and its phosphate derivatives are ubiquitous molecules involved as essential cofactors in many cellular processes. The de novo biosynthesis of thiamin employs the parallel synthesis of 4-methyl-5-(2-hydroxyethyl)thiazole (THZ-P) and 4-amino-2-methyl-5(diphosphooxymethyl) pyrimidine (HMP) pyrophosphate (HMP-PP), which are coupled to generate thiamin phosphate. Most organisms that can biosynthesize thiamin employ a kinase (HMPK or ThiD) to generate HMP-PP. In nearly all cases, this enzyme is bifunctional and can also salvage free HMP, producing HMP-P, the monophosphate precursor of HMP-PP. Here we present high-resolution crystal structures of an HMPK from Acinetobacter baumannii (AbHMPK), both unliganded and with pyridoxal 5-phosphate (PLP) noncovalently bound. Despite the similarity between HMPK and pyridoxal kinase enzymes, our kinetics analysis indicates that AbHMPK accepts HMP exclusively as a substrate and cannot turn over , , or nor does it display phosphatase activity. PLP does, however, act as a weak inhibitor of AbHMPK with an IC50 of 768 μM. Surprisingly, unlike other HMPKs, AbHMPK catalyzes only the phosphorylation of HMP and does not generate the diphosphate HMP-PP. This suggests that an additional kinase is present in A. baumannii, or an alternative mechanism is in operation to complete the biosynthesis of thiamin.

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Alternative Products

Product Details of Pyridoxal phosphate

CAS No. :54-47-7
Formula : C8H10NO6P
M.W : 247.14
SMILES Code : CC1=C(O)C(C=O)=C(COP(O)(O)=O)C=N1
Synonyms :
Pyridoxal 5′-phosphate; Pyridoxyl phosphate; MC-1
MDL No. :MFCD00006333
InChI Key :NGVDGCNFYWLIFO-UHFFFAOYSA-N
Pubchem ID :1051

Safety of Pyridoxal phosphate

GHS Pictogram:
Signal Word:Warning
Hazard Statements:H302-H315-H319-H335
Precautionary Statements:P261-P305+P351+P338

Application In Synthesis of Pyridoxal phosphate

* All experimental methods are cited from the reference, please refer to the original source for details. We do not guarantee the accuracy of the content in the reference.

  • Downstream synthetic route of [ 54-47-7 ]
 

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