Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A dicarboxylate monoamide amidohydrolase (half-amidase) was identified from a cyclicimide-metabolizing microorganism, Alcaligenes eutrophus 112R4. The enzyme catalyzed the hydrolysis of monoamidated dicarboxylates, which were the hydrolyzing products of cyclic imides by imidase, to dicarboxylates and ammonia. The enzyme showed high catalytic activity to succinamic acid, but no obvious activity to aliphatic amides, amino acid amides, N-carbamoyl amino acids and urea was observed. The productions of half-amidase and imidase were correlative in Alcaligenes eutrophus 112R4, in that succinimide and succinamic acid enhanced the expressions of these two enzymes simultaneously, while free ammonia repressed their expressions. Succinate showed regulation effects on either synthesis or activities of half-amidase and imidase. The characteristics of half-amidase were investigated by using the crude extract of recombined E. coli cell. The fact that cobalt ion stimulated the activity of half-amidase by a coefficient of 3.37, implied that half-amidase was probably a metal-binding enzyme.
 ...
PMID:[A dicarboxylate monoamide amidohydrolase (half-amidase) from Alcaligenes eutrophus 112R4]. 1627 76

TrzF, the allophanate hydrolase from Enterobacter cloacae strain 99, was cloned, overexpressed in the presence of a chaperone protein, and purified to homogeneity. Native TrzF had a subunit molecular weight of 65,401 and a subunit stoichiometry of alpha(2) and did not contain significant levels of metals. TrzF showed time-dependent inhibition by phenyl phosphorodiamidate and is a member of the amidase signature protein family. TrzF was highly active in the hydrolysis of allophanate but was not active with urea, despite having been previously considered a urea amidolyase. TrzF showed lower activity with malonamate, malonamide, and biuret. The allophanate hydrolase from Pseudomonas sp. strain ADP, AtzF, was also shown to hydrolyze biuret slowly. Since biuret and allophanate are consecutive metabolites in cyanuric acid metabolism, the low level of biuret hydrolase activity can have physiological significance. A recombinant Escherichia coli strain containing atzD, encoding cyanuric acid hydrolase that produces biuret, and atzF grew slowly on cyanuric acid as a source of nitrogen. The amount of growth produced was consistent with the liberation of 3 mol of ammonia from cyanuric acid. In vitro, TrzF was shown to hydrolyze biuret to liberate 3 mol of ammonia. The biuret hydrolyzing activity of TrzF might also be physiologically relevant in native strains. E. cloacae strain 99 grows on cyanuric acid with a significant accumulation of biuret.
 ...
PMID:Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth. 1659 48

Allantoin catabolism studies have been extended to intact leaf tissue of soybean (Glycine max L. Merr.). Phenyl phosphordiamidate, one of the most potent urease inhibitors known, does not inhibit (14)CO(2) release from [2,7-(14)C]allantoin (urea labeled), but inhibits urea dependent CO(2) release >/=99.9% under similar conditions. Furthermore, (14)CO(2) and [(14)C] allantoate are the only detectable products of [2,7-(14)C]allantoin catabolism. Neither urea nor any other product were detected by analysis on HPLC organic acid or organic base columns although urea and all commercially available metabolites that have been implicated in allantoin and glyoxylate metabolism can be resolved by a combination of these two columns. In contrast, when allantoin was labeled in the two central, nonureido carbons ([4,5-(14)C]allantoin), its catabolism to [(14)C]allantoate, (14)CO(2), [(14)C]glyoxylate, [(14)C]glycine, and [(14)C]serine in leaf discs could be detected. These data are fully consistent with the metabolism of allantoate by two amidohydrolase reactions (neither of which is urease) that occur at similar rates to release glyoxylate, which in turn is metabolized via the photorespiratory pathway. This is the first evidence that allantoate is metabolized without urease action to NH(4) (+) and CO(2) and that carbons 4 and 5 enter the photorespiratory pathway.
 ...
PMID:Ureide Catabolism of Soybeans : II. Pathway of Catabolism in Intact Leaf Tissue. 1666 92

We demonstrate that allantoate is catabolized in soybean seedcoat extracts by an enzyme complex that has allantoate amidohydrolase and ureidoglycolate amidohydrolase activities. Soybean seedcoat extracts released (14)CO(2) from [ureido-(14)C]ureidoglycolate under conditions in which urease is not detectable. CO(2) and glyoxylate are enzymically released in a one to one ratio indicating that ureidoglycolate amidohydrolase is the responsible activity. Ureidoglycolate amidohydrolase has a K(m) of 85 micromolar for ureidoglycolate. Glyoxylate and CO(2) are enzymically released from allantoate at linear rates in a one to 2.3 ratio from 5 to 30 min. This ratio is consistent with the degradation of allantoate to two CO(2) and one glyoxylate with approximately 23% of the allantoate degraded reacting with 2-mercaptoethanol to yield 2-hydroxyethylthio, 2'-ureido, acetate (RG Winkler, JC Polacco, DG Blevins, DD Randall 1985 Plant Physiol 79: 787-793). That [(14)C]urea production from [2,7-(14)C]allantoate is not detectable indicates that allantoate-dependent glyoxylate production is enzymic and not a result of nonenzymic hydrolysis of a ureido intermediate (nonenzymic hydrolysis releases urea). These results and those from intact tissue studies (RG Winkler DG Blevins, JC Polacco, DD Randall 1987 Plant Physiol 83: 585-591) suggest that soybeans have a second amidohydrolase reaction (ureidoglycolate amidohydrolase) that follows allantoate amidohydrolase in allantoate catabolism. The rate of (14)CO(2) release from [2,7-(14)C]allantoate is not reduced when the volume of the reaction mixture is increased, suggesting that the release of (14)CO(2) is not dependent on the accumulation of free intermediates. That [2,7-(14)C]allantoate dependent (14)CO(2) release is not proportionally diluted by unlabeled ureidoglycolate indicates that the reaction is carried out by an enzyme complex. This is the first report of ureidoglycolate amidohydrolase activity in any organism and the first in vitro demonstration in plants that the ureido-carbons of allantoate can be completely degraded to CO(2) without a urea intermediate.
 ...
PMID:Ureide Catabolism in Soybeans : III. Ureidoglycolate Amidohydrolase and Allantoate Amidohydrolase Are Activities of an Allantoate Degrading Enzyme Complex. 1666 35

Two pigmented mycobacteria isolated from sputum specimens were described by biochemical tests, whole-cell fatty acid analyses by High Performance Liquid Chromatography (HPLC) and sequencing of 65-kDa heat shock protein gene and 16S rRNA gene. The hsp65 gene and 16S rRNA gene sequences of the Mycobacterium sp. G1368 and Mycobacterium sp. E498 were deposited in DDBJ/EMBL/GenBank under accession numbers AY553874, DQ324791 and AY379074, DQ324792, respectively. Mycobacterium sp. G1368 grew in about one week at 37 degrees C and 42 degrees C and produced smooth, yellow colonies. It reduced tellurite and hydrolyzed urea. Nitrate reduction, aryl sulfatase, pyrazin amidase, heat stable catalase and semiquantitative catalase tests were also positive, while Tween 80 hydrolysis was weakly positive. Mycobacterium sp. E498 grew in about 9 days at 37 degrees C and formed smooth, yellow colonies. It hydrolyzed Tween 80, possessed aryl sulfatase, pyrazin amidase and heat stable catalase, however, it did not possess urease and nitrate reductase. These data, in addition to their position in the phylogenetic tree, strongly support the status of novel species at least for Mycobacterium sp. G1368.
 ...
PMID:[Characterization of two new pigmented mycobacteria isolates]. 1700 47

R-Enantioselective amidases are of considerable industrial interest due to potential applications in the production of optically active compounds. Strain ZJB-05174, capable of R-enantioselective degradation of 2,2-dimethylcyclopropanecarboxamide, was isolated employing a newly established colorimetric screening method. Based on morphology, physiological tests, ATB system (ID 32 GN) and the 16S rRNA sequence, this strain was identified as Delftia tsuruhatensis. The intracellular amidase exhibited excellent thermostability and was not inhibited by urea, a known inhibitor of many amidases. The enantiomeric ratio of intracellular amidase decreased from 27 to 5 when the reaction temperature was increased from 30 to 46 degrees C. A novel temperature-dependent reversal of stereospecificity was observed when the temperature was increased to 56 degrees C. Interestingly, when the reaction was performed at 46 degrees C, cell suspensions pre-incubated at 56 degrees C exhibited the same inversion of stereospecificity.
 ...
PMID:Isolation and characterization of Delftia tsuruhatensis ZJB-05174, capable of R-enantioselective degradation of 2,2-dimethylcyclopropanecarboxamide. 1732 Mar 53

With a view to clarify the induction of the "Crabtree consequence" in liver cells of S. mansoni infected mice, the curative effect of oil extract of C. longa was tested and compared to praziquantel (PZQ) the effective drug against all schistosome species occurring in man. Protein, glucose, glucose-6-phopsphatase, AMP-deaminase, adensoine deaminase, urea concentration, pyravate kinase (PK), phosphoenol pyruvate carboxykinase (PEPCK) and PK/PEPCK ratio were estimated. In addition, worm burden and ova count in mice infected with S. mansoni were elucidated. The result showed that C. longa normalized the concentration of protein, glucose, AMP-deaminase and adenosine deaminase, which were changed by infection. Moreover, it lowered pyruvate kinase level, while PZQ-treatment induced more elevation of this enzyme. PZQ was more effective in lowering worm burden while C. longa extract was more potent in reducing egg count.
 ...
PMID:Antischistosomal and liver protective effects of Curcuma longa extract in Schistosoma mansoni infected mice. 1790 45

We have developed a strategy for immobilization-stabilization of penicillin G acylase (PGA) from Kluyvera citrophila by controlled multipoint covalent attachment to agarose-aldehyde gels. This enzyme is composed by two dissimilar subunits noncovalently bound. Thus, in this article we establish clear correlations between enzyme stabilization and the multipoint immobilization and/or between enzyme stabilization and the involvement of the two subunits in the attachment of them to the support. We have demonstrated that important thermal stabilizations of derivatives were only obtained through a very intense enzyme-support multipoint attachment involving the whole enzyme molecule. In this way, we have prepared derivatives preserving more than 90% of catalytic activity and being more than 1000-fold more stable than soluble and one-point attached enzyme. In addition, the involvement of the two subunits in the covalent attachment to the support has proved to be essential to develop interesting strategies for reactivation of inactivated enzyme molecules [e.g., by refolding of immobilized PGA after previous unfolding with urea and sodium dodecyl sulfate (SDS)].
 ...
PMID:Stabilization of heterodimeric enzyme by multipoint covalent immobilization: Penicillin G acylase from Kluyvera citrophila. 1861 49

A 60 kDa antifungal amidase was purified from Peltophorum pterocarpum [corrected] seeds using an isolation procedure that entailed ion-exchange chromatography on Q-Sepharose, ion-exchange chromatography on DEAE-cellulose and FPLC-gel filtration on Superdex 75. Unlike most other antifungal proteins isolated previously, it was adsorbed on Q-Sepharose and DEAE-cellulose. The isolated protein, designated as peltopterin, exhibited an N-terminal amino acid sequence closely resembling those of amidases. It exhibited amidase activity and digested iodoacetamide with an optimum pH and temperature at pH 9 and 50 degrees C, respectively. It also hydrolyzed acrylamide and urea. It impeded mycelial growth in Rhizotonia solani with an IC(50) of 0.65 microm. Chitin deposition at hyphal tips in R. solani was observed by staining with Congo red after incubation with peltopterin. Its antifungal activity was stable throughout pH 0-14 and 25-100 degrees C. It potently inhibited HIV-1 reverse transcriptase with an IC(50) of 27 nm.
 ...
PMID:First report of an antifungal amidase from Peltophorum pterocarpum. [corrected]. 1968 18

Penicillin amidase from Alacaligenes faecalis is an attractive biocatalyst for hydrolysis of penicillin G for production of 6-aminopenicillanic acid, which is used in the synthesis of semi-synthetic beta-lactam antibiotics. Recently a mutant of this enzyme with extended C-terminus of the A-chain comprising parts of the connecting linker peptide was constructed. Its turnover number for the hydrolysis of penicillin G was 140 s(-1), about twice of the value for the wild-type enzyme (80 s(-1)). At the same time the specificity constant was improved about three-fold. The wild-type and the mutant enzymes showed similar pH stability suggesting that the linker peptide fragment covalently attached to the A-chain does not alter the electrostatic interactions in the protein core. Although the global stability of A. faecalis wild-type enzyme and the T206GS213G variant does not differ, the presence of the linker fragment stabilizes the domains interface, as evidenced by the monophasic transition of the mutant enzyme from folded to unfolded state during urea-induced denaturation. The high stability and activity of the mutant enzyme provides a rationale to use it as a biocatalyst in the industrial processes, where the enzyme must be more robust to fluctuations in the operational conditions.
 ...
PMID:Improved A. faecalis penicillin amidase mutant retains the thermodynamic and pH stability of the wild type enzyme. 2022 55


<< Previous 1 2 3 4 5 6 7 Next >>