scholarly journals Metabolism of biphenyl. Structure and physicochemical properties of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, the meta-cleavage product from 2,3-dihydroxybiphenyl by Pseudomonas putida

1974 ◽  
Vol 143 (2) ◽  
pp. 431-434 ◽  
Author(s):  
Danilo Catelani ◽  
Antonio Colombi
Keyword(s):  
Physicochemical Properties ◽  
Pseudomonas Putida ◽  
Dienoic Acid ◽  
Cleavage Product

The structure of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid for the meta-cleavage product of 2,3-dihydroxybiphenyl by a Pseudomonas putida strain was demonstrated on the basis of its chemical and physicochemical properties and those of its derivatives.

scholarly journals Metabolism of biphenyl. 2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoate: the meta-cleavage product from 2,3-dihydroxybiphenyl by Pseudomonas putida

1973 ◽  
Vol 134 (4) ◽  
pp. 1063-1066 ◽  
Author(s):  
Danilo Catelani ◽  
Antonio Colombi ◽  
Claudia Sorlini ◽  
Vittorio Treccani
Keyword(s):  
Mass Spectrometry ◽  
Benzoic Acid ◽  
Pseudomonas Putida ◽  
Dienoic Acid ◽  
Cleavage Product ◽  
Degradative Pathway

1. 2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid was isolated and identified from washed suspensions of Pseudomonas putida incubated in the presence of 2,3-dihydroxybiphenyl. 2. Benzoic acid was isolated from reaction mixtures of crude cell-free extracts incubated with 2,3-dihydroxybiphenyl. 3. The presence in the same reaction mixtures of either 4-hydroxy-2-oxovalerate or 2-hydroxypenta-2,4-dienoate was suggested by mass spectrometry. 4. The degradative pathway of biphenyl is discussed.

scholarly journals α-Pinene metabolism by Pseudomonas putida

1977 ◽  
Vol 168 (2) ◽  
pp. 315-318 ◽  
Author(s):  
N J Tudroszen ◽  
D P Kelly ◽  
N F Millis
Keyword(s):  
Pseudomonas Putida ◽  
Dienoic Acid ◽  
Enoic Acid ◽  
Alpha Pinene

By using metabolically altered mutants and acrylate, novel putative intermediates of alpha-pinene metabolism by Pseudomonas putida PIN11 were detected. They were characterized as 3-isopropylbut-3-enoic acid and (zeta)-2-methyl-5-isopropylhexa-2,5-dienoic acid.

scholarly journals 2,3-Dihydroxybenzoate pathway in Pseudomonas putida. 1H n.m.r. study on the ring-cleavage site

1981 ◽  
Vol 194 (2) ◽  
pp. 607-610 ◽  
Author(s):  
V Andreoni ◽  
L Canonica ◽  
E Galli ◽  
C Gennari ◽  
V Treccani
Keyword(s):  
Fission Product ◽  
Pseudomonas Putida ◽  
Cleavage Site ◽  
Dienoic Acid ◽  
Ring Cleavage ◽  
Ring Fission

1. Ring cleavage of 2,3-dihydroxybenzoate by cell-free extracts of Pseudomonas putida leads to 2-hydroxy-6-oxo-(2Z,4E)-hexa-2,4-dienoic acid and CO2. 2. The 1H n.m.r. spectrum of the ring-fission product obtained in a 2H2O solution suggests that the extra-diol cleavage occurs between C-3 and C-4.

Insight into the catalytic mechanism of meta-cleavage product hydrolase BphD: a quantum mechanics/molecular mechanics study

RSC Advances ◽  
2015 ◽  
Vol 5 (82) ◽  
pp. 66591-66597 ◽  
Author(s):  
Yanwei Li ◽  
Ruiming Zhang ◽  
Likai Du ◽  
Qingzhu Zhang ◽  
Wenxing Wang
Keyword(s):  
Quantum Mechanics ◽  
Molecular Mechanics ◽  
Catalytic Mechanism ◽  
Dienoic Acid ◽  
Cleavage Product ◽  
Natural Substrate ◽  
Catabolic Pathway ◽  
Insight Into

The catalytic mechanism of BphD (the fourth enzyme of the biphenyl catabolic pathway) toward its natural substrate 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOPDA) was investigated in atomistic detail by QM/MM approach.

Preparation and characterisation of vanadium pentoxide supported rhodium catalyst

1988 ◽  
Vol 46 ◽  
pp. 946-947
Author(s):  
A. Legrouri
Keyword(s):  
Aqueous Solution ◽  
Thermal Decomposition ◽  
Physicochemical Properties ◽  
Surface Area ◽  
Vanadium Pentoxide ◽  
High Purity ◽  
Gas Adsorption ◽  
Rhodium Catalyst ◽  
Optical Methods ◽  
Reducible Oxides

The industrial importance of metal catalysts supported on reducible oxides has stimulated considerable interest during the last few years. This presentation reports on the study of the physicochemical properties of metallic rhodium supported on vanadium pentoxide (Rh/V2O5). Electron optical methods, in conjunction with other techniques, were used to characterise the catalyst before its use in the hydrogenolysis of butane; a reaction for which Rh metal is known to be among the most active catalysts.V2O5 powder was prepared by thermal decomposition of high purity ammonium metavanadate in air at 400 °C for 2 hours. Previous studies of the microstructure of this compound, by HREM, SEM and gas adsorption, showed it to be non— porous with a very low surface area of 6m2/g3. The metal loading of the catalyst used was lwt%Rh on V2Q5. It was prepared by wet impregnating the support with an aqueous solution of RhCI3.3H2O.

Studies on the Degradation of Human Fibrinogen by Plasmin and Trypsin

1966 ◽  
Vol 16 (03/04) ◽  
pp. 526-540 ◽  
Author(s):  
E. A Beck ◽  
D. P Jackson
Keyword(s):  
Physicochemical Properties ◽  
Electrophoretic Mobility ◽  
Rapid Loss ◽  
Clotting System ◽  
Human Fibrinogen ◽  
Peptide Bonds ◽  
Physico Chemical ◽  
Starch Gel ◽  
Ph Stat ◽  
Rapid Appearance

SummaryThe effects of trypsin and plasmin on the functional and physicochemical properties of purified human fibrinogen were observed at various stages of proteolysis. Concentrations of plasmin and trypsin that produced fibrinogenolysis at comparable rates as measured in a pH stat produced, at similar rates, loss of precipitability of fibrinogen by heat and ammonium sulphate and alterations in electrophoretic mobility on starch gel. Trypsin produced a more rapid loss of clottability of fibrinogen and a more rapid appearance of inhibitors of the thrombin-fibrinogen clotting system than did plasmin. Consistent differences were noted between the effects of trypsin and plasmin on the immunoelectrophoretic properties of fibrinogen during the early stages of proteolysis.These results are consistent with the hypothesis that trypsin initially reacts with the same peptide bonds of fibrinogen that are split by thrombin, but these same bonds do not appear to be split initially by plasmin. Measurement of the various functional and physico-chemical changes produced by the action of trypsin and plasmin on fibrinogen can be used to recognize various stages of proteolysis.

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