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At least 541 records · Page 30Linked to original sources
PubMed2004

Amino acid sequence of a thrombin like enzyme, elegaxobin II, from the venom of Trimeresurus elegans (Sakishima-Habu).

The amino acid sequence of a thrombin like enzyme , named elegaxobin II, isolated from the venom of Trimeresurus elegans (Sakishima-habu) was determined by Edman sequencing of the peptides which was derived from digests with cyanogen bromide, achromobacter protease I, trypsin, endoproteinase Asp-N, and chymotrypsin. Elegaxobin II consisted of 233 amino acids and showed conservation of the catalytic amino acid residues (His(57), Asp(102), and Ser(195)) of chymotrypsin family serine protease in its amino acid sequence. The carboxyterminal amino acid, Leu, was determined using carboxypeptidase Y. This enzyme contains glucosamine and an N-linked glycosylation site. Elegaxobin II was 91% homologous in sequence to elegaxobin and protease I from the same snake venom, and it was 67, 75, 31 and 26% homologous in sequences to flavoxobin, KN-BJ 2, human kallikrein and bovine thrombin, respectively. Elegaxobin II lacked thrombin's ETW (146-148) loop, as well as its functionally important YPPW (60-insertion loop).

Amino Acid Sequence↗
PubMed1987

Chronic bacterial endophthalmitis.

We studied a specific syndrome of uveitis secondary to intraocular bacterial pathogens of low virulence after extracapsular cataract extraction and intraocular lens implantation in three eyes. The onset of photophobia, visual impairment, conjunctival redness, and uveitis was delayed for four days to 12 weeks after surgery. Chronic inflammation persisted for five weeks to 16 months before a definitive diagnosis was made. Signs and symptoms were suppressed by administration of topical and systemic corticosteroids. Intraocular biopsy and antibiotic injection both established the cause as bacterial endophthalmitis and resulted in resolution of signs and symptoms. Staphylococcus epidermidis was cultured in two eyes and Achromobacter was cultured in one.

Adrenal Cortex Hormones↗
PubMed1983

Superinfections in herpes simplex keratitis.

We reviewed 15 cases of culture-proven corneal superinfections in 15 patients (eight men and seven women ranging in age from 41 to 86 years) with recurrent herpes simplex keratitis. The factors that appeared to increase the risk of superinfection were the presence of an epithelial defect (found in all 15 cases), a history of recurrent herpetic keratouveitis (found in ten cases), and the use of topical corticosteroids (found in 13 cases). Eight of the 15 patients were taking antibiotics at the time the superinfections were diagnosed, indicating that topical antibiotics do not provide sufficient protection. Gram-negative rods were found in six cases (Proteus mirabilis, Pseudomonas aeruginosa, Serratia marcescens, Klebsiella oxytoca, Enterobacter cloacae, and Achromobacter sp.). Gram-positive organisms, often in association with another infecting agent, were found in six cases (Staphylococcus epidermidis, three cases; S. aureus, two cases; and Streptococcus sp., two cases). Fungal superinfections were found in three cases (Cephalosporium acremonium, Candida albicans, and Aspergillus fumigatus, one case each). Mycobacterium cheloni was found in two cases.

Administration, Topical↗
PubMed2002

Phosphorylation of calmodulin by Ca2+/calmodulin-dependent protein kinase IV.

Calmodulin-dependent protein kinase IV (CaM-kinase IV) phosphorylated calmodulin (CaM), which is its own activator, in a poly-L-Lys [poly(Lys)]-dependent manner. Although CaM-kinase II weakly phosphorylated CaM under the same conditions, CaM-kinase I, CaM-kinase kinase alpha, and cAMP-dependent protein kinase did not phosphorylate CaM. Polycations such as poly(Lys) were required for the phosphorylation. The optimum concentration of poly(Lys) for the phosphorylation of 1 microM CaM was about 10 microg/ml, but poly(Lys) strongly inhibited CaM-kinase IV activity toward syntide-2 at this concentration, suggesting that the phosphorylation of CaM is not due to simple activation of the catalytic activity. Poly-L-Arg could partially substitute for poly(Lys), but protamine, spermine, and poly-L-Glu/Lys/Tyr (6/3/1) could not. When phosphorylation was carried out in the presence of poly(Lys) having various molecular weights, poly(Lys) with a higher molecular weight resulted in a higher degree of phosphorylation. Binding experiments using fluorescence polarization suggested that poly(Lys) mediates interaction between the CaM-kinase IV/CaM complex and another CaM. The 32P-labeled CaM was digested with BrCN and Achromobacter protease I, and the resulting peptides were purified by reversed-phase HPLC. Automated Edman sequence analysis of the peptides, together with phosphoamino acid analysis, indicated that the major phosphorylation site was Thr44. Activation of CaM-kinase II by the phosphorylated CaM was significantly lower than that by the nonphosphorylated CaM. Thus, CaM-kinase IV activated by binding Ca2+/CaM can bind and phosphorylate another CaM with the aid of poly(Lys), leading to a decrease in the activity of CaM.

Amino Acid Sequence↗
PubMed2003

Crystal structure of a NO-forming nitrite reductase mutant: an analog of a transition state in enzymatic reaction.

I257E was obtained by site directed mutagenesis of nitrite reductase from Achromobacter cycloclastes. The mutant has no enzyme activity. Its crystal structure determined at 1.65A resolution shows that the side-chain carboxyl group of the mutated residue, Glu257, coordinates with the type 2 copper in the mutant and blocks the contact between the type 2 copper and its solvent channel, indicating that the accessibility of the type 2 copper is essential for maintaining the activity of nitrite reductase. The carboxylate is an analog of the substrate, nitrite, but the distances between the type 2 copper and the two oxygen atoms of the side-chain carboxyl group are reversed in comparison to the binding of nitrite to the native enzyme. In the mutant, both the type 2 copper and the N epsilon atom on the imidazole ring of its coordinated residue His135 move in the substrate binding direction relative to the native enzyme. In addition, an EPR study showed that the type 2 copper in the mutant is in a reduced state. We propose that mutant I257E is in a state corresponding to a transition state in the enzymatic reaction.

Alcaligenes↗
PubMed1990

The complete amino acid sequence of the mature form of rat sepiapterin reductase.

The partial amino acid sequence of rat sepiapterin reductase was determined using peptides generated by cleavage of the S-carboxyamidomethylated protein with Achromobacter protease I, cyanogen bromide, chymotrypsin or BNPS-skatole. The protein began with N-acetyl methionyl residue at the N-terminus and ended with isoleucyl residue at the C-terminus. The present results essentially coincided with the amino acid sequence predicted from the nucleotide sequence of the cDNA recently reported by Citron et al. (Proc. Natl. Acad. Sci. USA 87, 6436-6440 (1990)), clarified the processing event during the biosynthesis and provided the complete amino acid sequence of the mature form of the enzyme.

Alcohol Oxidoreductases↗
PubMed1988

Near stoichiometric, irreversible inactivation of bacterial collagenases by o-chloranil (3,4,5,6-tetrachloro-1,2-benzoquinone).

The hydrogen-abstracting quinone derivative 3,4,5,6-tetrachloro-1,2-benzoquinone (o-chloranil) caused a strong, near stoichiometric, irreversible inactivation of the collagenases from Bacillus cereus, Clostridium histolyticum and Achromobacter iophagus. p-Chloranil was a weaker inactivator. o-Chloranil reacted rapidly with a site that affected substrate binding. Amino acid analyses of native and totally inactivated enzymes, and the pH-profile of inactivation suggest that the dissociated form of a tyrosine residue was modified.

Alcaligenes↗
PubMed2000

Zeta-crystallin catalyzes the reductive activation of 2,4,6-trinitrotoluene to generate reactive oxygen species: a proposed mechanism for the induction of cataracts.

Exposure to 2,4,6-trinitrotoluene (TNT) has been shown to cause induction of cataract in which oxidative stress plays a critical role. From bovine lens we purified to homogeneity and identified an enzyme that catalyzes the reduction of TNT, resulting in the production of reactive oxygen species. The final preparation of TNT reductase showed a single band with a subunit molecular weight of 38 kDa on SDS-PAGE. Sequence data from peptides obtained by digestion with lysylendopeptidase Achromobacter protease I (API) revealed that TNT reductase is identical to zeta-crystallin. Superoxide anions were formed during reduction of TNT by zeta-crystallin, though negligible enzyme activity or protein content for superoxide dismutase, a superoxide scavenging enzyme, was found in the lens. Thus, the present results suggest that the induction of cataracts by TNT may be associated with increased oxidative stress, as a result of reductive activation of TNT generating superoxide anions, there being minimal antioxidant enzyme activity for defense against reactive oxygen species exogenously produced in the lens.

Amino Acid Sequence↗
PubMed2002

Amino acid sequence of a thrombin like enzyme, elegaxobin, from the venom of Trimeresurus elegans (Sakishima-habu).

The amino acid sequence of a thrombin like enzyme, named elegaxobin, isolated from the venom of Trimeresurus elegans (Sakishima-habu) was determined by Edman sequencing of the peptides, derived from digests with cyanogen bromide, hydroxylamine, achromobacter protease I, trypsin, V8 protease, and chymotrypsin. Elegaxobin showed conservation of the catalytic amino acid residues (His, Asp, and Ser) of trypsin like serine protease in the amino acid sequence. The carboxy-terminal amino acid, Leu, was determined using carboxypeptidase Y. Elegaxobin consisted of 233 amino acids and had a calculated molecular weight of 25,439. Elegaxobin was 53, 59, 26 and 40% homologous in sequence to ancrod, flavoxobin, bovine thrombin and trypsin, respectively.

Amino Acid Sequence↗
PubMedDate not supplied

Intravenous line infection due to Ochrobactrum anthropi (CDC Group Vd) in a normal host.

Ochrobactrum anthropi, formerly known as Achromobacter species (CDC group Vd), is an aerobic, gram-negative bacillus widely distributed in aquatic environments. Most important, it has been implicated as a cause of intravenous line infection in immunocompromised hosts with solid tumors or hematologic malignancies. Trimethoprim-sulfamethoxazole and aminoglycosides are usually active against O. anthropi, but this organism is usually resistant to beta-lactam antibiotics. Because O. anthropi is a low-virulence organism, patients with intravenous-line infections have been cured without removal of the intravenous catheter. We describe a case of intravenous-line infection in a normal host that was successfully resolved alter catheter removal.

Catheterization, Central Venous↗
PubMed1998

Cloning of a Lysobacter enzymogenes gene that encodes an arginyl endopeptidase (endoproteinase Arg-C).

Screening an expression library of Lysobacter enzymogenes DNA allowed us to clone a gene encoding a serine protease that cleaves synthetic substrates C-terminal to Arg and, to a lesser extent, Lys residues. The gene product, which shares sequence homology with the lysyl endopeptidases from L. enzymogenes and Achromobacter lyticus, consists of a signal sequence (24 residues), pro-region ( approximately 195 residues), and catalytic domain ( approximately 244 residues). Downstream of this gene is an open reading frame that lacks a promoter and appears to encode an inactive type I subtilase.

Amino Acid Sequence↗
PubMed1999

Helix 6 of subdomain III A of human serum albumin is the region primarily photolabeled by ketoprofen, an arylpropionic acid NSAID containing a benzophenone moiety.

It is well known that the subdomain III A (site II) of human serum albumin (HSA) binds a variety of endogenous and exogenous substances. However, the nature of the microenvironment of the binding site remains unclear. Ketoprofen (KP), an arylpropionic acid NSAID which contains a benzophenone moiety, was used as a photoaffinity labeling agent to label the binding region. Subsequent CNBr cleavage of the photolabeled HSA revealed that the 11.6 kDa and 9.4 kDa fragments contained most of the incorporated radioactivity. Competition experiments showed that the 11.6 kDa fragment contains the common binding region for site II ligands. This fragment was redigested with Achromobacter lyticus protease I (AP-I) and the amino acid sequence of the photolabeled peptide was determined to be XCTESLVNRR, which corresponds to the sequence 476C-485K of HSA. The complete amino acid sequence of the corresponding AP-I digested HSA peptide encompasses residues 476 to 499, which form helices 5 and 6 of subdomain III A. The HSA-Myr X-ray crystallography data showed that helix 5 is involved to the least extent in ligand binding. A docking model provided further support that helix 6 represents the photolabeled region of KP.

Affinity Labels↗
PubMed1985

Prevention of bacterial contamination of water in dental units.

A study of the bacterial contamination of water in dental units was conducted in five dental practitioners' clinics and one university dental hospital in Tokyo. Various bacteria in numbers of 10(2)-10(5)/ml were detected in the water delivered from all 42 of the dental units examined, though very few bacteria were detected in the tap water upstream of the units. Most of the organisms isolated from the water were Gram-negative bacilli, predominantly Alcaligenes, Achromobacter and Pseudomonas spp. A new decontamination apparatus that could be incorporated into the pipe system of dental units was devised and its performance was evaluated in one unit. It effectively prevented bacterial contamination of the water.

Bacteria↗
PubMedDate not supplied

Ambient STM and in situ AFM study of nitrite reductase proteins adsorbed on gold and graphite: influence of the substrate on protein interactions.

Trimeric Achromobacter cycloclastes Cu-containing nitrite reductase (CuNIR) proteins adsorbed on gold and graphite have been studied by ambient STM and in situ AFM. STM resolves them individually and in layers, distinguishing the sub-molecular individual units of the trimer. The Cu atoms are not visible to STM. STM shows that individual CuNIR denatures as it adsorbs on Au, although a deformed trimeric shape can be identified in some cases. CuNIR forms disordered layers on gold. On graphite, ordered self-assembled layers of CuNIR have been resolved by in situ AFM and ambient STM forming parallel rows whose separation distance corresponds to the size of one of the units of the trimer, 5nm. Ambient STM can achieve better resolution than in situ AFM in the images of the layers. We observe differences between domains showing the parallel row structure and unstructured parts of the CuNIR layer by in situ phase imaging AFM.

Adsorption↗
PubMed2000

Amino acid sequence and some properties of phytolacain G, a cysteine protease from growing fruit of pokeweed, Phytolacca americana.

A protease, phytolacain G, has been found to appear on CM-Sepharose ion-exchange chromatography of greenish small-size fruits of pokeweed, Phytolacca americana L, from ca. 2 weeks after flowering, and increases during fruit enlargement. Reddish ripe fruit of the pokeweed contained both phytolacain G and R. The molecular mass of phytolacain G was estimated to be 25.5 kDa by SDS-PAGE. Its amino acid sequence was reconstructed by automated sequence analysis of the peptides obtained after cleavage with Achromobacter protease I, chymotrypsin, and cyanogen bromide. The enzyme is composed of 216 amino acid residues, of which it shares 152 identical amino acid residues (70%) with phytolacain R, 126 (58%) with melain G, 108 (50%) with papain, 106 (49%) with actinidain, and 96 (44%) with stem bromelain. The amino acid residues forming the substrate binding S(2) pocket of papain, Tyr67, Pro68, Trp69, Val133, and Phe207, were predicted to be replaced by Trp, Met, His, Ala, and Ser in phytolacain G, respectively. As a consequence of these substitutions, the S(2) pocket is expected to be less hydrophobic in phytolacain G than in papain.

Amino Acid Sequence↗
PubMed1999

Structure of the glucan-binding sugar chain of Tip1p, a cell wall protein of Saccharomyces cerevisiae.

Tip1p is one of the major cell wall mannoproteins of Saccharomyces cerevisiae and is presumed to be synthesized as a glycosylphosphatidylinositol (GPI)-anchored form. We purified Tip1p from a glucanase extract of yeast cell walls and analyzed the sugar chain involved in the cell wall linkage. One mol of glucanase-extracted Tip1p contained 7.5 mol of glucose derived from glucan and 1 mol of ethanolamine, a component of the GPI anchor. One mol of the C-terminal peptide of Tip1p digested with Achromobacter protease I also contained 7.9 mol of glucose and 1 mol of ethanolamine. On the other hand, Tip1p contained no glucosamine, which is a component of the GPI anchor. The glucan-binding sugar chain of Tip1p was released by hydrazinolysis and isolated. This sugar chain contained ethanolamine with a free amino group and a glucose reducing end, but no mannose reducing end. Phosphodiesterase treatment eliminated the free amino group from this sugar chain, suggesting that a phosphodiester bond exists between the ethanolamine and the glucan remnant. These results indicate (1) the glucan-binding sugar chain of Tip1p is a GPI derivative, and (2) the GPI anchor is cleaved at the glycosyl moiety, and the resultant mannose reducing end is probably used to link Tip1p to cell wall glucan.

Amino Acid Sequence↗
PubMed2000

Isolation and identification of cellulolytic bacteria involved in the degradation of natural cellulosic fibres.

In search for bacterial cultures that are able to rapidly degrade cellulosic plant fibres in vitro, 77 cellulolytic strains were isolated from Belgian and Czech soils after enrichment on flax or sisal fibres as sole sources of carbon. The strains were characterized using fatty acid analysis, and 74 strains were grouped into three major clusters by numerical analysis. The first major cluster contained Cellulomonas strains. Within this cluster three subclusters could be delineated by principal component analysis, that were recognized by their fatty acid compositions as Cellulomonas gelida, Cellulomonas biazotea and Cellulomonas cellulans, containing 9, 8 and 13 strains respectively. The second major cluster, with 9 strains, was assigned to Flavobacterium johnsoniae. The 34 strains of the third cluster could not be identified by commercial identification systems on the basis of their fatty acid profiles and API 20NE profiles. On the basis of their phenotypic characteristics they met the description of the genus Cellvibrio, their fatty acid profiles were similar to those of four authentic Cellvibrio mixtus strains, and the 16S rRNA genes from four representatives showed up to 97.8% sequence similarity to 16S rDNA from Cellvibrio mixtus ACM 2603. Three non-clustered strains were assigned to Curtobacterium flaccumfaciens, Achromobacter piechaudii and Pseudomonas mendocina. Two strains assigned to Cellvibrio were able to degrade several flax, broom and cotton fibres very rapidly in a standardized in vitro test, causing mass losses of 40 to 86% within 13 days of incubation, but not jute.

Bacterial Typing Techniques↗
PubMed1997

Evidence for increased hydroxylation of pyrrolidone amino acid residues in the cuticle of mature Onchocerca volvulus.

To determine whether morphologic changes are accompanied by variations in the biochemical and antigenic properties of the cuticle of Onchocerca volvulus during development, we isolated and compared the 2-mercaptoethanol soluble cuticular proteins and the insoluble cuticlin from the predominant life-cycle stages occurring in man. SDS-PAGE analysis, before and after digestion with collagenase from Achromobacter iophagus, revealed that the polypeptide composition of the 2-mercaptoethanol-solubilised extracts from adult males and nodular microfilariae are quite distinct and that these extracts contained predominantly collagen-like proteins. Demonstrated by immunoblotting with a hyper immune patient serum pool (n = 107), five strongly reactive antigens with apparent molecular weights of 126, 68, 43, 37 and 33 kDa were detected in the extracts from adult males, while at least eight prominent and several weakly reactive components were detected in the extracts from nodular microfilariae. The overall amino acid composition of the cuticular extracts from the various stages demonstrates that: (a) the cuticle of the adult male stage is rich in glycine, pyrrolidone amino acids, and acidic amino acids or their amides, (b) eggshells are particularly poor in proline but rich in serine residues (14.5%), (c) nodular microfilariae cuticular extracts are poor in proline but rich in valine (9.0%) and lysine (7.3%) and (d) hydroxyproline and hydroxylysine are present in the cuticle of adults but absent in the juvenile life-cycle stages (nodular microfilariae and eggs). This study firstly, indicates that the composition of the cuticle of O. volvulus may thus, be quite distinct from one parasite stage to another and secondly, that the maturation of the parasite in the human host may be accompanied by the extensive hydroxylation of prolyl residues and to a lesser extent of lysyl residues in the predominantly collagen-like cuticular proteins.

Amino Acids↗