Chemistry of Amino Acids. V. Studies on α-Alkyl-α-amino Acids. IX. Mild Hydrolytic Ring Cleavage of Hydantoin Derivatives

1968 ◽  
Vol 16 (3) ◽  
pp. 444-447 ◽  
Author(s):  
KUNIO HIROI ◽  
KAZUO ACHIWA ◽  
SHUNICHI YAMADA
Keyword(s):  
Amino Acids ◽  
Ring Cleavage ◽  
Hydantoin Derivatives

ChemInform Abstract: Synthesis of ω-Nitro Acids and ω-Amino Acids by Ring Cleavage of α-Nitrocycloalkanones.

ChemInform ◽  
2010 ◽  
Vol 30 (21) ◽  
pp. no-no
Author(s):  
Roberto Ballini ◽  
Fabrizio Papa ◽  
Corrado Abate
Keyword(s):  
Amino Acids ◽  
Ring Cleavage

Cleavage Reactions of Oxazolin-5-ones Reactions with 4-Substituted-2-aryl-2-oxazolin-5-ones

1978 ◽  
Vol 33 (10) ◽  
pp. 1145-1149 ◽  
Author(s):  
Nazmi Kassab ◽  
Abdul Harhash ◽  
Said Elbahaii
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Alkaline Medium ◽  
Ring Closure ◽  
Ring Cleavage ◽  
Aminobenzoic Acids ◽  
Cleavage Reactions

Abstract The oxazoline ring in 4-arylazo-2-aryl-2-oxazolin-5-ones (1) is converted to triazolyl-carbonyl amino acids 2, 4 and 6 by the nucleophiles glycine, anthranilic and p-aminobenzoic acids, respectively. The arylidene derivatives 3 of 2-triazolyl-2-oxazolin-5-one were obtained. Triazolylbenzoxazinones 5, were obtained by the ring closure of the amino acid 4.Grignard's reagent effected ring cleavage of the oxazolinone ring in 4-cinnamylidene-2-aryl-2-oxazolin-5-ones yielding the carbinols 8, the latter cyclizes either in acidic or alkaline medium to afford either benzotropilidenes or oxazolines, respectively.

scholarly journals Cloning and Sequencing of a Novel meta-Cleavage Dioxygenase Gene Whose Product Is Involved in Degradation of γ-Hexachlorocyclohexane in Sphingomonas paucimobilis

1999 ◽  
Vol 181 (21) ◽  
pp. 6712-6719 ◽  
Author(s):  
Keisuke Miyauchi ◽  
Yugo Adachi ◽  
Yuji Nagata ◽  
Masamichi Takagi
Keyword(s):  
Amino Acids ◽  
Sole Source ◽  
Ring Cleavage ◽  
Hydroxyl Groups ◽  
Aromatic Rings ◽  
Cloning And Sequencing ◽  
Direct Demonstration ◽  
Rate Of Reaction ◽  
Dioxygenase Gene ◽  
New Type

ABSTRACT Sphingomonas (formerly Pseudomonas)paucimobilis UT26 utilizes γ-hexachlorocyclohexane (γ-HCH), a halogenated organic insecticide, as a sole source of carbon and energy. In a previous study, we showed that γ-HCH is degraded to chlorohydroquinone (CHQ) and then to hydroquinone (HQ), although the rate of reaction from CHQ to HQ was slow (K. Miyauchi, S. K. Suh, Y. Nagata, and M. Takagi, J. Bacteriol. 180:1354–1359, 1998). In this study, we cloned and characterized a gene, designated linE, which is located upstream oflinD and is directly involved in the degradation of CHQ. The LinE protein consists of 321 amino acids, and all of the amino acids which are reported to be essential for the activity ofmeta-cleavage dioxygenases are conserved in LinE.Escherichia coli overproducing LinE could convert both CHQ and HQ, producing γ-hydroxymuconic semialdehyde and maleylacetate, respectively, with consumption of O2 but could not convert catechol, which is one of the major substrates formeta-cleavage dioxygenases. LinE seems to be resistant to the acylchloride, which is the ring cleavage product of CHQ and which seems to react with water to be converted to maleylacetate. These results indicated that LinE is a novel type ofmeta-cleavage dioxygenase, designated (chloro)hydroquinone 1,2-dioxygenase, which cleaves aromatic rings with two hydroxyl groups at para positions preferably. This study represents a direct demonstration of a new type of ring cleavage pathway for aromatic compounds, the hydroquinone pathway.

scholarly journals Advances in engineering microbial biosynthesis of aromatic compounds and related compounds

2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Roman M. Dickey ◽  
Amanda M. Forti ◽  
Aditya M. Kunjapur
Keyword(s):  
Amino Acids ◽  
Aromatic Compounds ◽  
Review Article ◽  
Ring Cleavage ◽  
Future Research ◽  
Aromatic Polymer ◽  
Recent Trends ◽  
Considerable Work ◽  
Microbial Biosynthesis ◽  
Related Compounds

AbstractAromatic compounds have broad applications and have been the target of biosynthetic processes for several decades. New biomolecular engineering strategies have been applied to improve production of aromatic compounds in recent years, some of which are expected to set the stage for the next wave of innovations. Here, we will briefly complement existing reviews on microbial production of aromatic compounds by focusing on a few recent trends where considerable work has been performed in the last 5 years. The trends we highlight are pathway modularization and compartmentalization, microbial co-culturing, non-traditional host engineering, aromatic polymer feedstock utilization, engineered ring cleavage, aldehyde stabilization, and biosynthesis of non-standard amino acids. Throughout this review article, we will also touch on unmet opportunities that future research could address.

Highly Selective Ring-Cleavage of Acetals Catalyzed by Phenylboron Complexes Derived from Sulfonamides of α-Amino Acids

Synlett ◽  
1996 ◽  
Vol 1996 (01) ◽  
pp. 43-45 ◽  
Author(s):  
Motoharu Kinugasa ◽  
Toshiro Harada ◽  
Katsuhiro Fujita ◽  
Akira Oku
Keyword(s):  
Amino Acids ◽  
Ring Cleavage

scholarly journals Construction and Evaluation of a Novel Bifunctional N-Carbamylase–d-Hydantoinase Fusion Enzyme

2000 ◽  
Vol 66 (5) ◽  
pp. 2133-2138 ◽  
Author(s):  
Geun-Joong Kim ◽  
Dong-Eun Lee ◽  
Hak-Sung Kim
Keyword(s):  
Amino Acids ◽  
Fusion Protein ◽  
Bacillus Stearothermophilus ◽  
Gel Filtration ◽  
Intact Protein ◽  
E Coli ◽  
Fusion Enzyme ◽  
N Terminus ◽  
Fusion Enzymes ◽  
Hydantoin Derivatives

ABSTRACT A fully enzymatic process employing two sequential enzymes,d-hydantoinase and N-carbamylase, is a typical case requiring combined enzyme activity for the production ofd-amino acids. To test the possibility of generating a bifunctional fusion enzyme, we constructed a fusion protein via end-to-end fusion of a whole gene that encodes an intact protein at the N terminus of the d-hydantoinase. Firstly, maltose-binding protein (MBP) gene of E. coli was fused withd-hydantoinase gene from Bacillus stearothermophilus SD1, and the properties of the resulting fusion protein (MBP-HYD) were compared with those of natived-hydantoinase. Gel filtration and kinetic analyses clearly demonstrated that the typical characteristics ofd-hydantoinase are maintained even in a fusion state. Based on this result, we constructed an artificial fusion enzyme composed of the whole length of N-carbamylase (304 amino acids [aa]) from Agrobacterim radiobacter NRRL B11291 andd-hydantoinase (471 aa). The fusion enzyme (CAB-HYD) was functionally expressed with an expected molecular mass of 86 kDa and efficiently converted exogenous hydantoin derivatives to thed-amino acids. A related d-hydantoinase (HYD1) gene from Bacillus thermocatenulatus GH2 was also fused with the N-carbamylase gene at its N terminus. The resulting enzyme (CAB-HYD1) was bifunctional as expected and showed better performance than the CAB-HYD fusion enzyme. The conversion of hydantoin derivatives to corresponding amino acids by the fusion enzymes was much higher than that by the separately expressed enzymes, and comparable to that by the coexpressed enzymes. Thus, the fusion enzyme might be useful as a potential biocatalyst for the production of nonnatural amino acids.

Proton nuclear magnetic resonance studies on methylthiohydantoins, thiohydantoins, and hydantoins of amino acids

1977 ◽  
Vol 55 (5) ◽  
pp. 521-527 ◽  
Author(s):  
Tateo Suzuki ◽  
Tetsuhisa Tomioka ◽  
Katura Tuzimura
Keyword(s):  
Amino Acids ◽  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Proton Magnetic Resonance ◽  
Proton Nuclear Magnetic Resonance ◽  
Terminal Amino Acid ◽  
Magnetic Resonance Studies ◽  
Hydantoin Derivatives ◽  
Terminal Amino ◽  
Derivatives Of

Proton magnetic resonance spectra of methylthiohydantoin (3-methyl-2-thiohydantoin), thiohydantoin (2-thiohydantoin), and hydantoin derivatives of amino acids were studied in dimethyl sulfoxide-d6. Their parent amino acids could be identified by the spectra. An application to the N- and C-terminal amino acid analysis of a tripeptide was examined.

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