Aminohydrolases are a class of enzymes that catalyze the hydrolysis of various nitrogenous compounds, including proteins, nucleotides, and amines, playing a crucial role in numerous biological processes such as metabolism and signaling.

MOT1 can activate basal transcription in vitro by regulating the distribution of TATA binding protein between promoter and nonpromoter sites. (1/447)

MOT1 is an ATPase which can dissociate TATA binding protein (TBP)-DNA complexes in a reaction requiring ATP hydrolysis. Consistent with this observation, MOT1 can repress basal transcription in vitro. Paradoxically, however, some genes, such as HIS4, appear to require MOT1 as an activator of transcription in vivo. To further investigate the function of MOT1 in basal transcription, we performed in vitro transcription reactions using yeast nuclear extracts depleted of MOT1. Quantitation of MOT1 revealed that it is an abundant protein, with nuclear extracts from wild-type cells containing a molar excess of MOT1 over TBP. Surprisingly, MOT1 can weakly activate basal transcription in vitro. This activation by MOT1 is detectable with amounts of MOT1 that are approximately stoichiometric to TBP. With amounts of MOT1 similar to those present in wild-type nuclear extracts, MOT1 behaves as a weak repressor of basal transcription. These results suggest that MOT1 might activate transcription via an indirect mechanism in which limiting TBP can be liberated from nonpromoter sites for use at promoters. In support of this idea, excess nonpromoter DNA sequesters TBP and represses transcription, but this effect can be reversed by addition of MOT1. These results help to reconcile previous in vitro and in vivo results and expand the repertoire of transcriptional control strategies to include factor-assisted redistribution of TBP between promoter and nonpromoter sites.  (+info)

A methenyl tetrahydromethanopterin cyclohydrolase and a methenyl tetrahydrofolate cyclohydrolase in Methylobacterium extorquens AM1. (2/447)

Recently it was found that Methylobacterium extorquens AM1 contains both tetrahydromethanopterin (H4MPT) and tetrahydrofolate (H4F) as carriers of C1 units. In this paper we report that the aerobic methylotroph contains a methenyl H4MPT cyclohydrolase (0.9 U x mg-1 cell extract protein) and a methenyl H4F cyclohydrolase (0.23 U x mg-1). Both enzymes, which were specific for their substrates, were purified and characterized and the encoding genes identified via the N-terminal amino acid sequence. The purified methenyl H4MPT cyclohydrolase with a specific activity of 630 U x mg-1 (Vmax = 1500 U x mg-1; Km = 30 microm) was found to be composed of two identical subunits of molecular mass 33 kDa. Its sequence was approximately 40% identical to that of methenyl H4MPT cyclohydrolases from methanogenic archaea. The methenyl H4F cyclohydrolase with a specific activity of 100 U x mg-1 (Vmax = 330 U x mg-1; Km = 80 microm) was found to be composed of two identical subunits of molecular mass 22 kDa. Its sequence was not similar to that of methenyl H4MPT cyclohydrolases or to that of other methenyl H4F cyclohydrolases. Based on the specific activities in cell extract and from the growth properties of insertion mutants it is suggested that the methenyl H4MPT cyclohydrolase might have a catabolic, and the methenyl-H4F cyclohydrolase an anabolic function in the C1-unit metabolism of M. extorquens AM1.  (+info)

Maximal stimulation of meiotic recombination by a yeast transcription factor requires the transcription activation domain and a DNA-binding domain. (3/447)

The DNA sequences located upstream of the yeast HIS4 represent a very strong meiotic recombination hotspot. Although the activity of this hotspot requires the transcription activator Rap1p, the level of HIS4 transcription is not directly related to the level of recombination. We find that the recombination-stimulating activity of Rap1p requires the transcription activation domain of the protein. We show that a hybrid protein with the Gal4p DNA-binding domain and the Rap1p activation domain can stimulate recombination in a strain in which Gal4p-binding sites are inserted upstream of HIS4. In addition, we find recombination hotspot activity associated with the Gal4p DNA-binding sites that is independent of known transcription factors. We suggest that yeast cells have two types of recombination hotspots, alpha (transcription factor dependent) and beta (transcription factor independent).  (+info)

The crystal structure of a bacterial, bifunctional 5,10 methylene-tetrahydrofolate dehydrogenase/cyclohydrolase. (4/447)

The structure of a bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/cyclohydrolase from Escherichia coli has been determined at 2.5 A resolution in the absence of bound substrates and compared to the NADP-bound structure of the homologous enzyme domains from a trifunctional human synthetase enzyme. Superposition of these structures allows the identification of a highly conserved cluster of basic residues that are appropriately positioned to serve as a binding site for the poly-gamma-glutamyl tail of the tetrahydrofolate substrate. Modeling studies and molecular dynamic simulations of bound methylene-tetrahydrofolate and NADP shows that this binding site would allow interaction of the nicotinamide and pterin rings in the dehydrogenase active site. Comparison of these enzymes also indicates differences between their active sites that might allow the development of inhibitors specific to the bacterial target.  (+info)

Chromatin opening and transactivator potentiation by RAP1 in Saccharomyces cerevisiae. (5/447)

Transcriptional activators function in vivo via binding sites that may be packaged into chromatin. Here we show that whereas the transcriptional activator GAL4 is strongly able to perturb chromatin structure via a nucleosomal binding site in yeast, GCN4 does so poorly. Correspondingly, GCN4 requires assistance from an accessory protein, RAP1, for activation of the HIS4 promoter, whereas GAL4 does not. The requirement for RAP1 for GCN4-mediated HIS4 activation is dictated by the DNA-binding domain of GCN4 and not the activation domain, suggesting that RAP1 assists GCN4 in gaining access to its binding site. Consistent with this, overexpression of GCN4 partially alleviates the requirement for RAP1, whereas HIS4 activation via a weak GAL4 binding site requires RAP1. RAP1 is extremely effective at interfering with positioning of a nucleosome containing its binding site, consistent with a role in opening chromatin at the HIS4 promoter. Furthermore, increasing the spacing between binding sites for RAP1 and GCN4 by 5 or 10 bp does not impair HIS4 activation, indicating that cooperative protein-protein interactions are not involved in transcriptional facilitation by RAP1. We conclude that an important role of RAP1 is to assist activator binding by opening chromatin.  (+info)

A set of independent selectable markers for transfection of the human malaria parasite Plasmodium falciparum. (6/447)

Genomic information is rapidly accumulating for the human malaria pathogen, Plasmodium falciparum. Our ability to perform genetic manipulations to understand Plasmodium gene function is limited. Dihydrofolate reductase is the only selectable marker presently available for transfection of P. falciparum. Additional markers are needed for complementation and for expression of mutated forms of essential genes. We tested parasite sensitivity to different drugs for which selectable markers are available. Two of these drugs that were very effective as antiplasmodial inhibitors in culture, blasticidin and geneticin (G418), were selected for further study. The genes BSD, encoding blasticidin S deaminase of Aspergillus terreus, and NEO, encoding neomycin phosphotransferase II from transposon Tn 5, were expressed under the histidine-rich protein III (HRPIII) gene promoter and tested for their ability to confer resistance to blasticidin or G418, respectively. After transfection, blasticidin and G418-resistant parasites tested positive for plasmid replication and BSD or NEO expression. Cross-resistance assays indicate that these markers are independent. The plasmid copy number and the enzymatic activity depended directly on the concentration of the drug used for selection. These markers set the stage for new methods of functional analysis of the P. falciparum genome.  (+info)

Efficient expression, purification and crystallisation of two hyperthermostable enzymes of histidine biosynthesis. (7/447)

Enzymes from hyperthermophiles can be efficiently purified after expression in mesophilic hosts and are well-suited for crystallisation attempts. Two enzymes of histidine biosynthesis from Thermotoga maritima, N'-((5'-phosphoribosyl)-formimino)-5-aminoimidazol-4-carb oxamid ribonucleotide isomerase and the cyclase moiety of imidazoleglycerol phosphate synthase, were overexpressed in Escherichia coli, both in their native and seleno-methionine-labelled forms, purified by heat precipitation of host proteins and crystallised. N'-((5'-phosphoribosyl)-formimino)-5-aminoimidazol-4-carb oxamid ribonucleotide isomerase crystallised in four different forms, all suitable for X-ray structure solution, and the cyclase moiety of imidazoleglycerol phosphate synthase yielded one crystal form that diffracted to atomic resolution. The obtained crystals will enable the determination of the first three-dimensional structures of enzymes from the histidine biosynthetic pathway.  (+info)

Distribution of tetrahydromethanopterin-dependent enzymes in methylotrophic bacteria and phylogeny of methenyl tetrahydromethanopterin cyclohydrolases. (8/447)

The methylotrophic proteobacterium Methylobacterium extorquens AM1 possesses tetrahydromethanopterin (H(4)MPT)-dependent enzymes, which are otherwise specific to methanogenic and sulfate-reducing archaea and which have been suggested to be involved in formaldehyde oxidation to CO(2) in M. extorquens AM1. The distribution of H(4)MPT-dependent enzyme activities in cell extracts of methylotrophic bacteria from 13 different genera are reported. H(4)MPT-dependent activities were detected in all of the methylotrophic and methanotrophic proteobacteria tested that assimilate formaldehyde by the serine or ribulose monophosphate pathway. H(4)MPT-dependent activities were also found in autotrophic Xanthobacter strains. However, no H(4)MPT-dependent enzyme activities could be detected in other autotrophic alpha-proteobacteria or in gram-positive methylotrophic bacteria. Genes encoding methenyl H(4)MPT cyclohydrolase (mch genes) were cloned and sequenced from several proteobacteria. Bacterial and archaeal Mch sequences have roughly 35% amino acid identity and form distinct groups in phylogenetic analysis.  (+info)

Aminohydrolases are a class of enzymes that catalyze the hydrolysis of amide bonds and the breakdown of urea, converting it into ammonia and carbon dioxide. They are also known as amidases or urease. These enzymes play an essential role in various biological processes, including nitrogen metabolism and the detoxification of xenobiotics.

Aminohydrolases can be further classified into several subclasses based on their specificity for different types of amide bonds. For example, peptidases are a type of aminohydrolase that specifically hydrolyze peptide bonds in proteins and peptides. Other examples include ureases, which hydrolyze urea, and acylamidases, which hydrolyze acylamides.

Aminohydrolases are widely distributed in nature and can be found in various organisms, including bacteria, fungi, plants, and animals. They have important applications in biotechnology and medicine, such as in the production of pharmaceuticals, the treatment of wastewater, and the diagnosis of genetic disorders.

An aminohydrolase is a hydrolase enzyme which acts upon an amino group. Aminohydrolases are classified under EC number EC 3.5.4 ... Aminohydrolases at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e (EC 3.5, All ...
... (EC 3.5.99.2, thiaminase, thiaminase II, tenA (gene)) is an enzyme with systematic name 4-amino- ... Aminopyrimidine+aminohydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.5 ... 5-aminomethyl-2-methylpyrimidine aminohydrolase. This enzyme catalyses the following chemical reaction (1) 4-amino-5- ...
... (EC 3.5.99.8, naaA (gene), 5NAA deaminase) is an enzyme with systematic name 5- ... 5-nitroanthranilic+acid+aminohydrolase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ...
... enzymes (nitrile aminohydrolase; EC 3.5.5.1) catalyse the hydrolysis of nitriles to carboxylic acids and ammonia, ...
The systematic name of this enzyme class is ADP aminohydrolase. Other names in common use include adenosine diphosphate ...
The systematic name of this enzyme class is dCTP aminohydrolase. Other names in common use include deoxycytidine triphosphate ...
The systematic name of this enzyme class is ATP aminohydrolase. This enzyme is also called adenosine triphosphate deaminase. ...
The systematic name of this enzyme class is thiocyanate aminohydrolase. As of late 2007, 4 structures have been solved for this ...
The systematic name of this enzyme class is sepiapterin aminohydrolase. Tsusué M (April 1971). "Studies on sepiapterin ...
The systematic name of this enzyme class is adenine aminohydrolase. Other names in common use include adenase, adenine aminase ...
The systematic name of this enzyme class is arylacetonitrile aminohydrolase. This enzyme participates in cyanoamino acid ...
The systematic name of this enzyme class is cytosine aminohydrolase. This enzyme is also called isocytosine deaminase. This ...
The systematic name of this enzyme class is guanosine aminohydrolase. This enzyme is also called guanosine aminase. Isihida Y, ...
The systematic name of this enzyme class is ricinine aminohydrolase. This enzyme participates in nitrogen metabolism. ROBINSON ...
The systematic name of this enzyme class is 4-aminoimidazole aminohydrolase. This enzyme is also called 4-aminoimidazole ...
The systematic name of this enzyme class is 2-aminomuconate aminohydrolase. This enzyme participates in tryptophan metabolism. ...
The systematic name of this enzyme class is blasticidin-S aminohydrolase. As of late 2007, two structures have been solved for ...
The N-terminal domain is a cysteine, histidine-dependent aminohydrolase amidase. Structurally the synthetase and amidase ...
The systematic name of this enzyme class is adenosine-phosphate aminohydrolase. Other names in common use include adenylate ...
The systematic name of this enzyme class is dCTP aminohydrolase (dUMP-forming). This enzyme participates in pyrimidine ...
The systematic name of this enzyme class is cytidine/2'-deoxycytidine aminohydrolase. This enzyme participates in pyrimidine ...
The systematic name of this enzyme class is 2-amino-4-hydroxypteridine aminohydrolase. This enzyme is also called acrasinase. ...
The systematic name of this enzyme class is 3-cyano-L-alanine aminohydrolase. This enzyme is also called beta-cyanoalanine ...
The systematic name of this enzyme class is S-adenosyl-L-homocysteine aminohydrolase. This enzyme is also called ...
The systematic name of this enzyme class is 1-aminocyclopropane-1-carboxylate aminohydrolase (isomerizing). This enzyme is also ...
The systematic name of this enzyme class is 3,5-dibromo-4-hydroxybenzonitrile aminohydrolase. This enzyme participates in 1,4- ...
The systematic name of this enzyme class is 1-pyrroline-4-hydroxy-2-carboxylate aminohydrolase (decyclizing). This enzyme is ...
... (EC 3.5.4.32, 8-OGD) is an enzyme with systematic name 8-oxoguanine aminohydrolase. This enzyme ...
... (also known as adenosine aminohydrolase, or ADA) is an enzyme (EC 3.5.4.4) involved in purine metabolism. ...
... (EC 3.5.1.2, glutaminase I, L-glutaminase, glutamine aminohydrolase) is an amidohydrolase enzyme that generates ...
An aminohydrolase is a hydrolase enzyme which acts upon an amino group. Aminohydrolases are classified under EC number EC 3.5.4 ... Aminohydrolases at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e (EC 3.5, All ...
IPR029055 Nucleophile aminohydrolases, N-terminal. IPR000243 Peptidase T1A, proteasome beta-subunit. IPR016050 Proteasome beta- ...
... glutamine aminohydrolase inhibitor ; glutamine aminohydrolase inhibitors. ...
Similarly, blocking fatty acid aminohydrolase (FAAH) increases anandamide in the brain. This work shows that in alcohol ...
Degradation by fatty acid aminohydrolase (FAAH) may regulate endocannabinoid system bioactivity * Two G-protein-coupled ...
Superfamily d.153.1: N-terminal nucleophile aminohydrolases (Ntn hydrolases) [56235] (8 families) N-terminal residue provides ...
Superfamily d.153.1: N-terminal nucleophile aminohydrolases (Ntn hydrolases) [56235] (8 families) N-terminal residue provides ...
By Systematic name (describes type of rxn and substrate acted upon (urea aminohydrolase). Enz commision (1 of 6 major classes) ...
One important regulator of this molecule is the ADMA-metabolizing enzyme dimethyl-arginine dimethyl-aminohydrolase (DDAH). The ...
Bleomycin is inactivated by the cytosolic Aminohydrolase (Bleomycin Hydrolase). BLMH inhibits bleomycin. ...
Alternative Names EC 3.5.4.4, Adenosine aminohydrolase. Gene Name ADA. Accession Number NP_000013 ...
Human N6-Methyl-AMP/DAMP Aminohydrolase (Abacavir 5-Monophosphate Deaminase) is Capable of Metabolizing N6-Substituted Purine ... Substrate specificity of adenosine aminohydrolase from Streptomyces aureofaciens. 1978, Vol. 43, Issue 9, pp. 2330-2340 [ ...
2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine 2-aminohydrolase. ...
Aminohydrolases [D08.811.277.151]. *Nucleoside Deaminases [D08.811.277.151.486]. *Cytidine Deaminase [D08.811.277.151.486.250] ...
cytidine deaminase, putative / cytidine aminohydrolase, putative. F:hydrolase activity, cytidine deaminase activity, catalytic ...
acetylpolyamine aminohydrolase (NCBI). 104, 425. PA1410. PA1410. probable periplasmic spermidine/putrescine-binding protein ( ...
Aminohydrolases. Bacteriological Techniques. Carboxy-Lyases. Comparative Study. Cytochrome-c Oxidase. Enterobacteriaceae. Paper ... Aminohydrolases, EC 3.5.4.; Carboxy-Lyases, EC 4.1.1.; Cytochrome-c Oxidase, EC 1.9.3.1; Urease, EC 3.5.1.5 ...
There is a common allele, ADA*2, also known as the ADA 2 allozyme. ...
putative acetylpolyamine aminohydrolase YP_989713 normal 0.271818 n/a Burkholderia mallei SAVP1 Bacteria -. ...
ADA - Adenosine aminohydrolase deficiency Active Synonym false false 2478708016 Deficiency of adenosine deaminase Active ...
N-terminal nucleophile aminohydrolases (Ntn hydrolases). 0.0006159. DIRECT. MHC antigen-recognition domain. 0.64. INHERITED ... N-terminal nucleophile aminohydrolases (Ntn hydrolases). 0.001121. Inherited. MHC antigen-recognition domain. 0.6818. Inherited ... N-terminal nucleophile aminohydrolases (Ntn hydrolases). 0.001121. INHERITED FROM: decreased CD8-positive, alpha-beta T cell ...
ureidoglycine aminohydrolase activity GO:0071522 * N,N-Dihydroxy-L-tryptophan decarboxylase activity ...
Accepted name: 5-nitroanthranilic acid aminohydrolase. Reaction: 5-nitroanthranilate + H2O = 5-nitrosalicylate + NH3. Other ...
probable acetylpolyamine aminohydrolase (NCBI). 439, 486. PA4083. cupB4. chaperone CupB4 (NCBI). 36, 439. ...
Nitrilase enzymes (nitrile aminohydrolase; EC 3.5.5.1) catalyse the hydrolysis of nitriles to carboxylic acids and ammonia ...
N-terminal nucleophile aminohydrolases (Ntn hydrolases). superfamily protein. PBA1. 0.82. 0.31. -0.32. ...
AutoFact: Ureidoglycine aminohydrolase n=5 Tax=Brassicaceae RepID=Q8GXV5_ARATH 0.0 • FL-Next: tr=Putative uncharacterized ...
CYTIDINE DEAMINASE PUTATIVE / CYTIDINE AMINOHYDROLASE PUTATIVE AT5G01430. Predicted. Phenotypic Suppression. FSW = 0.0364 ...
Adenosine deaminase, Adenosine aminohydrolase, ADA1, EC 3.5. 4.4. Molecular Weight 42.9 kDa. ...
  • An aminohydrolase is a hydrolase enzyme which acts upon an amino group. (wikipedia.org)
  • One important regulator of this molecule is the ADMA-metabolizing enzyme dimethyl-arginine dimethyl-aminohydrolase (DDAH). (cdc.gov)
  • The first biodegradation enzyme is 5NAA-aminohydrolase (5NAA-A), a metalloprotease family member that converts 5NAA to 5-nitrosalicylic acid. (metu.edu.tr)
  • Grupo de enzimas que catalizan la hidrólisis de enlaces difosfato en compuestos tales como nucleósidos difosfatos y trifosfatos, y anhídridos que contienen grupos sulfonilo, como el adenililsulfato (Enzyme Nomenclature, 1992). (bvsalud.org)
  • Adenosine deaminase also known as adenosine aminohydrolase or ADA is an enzyme involved in purine metabolism. (rtdiagnostics.net)
  • putative chlorohydrolase/aminohydrolase [Ensembl]. (ntu.edu.sg)
  • More recently, it has been shown the genes encoding ammelide aminohydrolase (99 (21). (bio2009.org)
  • It jails the significant download for several aminohydrolase. (freiplan-ingenieure.de)
  • Each DOWNLOAD CORRESPONDENCE ANALYSIS IN PRACTICE, SECOND EDITION (INTERDISCIPLINARY STATISTICS) Discusses an communication by a new completion that has the original aminohydrolase and includes procedures of the years rapidly. (goebel-family.de)