Metabolism of mandelic acid by Neurospora crassa

1977 ◽  
Vol 23 (10) ◽  
pp. 1496-1499 ◽  
Author(s):  
D. N. Ramakrishna Rao ◽  
C. S. Vaidyanathan
Keyword(s):  
Aspergillus Niger ◽  
Benzoic Acid ◽  
Formic Acid ◽  
Neurospora Crassa ◽  
Mandelic Acid ◽  
Protocatechuic Acid ◽  
Hydroxybenzoic Acid ◽  
Bacterial Systems

Preliminary studies on the metabolism of mandelic acid by Neurospora crassa reveal the operation of a pathway for its degradation which involves benzoyl formic acid, benzaldehyde, benzoic acid, 4-hydroxybenzoic acid, and protocatechuic acid as the intermediates. This pathway is different from that followed by bacterial systems and is the same as that observed in Aspergillus niger.

Biosynthese von p-Hydroxybenzoesäure und anderer Benzoesäuren in höheren Pflanzen

1964 ◽  
Vol 19 (5) ◽  
pp. 398-405 ◽  
Author(s):  
M. H. Zenk ◽  
G. Müller
Keyword(s):  
Benzoic Acid ◽  
Protocatechuic Acid ◽  
Higher Plants ◽  
Side Chain ◽  
Hydroxybenzoic Acid ◽  
Benzoic Acids ◽  
Coumaric Acid ◽  
Cinnamic Acids ◽  
Feeding Experiments ◽  
Catalpa Ovata

Feeding experiments with glucose- (2-14C), phenylalanine- (3-14C), tyrosine- (3-14C) and p-coumaric acid- (3-14C) showed that the latter three substances are incorporated in good yields into p-hydroxybenzoic acid in leaves of Catalpa ovata. Kinetic experiments showed that p-hydroxybenzoic acid is formed from phenylalanine via p-coumaric acid and the subsequent β-oxidation of the side chain. p-Hydroxybenzoic acid can also be synthetised by hydroxylation of benzoic acid, but this does not seem to be the biosynthetic route in Catalpa.Phenylalanine- (3-14C) is also incorporated into benzoic acid, protocatechuic acid, and vanillic acid by different plants; the radioactivity of the β-C atom of the amino acid was found in each case to be located in the carboxyl group of the C6 — C1 acid. This suggests that in higher plants the benzoic acids are formed from the corresponding cinnamic acids via β-oxidation.

m-Hydroxybenzoic acid 4-hydroxylase from Aspergillus niger

1969 ◽  
Vol 47 (8) ◽  
pp. 825-827 ◽  
Author(s):  
R. Premkumar ◽  
P. V. Subba Rao ◽  
N. S. Sreeleela ◽  
C. S. Vaidyanathan
Keyword(s):  
Aspergillus Niger ◽  
Molecular Oxygen ◽  
Protocatechuic Acid ◽  
Hydroxybenzoic Acid ◽  
Dihydroxybenzoic Acid

m-Hydroxybenzoic acid 4-hydroxylase was isolated and partially purified from Aspergillus niger grown in presence of m-hydroxybenzoic acid. The enzyme catalyzed the stoichiometric formation of protocatechuic acid (3,4-dihydroxybenzoic acid) from m-hydroxybenzoic acid with the consumption of NADPH and molecular oxygen. The reaction proceeded best at pH 7.2 and showed a requirement for FAD.

DEGRADATION OF AROMATIC AMINO ACIDS BY FUNGI: I. FATE OF L-PHENYLALANINE IN SCHIZOPHYLLUM COMMUNE

1967 ◽  
Vol 45 (11) ◽  
pp. 1659-1665 ◽  
Author(s):  
Keith Moore ◽  
G. H. N. Towers
Keyword(s):  
Amino Acids ◽  
Benzoic Acid ◽  
Protocatechuic Acid ◽  
Phenylacetic Acid ◽  
Schizophyllum Commune ◽  
Aromatic Amino Acids ◽  
Ring Cleavage ◽  
Hydroxybenzoic Acid ◽  
Phenyllactic Acid ◽  
Phenylalanine Metabolism

Growing cultures of Schizophyllum commune could produce 14CO2 from ring-labelled DL-phenylalanine-14C. Intermediates in the pathway of L-phenylalanine degradation prior to ring cleavage were shown to be cinnamic acid, benzoic acid, p-hydroxybenzoic acid, and protocatechuic acid. Phenylacetic acid and L(−)-β-phenyllactic acid were also identified as products of phenylalanine metabolism.

scholarly journals Degradation of phenylalanine and tyrosine by Sporobolomyces roseus

1968 ◽  
Vol 106 (2) ◽  
pp. 507-514 ◽  
Author(s):  
Keith Moore ◽  
P. V. Subba Rao ◽  
G. H. N. Towers
Keyword(s):  
Benzoic Acid ◽  
Caffeic Acid ◽  
Cinnamic Acid ◽  
Protocatechuic Acid ◽  
Acid Metabolism ◽  
Hydroxybenzoic Acid ◽  
Coumaric Acid ◽  
Tracer Studies ◽  
Lyase Activity ◽  
Sporobolomyces Roseus

Ammonia-lyase activity for l-phenylalanine, m-hydroxyphenylalanine and l-tyrosine was demonstrated in cell-free extracts of Sporobolomyces roseus. Cultures of this organism converted dl-[ring−14C]phenylalanine and l-[U−14C]tyrosine into the corresponding cinnamic acid. Tracer studies showed that these compounds were further metabolized to [14C]protocatechuic acid. Benzoic acid and p-hydroxybenzoic acid were intermediates in this pathway. Washed cells of the organism readily utilized cinnamic acid, p-coumaric acid, caffeic acid, benzoic acid and p-hydroxybenzoic acid. Protocatechuic acid was the terminal aromatic compound formed during the metabolism of these compounds. The cells of S. roseus were able to convert m-coumaric acid into m-hydroxybenzoic acid, but the latter compound, which accumulated in the medium, was not further metabolized. 4-Hydroxycoumarin was identified as the product of o-coumaric acid metabolism by this organism.

scholarly journals Crystallization and preliminary X-ray characterization of the 2,4′-dihydroxyacetophenone dioxygenase fromAlcaligenessp. 4HAP

2014 ◽  
Vol 70 (6) ◽  
pp. 823-826 ◽  
Author(s):  
G. Beaven ◽  
A. Bowyer ◽  
P. Erskine ◽  
S. P. Wood ◽  
A. McCoy ◽  
...  
Keyword(s):  
Synchrotron Radiation ◽  
Formic Acid ◽  
Molecular Oxygen ◽  
Aromatic Ring ◽  
Bond Cleavage ◽  
Its Sequence ◽  
Hydroxybenzoic Acid ◽  
X Ray

The enzyme 2,4′-dihydroxyacetophenone dioxygenase (or DAD) catalyses the conversion of 2,4′-dihydroxyacetophenone to 4-hydroxybenzoic acid and formic acid with the incorporation of molecular oxygen. Whilst the vast majority of dioxygenases cleave within the aromatic ring of the substrate, DAD is very unusual in that it is involved in C—C bond cleavage in a substituent of the aromatic ring. There is evidence that the enzyme is a homotetramer of 20.3 kDa subunits each containing nonhaem iron and its sequence suggests that it belongs to the cupin family of dioxygenases. By the use of limited chymotrypsinolysis, the DAD enzyme fromAlcaligenessp. 4HAP has been crystallized in a form that diffracts synchrotron radiation to a resolution of 2.2 Å.

Formation of Benzoic Acid and p-Hydroxybenzoic Acid in the Blue Green Alga Anacystis nidulans: A Thylakoid-Bound Enzyme Complex Analogous to the Chloroplast System

1976 ◽  
Vol 31 (11-12) ◽  
pp. 693-699 ◽  
Author(s):  
W. Löffelhardt ◽  
H. Kindl
Keyword(s):  
Benzoic Acid ◽  
Phenylalanine Ammonia Lyase ◽  
Higher Plants ◽  
Anacystis Nidulans ◽  
Striking Similarity ◽  
Hydroxybenzoic Acid ◽  
Cinnamic Acids ◽  
Tyrosine Ammonia Lyase ◽  
Membrane Bound ◽  
Enzyme Complexes

Abstract Membrane-Bound Enzyme Complexes, Anacystis nidulans, Thylakoids, Benzoate Synthase The photosynthetic procaryote Anacystis nidulans converts L-phenylalanine and L-tyrosine into benzoic acid and p-hydroxybenzoic acid, respectively. Results obtained with thylakoid fractions support the hypothesis that the reaction sequence is catalyzed by thylakoid-bound enzyme complexes consisting of phenylalanine ammonia-lyase and benzoate synthase or tyrosine ammonia-lyase and p-hydroxybenzoate synthase, respectively. Both complexes do not accept phenylacetic acids as substrates, and cinnamic acids only at a small extent. These properties suggest a striking similarity to a benzoic acid-synthesizing enzyme system from higher plants which is situated at the thylakoid membrane of chloroplasts. The respective complexes of Dunaliella marina and Porphyridium sp. were included in this comparison.

scholarly journals CO2 Improved Synthesis of Benzimidazole with the Catalysis of a New Calcium 4-Amino-3-hydroxybenzoate

2021 ◽  
Vol 68 (1) ◽  
pp. 205-211
Author(s):  
Ruo-Xuan Gao ◽  
Yuan-Yuan Gao ◽  
Ning Zhu ◽  
Li-Min Han
Keyword(s):  
Synergistic Effect ◽  
Benzoic Acid ◽  
Calcium Salt ◽  
Tricarboxylic Acid ◽  
Hydroxybenzoic Acid ◽  
Catalyst Screening

In this paper, we explored the synthesis of benzimidazole by the reaction of DMF and o-phenylenediamine. In the process of catalyst screening, we found that 4-amino-3-hydroxybenzoic acid, benzoic acid, and benzene-1,3,5-tricarboxylic acid could catalyze the reaction. Moreover, the calcium 4-amino-3-hydroxybenzoate and CO2 could more effectively catalyze the reaction, the synergistic effect of CO2 and 4-amino-3-hydroxybenzoic acid calcium salt can increase the yield of benzimidazole from 28% to 94%.

scholarly journals The impact of certain flavourings and preservatives on the survivability of eggs of Ascaris suum and Trichuris suis

2020 ◽  
Vol 11 (2) ◽  
pp. 344-348
Author(s):  
O. O. Boyko ◽  
V. V. Brygadyrenko
Keyword(s):  
Benzoic Acid ◽  
Formic Acid ◽  
Negative Impact ◽  
Ascaris Suum ◽  
Food Additives ◽  
Antibacterial Properties ◽  
Parasitic Nematodes ◽  
Trichuris Suis ◽  
The Impact ◽  
Eggs And Larvae

The article describes a laboratory study of nematocidal properties of flavourings with antibacterial effect against Ascaris suum (Goeze, 1782) and Trichuris suis Schrank, 1788. In the experiments, eight concentrations of food additives with antibacterial properties were used: cinnamaldehyde, benzoic acid, formic acid, linalool, citral, β-ionone. Minimum LC50 value for eggs of A. suum was observed while using cinnamaldehyde and benzoic acid – 1.62 ± 0.37% and 1.69 ± 0.14%, and for eggs of T. suis – 0.57 ± 0.03% and 1.80 ± 0.11% respectively. The lowest influence on the development of eggs of nematodes of pigs’ A. suum and T. suis was exerted by formic acid, linalool, citral and β-ionone. In eggs of A. suum and T. suis, larvae formed in 21 and 50 days even during exposure to 3% emulsions of these substances. The strongest negative impact on the eggs of parasitic nematodes was displayed by cinnamaldehyde flavouring. Further study on nematocidal properties of flavourings, as well as their mixtures, would contribute to the development of preparations which would have a strong effect on eggs and larvae of nematodes of animals and humans.

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