(-)-3-Dehydroshikimic acid - CAS 2922-42-1
Category:
Main Product
Product Name:
(-)-3-Dehydroshikimic acid
Catalog Number:
2922-42-1
Synonyms:
DHS; 5-DEHYDROSHIKIMIC ACID; (-)-3-DEHYDROSHIKIMIC ACID; 4,5-DIHYDROXY-3-OXO TRANS; (4(S)-TRANS)-4,5-DIHYDROXY-3-OXO-1-CYCLOHEXENE-1-CARBOXYLIC ACID; DHS, 5-Dehydroshikimic Acid, 1-Cyclohexene-1-carboxylic Acid, 4,5-Dihydroxy-3-oxo trans
CAS Number:
2922-42-1
Molecular Weight:
172.14
Molecular Formula:
C7H8O5
Quantity:
Data not available, please inquire.
COA:
Inquire
MSDS:
Inquire
Canonical SMILES:
C1C(C(C(=O)C=C1C(=O)O)O)O
InChI:
InChI=1S/C7H8O5/c8-4-1-3(7(11)12)2-5(9)6(4)10/h1,5-6,9-10H,2H2,(H,11,12)/t5-,6-/m1/s1
InChIKey:
SLWWJZMPHJJOPH-PHDIDXHHSA-N
Chemical Structure
CAS 2922-42-1 (-)-3-Dehydroshikimic acid

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Reference Reading


1.Crystal structures of type I dehydroquinate dehydratase in complex with quinate and shikimate suggest a novel mechanism of Schiff base formation.
Light SH1, Antanasijevic A, Krishna SN, Caffrey M, Anderson WF, Lavie A. Biochemistry. 2014 Feb 11;53(5):872-80. doi: 10.1021/bi4015506. Epub 2014 Jan 31.
A component of the shikimate biosynthetic pathway, dehydroquinate dehydratase (DHQD) catalyzes the dehydration of 3-dehydroquniate (DHQ) to 3-dehydroshikimate. In the type I DHQD reaction mechanism a lysine forms a Schiff base intermediate with DHQ. The Schiff base acts as an electron sink to facilitate the catalytic dehydration. To address the mechanism of Schiff base formation, we determined structures of the Salmonella enterica wild-type DHQD in complex with the substrate analogue quinate and the product analogue shikimate. In addition, we determined the structure of the K170M mutant (Lys170 being the Schiff base forming residue) in complex with quinate. Combined with nuclear magnetic resonance and isothermal titration calorimetry data that revealed altered binding of the analogue to the K170M mutant, these structures suggest a model of Schiff base formation characterized by the dynamic interplay of opposing forces acting on either side of the substrate.
2.Expression of a bacterial 3-dehydroshikimate dehydratase reduces lignin content and improves biomass saccharification efficiency.
Eudes A1,2, Sathitsuksanoh N1,3, Baidoo EE1,2, George A1,3, Liang Y1,2, Yang F1,2, Singh S1,3, Keasling JD1,2,4, Simmons BA1,3, Loqué D1,2. Plant Biotechnol J. 2015 Dec;13(9):1241-1250. doi: 10.1111/pbi.12310. Epub 2015 Jan 13.
Lignin confers recalcitrance to plant biomass used as feedstocks in agro-processing industries or as source of renewable sugars for the production of bioproducts. The metabolic steps for the synthesis of lignin building blocks belong to the shikimate and phenylpropanoid pathways. Genetic engineering efforts to reduce lignin content typically employ gene knockout or gene silencing techniques to constitutively repress one of these metabolic pathways. Recently, new strategies have emerged offering better spatiotemporal control of lignin deposition, including the expression of enzymes that interfere with the normal process for cell wall lignification. In this study, we report that expression of a 3-dehydroshikimate dehydratase (QsuB from Corynebacterium glutamicum) reduces lignin deposition in Arabidopsis cell walls. QsuB was targeted to the plastids to convert 3-dehydroshikimate - an intermediate of the shikimate pathway - into protocatechuate.
3.Mechanism-Based Trapping of the Quinonoid Intermediate by Using the K276R Mutant of PLP-Dependent 3-Aminobenzoate Synthase PctV in the Biosynthesis of Pactamycin.
Hirayama A1, Miyanaga A2, Kudo F3, Eguchi T4. Chembiochem. 2015 Nov;16(17):2484-90. doi: 10.1002/cbic.201500426. Epub 2015 Oct 23.
Mutational analysis of the pyridoxal 5'-phosphate (PLP)-dependent enzyme PctV was carried out to elucidate the multi-step reaction mechanism for the formation of 3-aminobenzoate (3-ABA) from 3-dehydroshikimate (3-DSA). Introduction of mutation K276R led to the accumulation of a quinonoid intermediate with an absorption maximum at 580 nm after the reaction of pyridoxamine 5'-phosphate (PMP) with 3-DSA. The chemical structure of this intermediate was supported by X-ray crystallographic analysis of the complex formed between the K276R mutant and the quinonoid intermediate. These results clearly show that a quinonoid intermediate is involved in the formation of 3-ABA. They also indicate that Lys276 (in the active site of PctV) plays multiple roles, including acid/base catalysis during the dehydration reaction of the quinonoid intermediate.
4.Structure-based virtual screening as a tool for the identification of novel inhibitors against Mycobacterium tuberculosis 3-dehydroquinate dehydratase.
Petersen GO1, Saxena S2, Renuka J2, Soni V2, Yogeeswari P2, Santos DS3, Bizarro CV4, Sriram D5. J Mol Graph Model. 2015 Jul;60:124-31. doi: 10.1016/j.jmgm.2015.05.001. Epub 2015 May 11.
3-Dehydroquinate dehydratase (DHQase), the third enzyme of the shikimate pathway, catalyzes the reversible reaction of 3-dehydroquinate into 3-dehydroshikimate. The aim of the present study was to identify new drug-like molecules as inhibitors for Mycobacterium tuberculosis DHQase employing structure-based pharmacophore modeling technique using an in house database consisting of about 2500 small molecules. Further the pharmacophore models were validated using enrichment calculations, and finally three models were employed for high-throughput virtual screening and docking to identify novel small molecules as DHQase inhibitors. Five compounds were identified, out of which, one molecule (Lead 1) showed 58% inhibition at 50μ M concentration in the Mtb DHQase assay. Chemical derivatives of the Lead 1 when tested evolved top two hits with IC50s of 17.1 and 31.5 μM as well as MIC values of 25 and 6.25 μg/mL respectively and no cytotoxicity up to 100 μM concentration.