| the primary structure of alcohol dehydrogenase from drosophila lebanonensis. extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc. | insect alcohol dehydrogenase is highly different from the well-known yeast and mammalian alcohol dehydrogenases. the enzyme from drosophila lebanonensis has now been characterized by protein analysis and was found to have a 254-residue protein chain with an acetyl-blocked n-terminal met. comparisons with the structures of the enzyme from other species allows judgement of the extent of variability within the insect alcohol dehydrogenases. they have diverged to a considerable extent; two forms ana ... | 1989 | 2707261 |
| drosophila lebanonensis adh: analysis of recombinant wild-type enzyme and site-directed mutants. the effect of restoring the consensus sequence in two positions. | unique amino acid substitutions occur in d. lebanonensis adh. they are found within the putative nad(+)-binding domain and affect residues that are otherwise highly conserved in all other species of the genus. to restore the consensus amino acids, we have constructed an expression system for this enzyme in e. coli, and engineered two mutants, ala13gly and asn56thr. the biochemical and kinetic features of these retromutants are consistent with increased catalytic efficiency and thermal stability. ... | 1994 | 8137935 |
| a compact gene cluster in drosophila: the unrelated cs gene is compressed between duplicated amd and ddc. | cs, a gene with unknown function, and amd and ddc, which encode decarboxylases, are among the most closely spaced genes in d. melanogaster. untranslated 3' ends of the convergently transcribed genes cs and ddc are known to overlap by 88bp. a number of questions arise about the organization of this tightly-packed gene region and about the evolution and function of the cs gene. we have now investigated this three-gene cluster in scaptodrosophila lebanonensis (which diverged from d. melanogaster 60 ... | 1999 | 10231575 |
| addition of side chains to a known backbone with defined side-chain centroids. | an automatic procedure is proposed for adding side chains to a protein backbone; it is based on optimization of a simplified energy function for peptide side chains, given its backbone and positions of side-chain centroids. the energy is expressed as a sum of the energies of interaction between side chains, and a harmonic penalty function accounting for the preservation of the positions of the c(alpha) atoms and the side-chain centroids. the energy of side-chain interactions is calculated with t ... | 2003 | 12646370 |
| evolution of the sex-lethal gene in insects and origin of the sex-determination system in drosophila. | sex-lethal (sxl) functions as the switch gene for sex-determination in drosophila melanogaster by engaging a regulatory cascade. thus far the origin and evolution of both the regulatory system and sxl protein's sex-determination function have remained largely unknown. in this study, we explore systematically the sxl homologs in a wide range of insects, including the 12 sequenced drosophila species, medfly, blowflies, housefly, megaselia scalaris, mosquitoes, butterfly, beetle, honeybee, ant, and ... | 2014 | 24271947 |
| functional constraints of alcohol dehydrogenase (adh) of tephritidae and relationships with other dipteran species. | alcohol dehydrogenase is considered a very important enzyme in insect metabolism because it is involved (in its homodimeric form) in the catalysis of the reversible conversion of various alcohols in larval feeding sites to their corresponding aldehydes and ketones, thus contributing to detoxification and metabolic purposes. using 14 amino acid adh sequences recently determined in our laboratory, we constructed a three-dimensional (3d) model of olive fruit fly bactrocera oleae adh1 and adh2, base ... | 2004 | 15170253 |
| interspecific analysis of the glycosidases of the sperm plasma membrane in drosophila. | we have studied the presence of four sperm glycosidases, alpha-mannosidase, alpha-l- fucosidase and two beta-hexosaminidase isoforms, in 11 species of the genus drosophila spanning approximately an evolutionary 60 my period, and in scaptodrosophila lebanonensis, belonging to the ancestor genus scaptodrosophila. these enzymes had been previously identified in drosophila melanogaster as putative receptors for glycoconjugates of the egg surface. alpha-mannosidase and beta-hexosaminidases are intrin ... | 2009 | 18484570 |
| theoretical calculations of the catalytic triad in short-chain alcohol dehydrogenases/reductases. | three highly conserved active site residues (ser, tyr, and lys) of the family of short-chain alcohol dehydrogenases/reductases (sdrs) were demonstrated to be essential for catalytic activity and have been denoted the catalytic triad of sdrs. in this study computational methods were adopted to study the ionization properties of these amino acids in sdrs from drosophila melanogaster and drosophila lebanonensis. three enzyme models, with different ionization scenarios of the catalytic triad that mi ... | 2008 | 17981907 |
| drosophila alcohol dehydrogenase: acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis. | drosophila alcohol dehydrogenase (dadh) is an nad+-dependent enzyme that catalyzes the oxidation of alcohols to aldehydes/ketones and that is also able to further oxidize aldehydes to their corresponding carboxylic acids. the structure of the ternary enzyme-nadh-acetate complex of the slow alleloform of drosophila melanogaster adh (dmadh-s) was solved at 1.6 a resolution by x-ray crystallography. the coenzyme stereochemistry of the aldehyde dismutation reaction showed that the obtained enzyme-na ... | 2005 | 15581900 |
| duplication, dicistronic transcription, and subsequent evolution of the alcohol dehydrogenase and alcohol dehydrogenase-related genes in drosophila. | it has recently been discovered that the alcohol dehydrogenase and alcohol dehydrogenase-related genes of drosophila melanogaster and closely related species constitute a single transcription unit and that the alcohol dehydrogenase-related gene is exclusively expressed from a dicistronic mrna. here, we show that in drosophila lebanonensis, subgenus scaptodrosophila, adhr: is also transcribed as a dicistronic transcript with adh using degenerate primers designed on the sequence of the known adhr ... | 2000 | 10958851 |
| drosophila lebanonensis alcohol dehydrogenase: ph dependence of the kinetic coefficients. | the alcohol dehydrogenase (adh) from drosophila lebanonensis shows 82% positional identity to the alcohol dehydrogenases from drosophila melanogaster. these insect adhs belong to the short-chain dehydrogenase/reductase family which lack metal ions in their active site. in this family, it appears that the function of zinc in medium chain dehydrogenases has been replaced by three amino acids, ser138, tyr151 and lys155. the present work on d. lebanonensis adh has been performed in order to obtain i ... | 1999 | 10209281 |
| the refined crystal structure of drosophila lebanonensis alcohol dehydrogenase at 1.9 a resolution. | drosophila alcohol dehydrogenase (dadh; ec 1.1.1.1) is a nad(h)-dependent oxidoreductase belonging to the short-chain dehydrogenases/reductases (sdr) family. this homodimeric enzyme catalyzes the dehydrogenation of alcohols to their respective ketones or aldehydes in the fruit-fly drosophila, both for metabolic assimilation and detoxification purposes. the crystal structure of the apo form of dadh, one of the first biochemically characterized member of the sdr family, was solved at 1.9 a resolut ... | 1998 | 9735295 |
| fate of dot chromosome genes in drosophila willistoni and scaptodrosophila lebanonensis determined by in situ hybridization. | one modification of the primitive karyotype of the drosophilidae is the absence of dot chromosomes. the origin of this modification is diverse. in some cases, the fate of the dot chromosomes can be directly inferred from cytogenetic analysis but in other cases a genetic or a combined molecular and cytogenetic analysis is needed, as occurs in drosophila willistoni and scaptodrosophila lebanonensis. we determined the location of four dot chromosome sequences in d. willistoni and s. lebanonensis us ... | 1998 | 9510510 |
| chromosomal homologies between drosophila lebanonensis and d. melanogaster determined by in situ hybridization. | twelve biotin-labelled recombinant dna probes were hybridized to polytene chromosomes of drosophila melanogaster and d. lebanonensis. probes were chosen in order to cover the whole chromosomal complement. six probes correspond to known genes from d. melanogaster (rpii215, h3-h4, mhc, hsp28/23, hsp83, hsp70), four probes are clones isolated from a d. subobscura library (xdh, lambda dsubs3, lambdadsubg3, lambdadsubg4) and the remaining two probes correspond to the adh gene of d. lebanonensis and t ... | 1993 | 8325168 |
| two drosophilids exhibit distinct egf pathway patterns in oogenesis. | deciphering the evolution of morphological structures is a remaining challenge in the field of developmental biology. the respiratory structures of insect eggshells, called the dorsal appendages, provide an outstanding system for exploring these processes since considerable information is known about their patterning and morphogenesis in drosophila melanogaster and dorsal appendage number and morphology vary widely across drosophilid species. we investigated the patterning differences that might ... | 2017 | 29264645 |
| expression study of an alpha-l-fucosidase gene in the drosophilidae family. | the plasma membrane of drosophila (sophophora) melanogaster spermatozoa contains an alpha-l-fucosidase that might be involved in fertilization by interacting with alpha-l-fucose residues on the micropyle of the eggshell. d. (s.) melanogaster has a single gene called cg6128 or fuca encoding for a putative alpha-l-fucosidase. two transcripts have been annotated, ra of 3514 bp, and rb of 1673 bp. while both transcripts encode an alpha-l-fucosidase, ra contains an upstream open reading frame, transl ... | 2008 | 18556148 |
| comparative molecular dynamic simulations of wild type and thr114val mutated scaptodrosophila lebanonensis alcohol dehydrogenase. | enzyme kinetics studies have shown that scaptodrosophila lebanonensis alcohol dehydrogenase (sladh) and other drosophilid alcohol dehydrogenases function by a compulsory-ordered mechanism where the coenzyme binds to the free enzyme, and that a proton is released upon formation of the binary enzyme-nad(+) complex. a proton relay mechanism for the proton abstraction has been suggested that includes an eight-membered chain of water molecules connecting the active site with the bulk solvent. thr114 ... | 2014 | 23528031 |
| an intact eight-membered water chain in drosophilid alcohol dehydrogenases is essential for optimal enzyme activity. | all drosophilid alcohol dehydrogenases contain an eight-member water chain connecting the active site with the solvent at the dimer interface. a similar water chain has also been shown to exist in other short-chain dehydrogenase/reductase (sdr) enzymes, including therapeutically important sdrs. the role of this water chain in the enzymatic reaction is unknown, but it has been proposed to be involved in a proton relay system. in the present study, a connecting link in the water chain was removed ... | 2012 | 22741949 |
| sequences upstream of the homologous cis-elements of the adh adult enhancer of drosophila are required for maximal levels of adh gene transcription in adults of scaptodrosophila lebanonensis. | the evolution of cis-regulatory elements is of particular interest for our understanding of the evolution of gene regulation. the adh gene of drosophilidae shows interspecific differences in tissue-specific expression and transcript levels during development. in scaptodrosophila lebanonensis adults, the level of distal transcripts is maximal between the fourth and eighth day after eclosion and is around five times higher than that in d. melanogaster adh(s). to examine whether these quantitative ... | 2004 | 15166155 |
| a minisatellite with fold-back structure is included in the 5'-flanking region of the adh gene of scaptodrosophila lebanonensis. | a tandem repetitive sequence with a repeat unit of 12 bp has been found 1.3 kb upstream of the adh gene of scaptodrosophila lebanonensis. this repetitive sequence extends over 4.3 kb and consists of two inverted arrays (a fold-back segment). the repeated unit with a consensus sequence gaatacagaata is highly conserved and the nucleotide substitutions are not distributed randomly among the 12 bp. in situ hybridization in s. lebanonensis polytene chromosomes revealed two signals, one at the 60a sec ... | 2006 | 14757731 |
| the catalytic mechanism of drosophila alcohol dehydrogenase: evidence for a proton relay modulated by the coupled ionization of the active site lysine/tyrosine pair and a nad+ ribose oh switch. | the ionization properties of the active site residues in drosophila lebanonensis alcohol dehydrogenase (dadh) were investigated theoretically by using an approach developed to account for multiple locations of the hydrogen atoms of the titratable and polar groups. the electrostatic calculations show that (a) the protonation/deprotonation transition of the binary complex of dadh is related to the coupled ionization of tyr151 and lys155 in the active site and (b) the ph dependence of the proton ab ... | 2003 | 12660997 |
| genesis of drosophila adh: the shaping of the enzymatic activity from a sdr ancestor. | drosophila alcohol dehydrogenase (adh) is an nad(h)-dependent oxidoreductase that catalyzes the oxidation of alcohols and aldehydes. structurally and biochemically distinct from all the reported adhs (typically, the mammalian medium-chain dehydrogenase/reductase-ethanol-metabolizing enzyme), it stands as the only small-alcohol transforming system that has originated from a short-chain dehydrogenase/reductase (sdr) ancestor. the crystal structures of the apo, binary (e.nad(+)) and three ternary ( ... | 2001 | 11306062 |
| the catalytic triad in drosophila alcohol dehydrogenase: ph, temperature and molecular modelling studies. | drosophila alcohol dehydrogenase belongs to the short chain dehydrogenase/reductase (sdr) family which lack metal ions in their active site. in this family, it appears that the three amino acid residues, ser138, tyr151 and lys155 have a similar function as the catalytic zinc in medium chain dehydrogenases. the present work has been performed in order to obtain information about the function of these residues. to obtain this goal, the ph and temperature dependence of various kinetic coefficients ... | 1999 | 10610783 |
| well ordered crystals of a short-chain alcohol dehydrogenase from drosophila lebanonensis: re-evaluation of the crystallographic data and rotation-function analysis. | alcohol dehydrogenase prepared from drosophila lebanonensis yields well ordered plate-like crystals which diffract to better than 2.3 a resolution. the crystals belong to space group p2(1) of the monoclinic system; the unit-cell dimensions are a = 65.25, b = 55.77, c = 70.02 a, alpha = 90, beta = 107.08, gamma = 90 degrees. the asymmetric unit of the crystal cell is most probably occupied by a dimer, corresponding to a packing density of 2.15 a(3) da-l. the orientation of the non-crystallographi ... | 1995 | 15299337 |
| adh and adh-dup sequences of drosophila lebanonensis and d. immigrans: interspecies comparisons. | we have cloned and sequenced the adh genomic region of drosophila lebanonensis (subgenus scaptodrosophila) and d. immigrans (subgenus drosophila). this region, which contains adh, encoding the alcohol dehydrogenase enzyme, and adh-dup (duplicate of adh), has been compared with the same fragment from d. subobscura (subgenus sophophora). even though the flanking regions and introns of both genes have been affected by high substitution rates, the consensus sequences have been clearly identified. al ... | 1993 | 8482531 |
| preliminary x-ray crystallographic studies on alcohol dehydrogenase from drosophila. | the alcohol dehydrogenase (adhase) enzyme catalyses the oxidation of alcohols to aldehydes or ketones using nad+ as a cofactor. functional adhase from drosophila lebanonensis is a dimer, with a monomeric molecular weight of 27,000 and with 254 residues in each polypeptide chain. crystals of the protein have been grown with and without nad+. two crystal forms have been observed. most crystals are plate-like, 0.05 mm in their shortest dimension and up to 0.4 mm in their longest dimension. these cr ... | 1992 | 1522600 |
| adh and phylogenetic relationships of drosophila lebanonesis (scaptodrosophila). | increasing data on drosophila alcohol dehydrogenase (adh) sequences have made it possible to calculate the rate of amino acid replacement per year, which is 1.7 x 10(-9). this value makes this protein suitable for reconstructing phylogenetic relationships within the genus for those species for which no molecular data are available such as scaptodrosophila. the amino acid sequence of drosophila lebanonensis is compared to all of the already known drosophila adhs, stressing the unique characterist ... | 1991 | 1904097 |
| nucleotide sequence of the adh gene of drosophila lebanonensis. | | 1990 | 2251140 |
| nucleotide sequence of the adh gene of drosophila lebanonensis. | | 1990 | 2243785 |
| biochemical properties of alcohol dehydrogenase from drosophila lebanonensis. | purified drosophila lebanonensis alcohol dehydrogenase (adh) revealed one enzymically active zone in starch gel electrophoresis at ph 8.5. this zone was located on the cathode side of the origin. incubation of d. lebanonensis adh with nad+ and acetone altered the electrophoretic pattern to more anodal migrating zones. d. lebanonensis adh has an mr of 56,000, a subunit of mr of 28 000 and is a dimer with two active sites per enzyme molecule. this agrees with a polypeptide chain of 247 residues. m ... | 1986 | 2943270 |
| circadian control of the cellular response to beta-ecdysone in drosophila lebanonensis. i. experimental puff induction and its relation to puparium formation. | | 1974 | 4448116 |
| developmental changes in genome activity in drosophila lebanonensis casteeli pipkin. | | 1971 | 5088498 |