Full Text Available AU005182 ws30355 11/12/09 GO hit GO:0003824(catalytic activity)|GO:0016831(carboxy-lyase activit ... m castaneum] 10/08/28 36 %/126 aa FBpp0232658|Dvir\\amd -PA 10/08/27 34 %/115 aa K01C8.3b#CE28344#WBGene000 ...
Reiskind, J B; Bowes, G.
Udotea flabellum is a marine, macroscopic green alga with C4-like photosynthetic characteristics, including little O2 inhibition of photosynthesis, a low CO2 compensation point, and minimal photorespiration; but it lacks anatomical features analogous to the Kranz compartmentation of C4 plants, and phosphoenolpyruvate carboxylase [PEPC; orthophosphate:oxaloacetate carboxy-lyase (phosphorylating), EC 126.96.36.199] activity is negligible. Phosphoenolpyruvate carboxykinase (PEPCK) activity (carboxyla...
Cronan, J. E.
The enzyme, aspartate 1-decarboxylase (L-aspartate 1-carboxy-lyase; EC 188.8.131.52), that catalyzes the reaction aspartate leads to beta-alanine + CO2 was found in extracts of Escherichia coli. panD mutants of E. coli are defective in beta-alanine biosynthesis and lack aspartate 1-decarboxylase. Therefore, the enzyme functions in the biosynthesis of the beta-alanine moiety of pantothenate. The genetic lesion in these mutants is closely linked to the other pantothenate (pan) loci of E. coli K-12.
Brabant, M; McConlogue, L; van Daalen Wetters, T; Coffino, P
We used molecular cloning to isolate a functional gene for mouse ornithine decarboxylase (OrnDCase; L-ornithine carboxy-lyase, EC 184.108.40.206) from a cell line in which that gene had been selectively amplified. The position of the 5' terminus of the mRNA was identified, and the coding sequence was shown to be preceded by a 312- or 313-nucleotide (nt) untranslated leader. The latter is highly G + C rich, particularly in its 5'-most portion. The leader can be anticipated to have extensive and stab...
O' Leary, M.H. (Univ. of Wisconsin, Madison); Joworski, R.J.; Hartman, F.C.
Ribulosebisphosphate carboxylase (3-phospho-D-glycerate carboxy-lyase (dimerizing), EC 220.127.116.11) from Rhodospirillum rubrum is activated by CO/sub 2/ and Mg/sup 2 +/. /sup 13/C NMR spectra were determined for the unactivated enzyme and for enzyme that had been activated by /sup 13/CO/sub 2/ and Mg/sup 2 +/. In addition to the expected resonance for H/sup 13/CO/sub 3//sup -//CO/sub 3//sup 2 -/ at 161.8 ppM downfield from tetramethylsilane, the spectrum of the activated enzyme shows a broad resonance at 164.9 ppM. Analogy with previous NMR studies of /sup 13/CO/sub 2/ binding to hemoglobin suggests that the CO/sub 2/ activation of ribulosebisphosphate carboxylase involves formation of a carbamate between an enzyme amino group and CO/sub 2/.
The diurnal change in activity of ribulose 1,5-bisphosphate (Rbu-1,5-P2) carboxylase [3-phospho-D-glycerate carboxy-lyase (dimerizing); EC 18.104.22.168] of leaves of Phaseolus vulgaris is regulated (in part) by mechanisms that control the level of an endogenous inhibitor that binds tightly to the activated (carbamoylated) form of Rbu-1,5-P2 carboxylase. This inhibitor was extracted from leaves and copurified with the Rbu-1,5-P2 carboxylase of the leaves. Further purification by ion-exchange chromatography, adsorption to purified Rbu-1,5-P2 carboxylase, barium precipitation, and HPLC separation yielded a phosphorylated compound that was a strong inhibitor of Rbu-1,5-P2 carboxylase. The compound was analyzed by GC/MS, 13C NMR, and 1H NMR and shown to be 2-carboxyarabinitol 1-phosphate [(2-C-phosphohydroxymethyl)-D-ribonic acid]. The structure of the isolated compound differs from the Rbu-1,5-P2 carboxylase transition-state analogue 2-carboxyarabinitol 1,5-bisphosphate only by the lack of the C-5 phosphate group. This difference results in a higher binding constant for the monophosphate compared with the bisphosphate. The less tightly bound compound acts in a light-dependent, reversible regulation of Rbu-1,5-P2 carboxylase activity in vivo
Full Text Available Abstract Background During mating, insect males eject accessory gland proteins (Acps into the female genital tract. These substances are known to affect female post-mating behavior and physiology. In addition, they may harm the female, e.g., in reducing its lifespan. This is interpreted as a consequence of sexual antagonistic co-evolution. Whereas sexual conflict abounds in non-social species, the peculiar life history of social insects (ants, bees, wasps with lifelong pair-bonding and no re-mating aligns the reproductive interests of the sexes. Harming the female during mating would negatively affect male fitness and sexual antagonism is therefore not expected. Indeed, mating appears to increase female longevity in at least one ant species. Acps are presumed to play a role in this phenomenon, but the underlying mechanisms are unknown. In this study, we investigated genes, which are preferentially expressed in male accessory glands of the ant Leptothorax gredleri, to determine which proteins might be transferred in the seminal fluid. Results By a suppression subtractive hybridization protocol we obtained 20 unique sequences (USs. Twelve had mutual best matches with genes predicted for Apis mellifera and Nasonia vitripennis. Functional information (Gene Ontology was available only for seven of these, including intracellular signaling, energy-dependent transport and metabolic enzyme activities. The remaining eight USs did not match sequences from other species. Six genes were further analyzed by quantitative RT-PCR in three life cycle stages of male ants. A gene with carboxy-lyase activity and one of unpredicted function were significantly overexpressed in accessory glands of sexually mature males. Conclusions Our study is the first one to investigate differential gene expression in ants in a context related to mating. Our findings indicate that male accessory glands of L. gredleri express a series of genes that are unique to this species