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PubMed2005

DNA mismatch binding activities in Chlorella pyrenoidosa extracts and affinity isolation of G-T mismatch binding proteins.

DNA mismatch recognition proteins contained in the extracts of unicellular alga Chlorella pyrenoidosa were isolated by affinity adsorption and 2-D gel electrophoresis. Incubation of the algal extracts with a 38-mer duplex oligonucleotide carrying a single DNA simple mispair generated a few gel retardation complexes. G-T mispair was recognized significantly better than C-T, G-G, G-A, and C-C mispairs by the algal extracts and these extracts bound very weakly to G-A and C-C mispairs, displaying a universal trend of mismatch binding efficiency. The levels of mismatch recognition complexes were slightly increased in the presence of 1 mM ATP. Two 13-kDa G-T binding polypeptides possessing pIs of 5.3 and 5.5 were isolated after resolving affinity-captured proteins by 2-D gel electrophoresis and the two factors were found to bind 5.5- and 2.8-fold stronger to heteroduplex than to homoduplex DNA, respectively. No proteins significantly homologous to the two algal G-T binding proteins were found by peptide mass fingerprinting (PMF). The sequence of a peptide generated from trypsin-cleavage of one G-T binding factor (pI 5.5) could be aligned with the amino acid sequences that form the C-terminal active sites of human and mouse mismatch-specific uracil/thymine-DNA glycosylases, suggesting the possibility of this factor as an algae- or a Chlorella-specific DNA mismatch glycosylase.

Algal Proteins↗
PubMed2003

Characterization of a chlorella virus PBCV-1 encoded ribonuclease III.

Sequence analysis of the 330-kb genome of chlorella virus PBCV-1 revealed an open reading frame, A464R, which encodes a protein with 30-35% amino acid identity to ribonuclease III (RNase III) from many bacteria. The a464r gene was cloned and the protein was expressed in Escherichia coli using the chitin-binding intein system. The recombinant PBCV-1 RNase III cleaves model dsRNA substrates, in a Mg(2+)-dependent manner, into a defined set of products. The substrate cleavage specificity overlaps, but is nonidentical to that of E. coli RNase III. The a464r gene is expressed very early during PBCV-1 infection, within 5-10 min p.i. The RNase III protein appears at 15 min p.i. and disappears by 120 min p.i. The a464r gene is highly conserved among the chlorella viruses. Phylogenetic analyses indicate that the PBCV enzyme is most closely related to Mycoplasma pneumoniae RNase III.

Amino Acid Sequence↗
PubMed2004

Genetic diversity in chlorella viruses flanking kcv, a gene that encodes a potassium ion channel protein.

The chlorella virus PBCV-1 encodes a 94-amino acid protein named Kcv that produces a K+-selective and slightly voltage-sensitive conductance when expressed in heterologous systems. As reported herein, (i) Northern analysis of kcv expression in PBCV-1-infected cells revealed a complicated pattern suggesting that the gene might be transcribed as a di- or tri-cistronic mRNA both at early and late times after virus infection. (ii) The protein kinase inhibitors H-89, A3, and staurosporine inhibited PBCV-1 Kcv activity in Xenopus oocytes, suggesting that Kcv activity might be controlled by phosphorylation or dephosphorylation. (iii) The PBCV-1 genomic sequence revealed a gene encoding a putative protein kinase (pkx) adjacent to kcv. These findings prompted us to examine the kcv flanking regions in 16 additional chlorella viruses and transcription in two of these viruses, as well as the effect of the three protein kinase inhibitors on two Kcv homologs in Xenopus oocytes. The results indicate (i) pkx is always located 5' to kcv, but the spacing between the two genes varies from 31 to 1588 nucleotides. More variation occurs in the kcv 3' flanking region of the 16 viruses. (ii) The kcv gene is expressed as a late mono-cistronic mRNA. (iii) Unlike the affect on PBCV-1 Kcv, the three protein kinase inhibitors have little or no effect on the activity of the two Kcv homologs in oocytes. (iv) A comparison of the kcv 5' upstream sequences from the 16 viruses identified a highly conserved 10-nucleotide sequence that is present in the promoter region of all of the viruses.

3' Flanking Region↗
PubMedDate not supplied

Inertial migration based concentration factors for suspensions of Chlorella microalgae in branched tubes.

When a dilute suspension flows in the laminar regime through a tube, under certain conditions the suspended particles migrate radially to an equilibrium radial position. Branched tubes can use this radial concentration distribution to concentrate dilute suspensions. Suspensions of microalgae, Chlorella vulgaris, were pumped through tubes of various diameters for tube Reynolds number ranging from 47-1839 and photographed. Upstream particle concentration profiles were obtained by image analysis of the photographs. The dividing stream surfaces in branched tubes were obtained from the three-dimensional numerical solutions of the Navier-Stokes equations for steady, laminar, and homogeneous flow through tubes having one and two orthogonal branches. Concentration factors for Chlorella suspensions in branched tubes, predicted by a general method, fall in the range of 1.0-1.3.

Chlorella↗
PubMed2003

Mechanistic characterization of omega-3 desaturation in the green alga Chlorella vulgaris.

alpha-Linolenic acid (ALA, 9(Z),12(Z),15(Z)-octadecatrienoic acid) derivatives are important plant lipids which play a critical key role in cold tolerance. The final steps of ALA biosynthesis feature a series of regio- and stereoselective dehydrogenation reactions which are catalyzed by a set of enzymes known as fatty acid desaturases. In conjunction with ongoing research into the structural biology of these remarkable catalysts, we have examined the mechanism of double bond introduction at C15,16 as it occurs in a model photosynthetic organism, Chlorella vulgaris. The individual deuterium kinetic isotope effects associated with the C-H bond cleavages at C-15 and C-16 of a thialinoleoyl analogue were measured via competition experiments using appropriately deuterium-labelled 7-thia substrates. A large kinetic isotope effect (KIE) (k(H)/k(D)=10.2+/-2.8) was observed for the C-H bond-breaking step at C-15 while the C-H bond cleavage at C-16 was found to be relatively insensitive to deuterium substitution (k(H)/k(D)=0.8+/-0.2). These results point to C-15 as the site of initial oxidation in omega-3 desaturation and imply that the Chlorella and corresponding plant systems share a common active site architecture.

Chlorella↗
PubMed2002

Factors affecting seasonal variation of membrane filtration resistance caused by Chlorella algae.

A seasonal fluctuation pattern was observed in membrane filtration resistance by Chlorella algae cultured in open ponds in the tropical environment. In order to investigate the causes of this phenomenon, Chlorella was cultivated under controlled conditions and the cake resistance was measured by batch filtration in dead-end mode. The filtration resistance was found to be a function of environmental conditions. Algae could grow favourably and offered low specific cake resistance (R,s) on the order of 10(11) m/g for the culture temperature from 28 degrees C to 35 degrees C. The algal growth was inhibited and the specific cake resistance increased to the order of 10(12) m/g below or above this optimum temperature range. Strong solar radiation, coupled with high temperatures, also inhibited the growth of algae and resulted in higher specific cake resistance. The specific cake resistance of algae cultured at different temperatures increased with the amount of the extracellular organic matter (EOM) extracted by 0.1 N NaOH. Hence EOM, rather than bacteria present in the mono-algal culture, was considered to be the primary factor affecting the cake resistance. The specific cake resistance increased drastically after actively growing cells were stored in nutrient-free water under dark conditions. However, the resistance was slightly decreased when the algal cells were stored in NSIII nutrient media in a dark room, indicating the effect of nutrient availability on the change of the specific cake resistance under the light-limiting conditions. EOM extracted from the cells kept in the nutrient-free water contained less sugar than the fresh culture, whereas the EOM extracted from the cells stored in the NSIII media contained more sugar. The molecular distribution of the EOM shifted from below 1,000 kDa before storage to more than 2,000 kDa after storage in both the nutrient-free and NSIII media.

Chlorella↗
PubMed2000

The Chlorella hexose/H(+)-symporters.

The physiology, molecular biology, and biochemistry of the inducible hexose uptake protein of Chlorella kessleri is reviewed. The protein encoded by the HUP1 gene is the most intensively studied membrane transporter of plants. Responsible for substrate accumulation up to 1500-fold, it translocates one proton together with one hexose, and the cell invests 1 ATP per sugar transported. Kinetics suggest that substrate accumulation is mainly brought about by a large delta Km (Kminside >> Kmoutside). The HUP1 protein (534aa) consists of 12 transmembrane helices of which at least helices I, V, VII, and XI interact with the sugar during translocation and participate in lining the transport path through the membrane. The helix packing might very well be identical to the one suggested for the E. coli lac permease, although the mechanism for transport and proton coupling that has been suggested for lac permease (Kaback, 1997) certainly does not hold for the Chlorella symporter; both are distantly related members, however, of the MFS-family of transporters. HUP1 has been functionally expressed in Schizosaccharomyces pombe, Saccharomyces cerevisiae, Escherichia coli, Volvox carteri, and in Xenopus oocytes.

Amino Acid Sequence↗
PubMed1997

Large-scale production and plaque titration of European Chlorella viruses.

Viruses of the exsymbiotic green freshwater algae Chlorella, family Phycodnaviridae, appear to be distributed worldwide but those found in North American algae have been characterized in detail. The distinct European Chlorella viruses were studied and it was necessary to adapt both large scale purification and the plaque titration assay to the host organisms' different physiology and to our specific laboratory needs. In the virus purification scheme, a precipitation step with polyethylene glycol was introduced which allows high yield recovery of infective particles from large volumes by rapid low-speed centrifugation. In the plaque assay, a standardized algal culture was introduced. The influence of other factors, e.g. circadian rhythm, on plaque growth is also described.

Centrifugation, Density Gradient↗
PubMed2002

Isolation and molecular characterization of the [Fe]-hydrogenase from the unicellular green alga Chlorella fusca.

[Fe]-hydrogenases are redoxenzymes that catalyze the reversible reduction of protons to hydrogen. Hydrogenase activity was observed in a culture of the unicellular green alga Chlorella fusca after an anaerobic incubation, but not in the related species Chlorella vulgaris. Specific polymerase chain reaction (PCR) techniques lead to the isolation of the cDNA and the genomic DNA of a special type of [Fe]-hydrogenase in C. fusca. The functional [Fe]-hydrogenase was purified to homogeneity and its N-terminus was sequenced. The polypeptide sequence shows a high degree of identity with the amino acid sequence deduced from the respective cDNA region. Structural and biochemical analyses indicate that ferredoxin is the main physiological electron donor.

Algal Proteins↗
PubMed2001

UV-B effects on Antarctic Chlorella sp cells.

Growth of Antarctic Chlorella sp cells was measured in cultures irradiated with 30 kJ m(-2) UV-B (280-320 nm). The specific growth rate immediately after the lag phase was 0.36+/-0.06 and 0.26+/-0.03 day(-1) for unirradiated cultures and cultures irradiated with UV-B, respectively, UV-B irradiation significantly decreased ascorbate content by 54.5%, and increased the ascorbyl radical content/ascorbate content ratio by 2.25-fold in algae cultures in log phase. UV-B exposure significantly decreased by 95, 62 and 71% the content of alpha-tocopherol, beta-carotene and total thiols, respectively, in cells in log phase of development. The cellular content of alpha-tocopherol, beta-carotene and total thiols was reduced by 78, 43 and 44%, respectively in stationary phase, as compared to the antioxidant content in the cells during log phase of development. UV-B exposure reduced the content of alpha-tocopherol and total thiols in stationary phase of development by 64 and 91%, respectively, as compared to unirradiated cells. The content of beta-carotene in stationary phase was not affected by UV-B exposure. The results presented here suggest that increased UV-B radiation was responsible for the development of oxidative stress conditions, assessed as the ascorbyl radical content/ascorbate content ratio, in Antarctic Chlorella sp cells. Moreover, a significant decrease in the content of both lipid and water soluble antioxidants might contribute to establish oxidative stress in the cells.

Antarctic Regions↗
PubMedDate not supplied

Characterization of three genes encoding the subunits of light-independent protochlorophyllide reductase in Chlorella protothecoides CS-41.

Light is necessary for hydrogenation of the D ring of protochlorophyllide leading to chlorophyllide formation in higher plants (light-dependent pathway), but it is not essential in phototrophic bacteria (dark pathway). Both pathways, however, occur in some algae, mosses, ferns, and gymnosperms, and each chloroplast genome of these organisms contains three genes, chlL, chlN, and chlB, encoding the three subunits of light-independent protochlorophyllide reductase (LIPOR) required for protochlorophyllide reduction in the dark. In this study, the three LIPOR genes chlL, chlN, and chlB were cloned from the chloroplast of Chlorella protothecoides CS-41 (CSIRO), which grew heterotrophically with considerable chlorophyll yield. Phylogenetic analysis of ChlL/BchL showed that C. protothecoides CS-41 and Chlorella vulgaris C-27 were closely related. Alignment of their amino acid sequences demonstrated that the conserved domains, including the ATP-binding motif and the Fe-S binding motif in the three subunits, were similar to those in nitrogenases. The three-dimensional structural model of ChlL revealed a hypothetical Fe-S center for redox control. Results from RT-PCR amplification indicated that the chlL gene in C. protothecoides contained a 951-bp intron, and the splicing catalytic core structure was similar to that of the light-regulated intron in the psbA gene of Chlamydomonas. The three genes were expressed in E. coli BL21. The sizes of ChlL, ChlN, and ChlB were estimated to be 38, 49, and 58 kDa, respectively, based on the SDS-PAGE analysis.

Amino Acid Sequence↗
PubMed1998

Alternative splicing of a precursor-mRNA encoded by the Chlorella sorokiniana NADP-specific glutamate dehydrogenase gene yields mRNAs for precursor proteins of isozyme subunits with different ammonium affinities.

Chlorella sorokiniana has seven ammonium-inducible, chloroplastic NADP-specific glutamate dehydrogenase (NADP-GDH) isozymes composed of varying ratios of alpha- and beta-subunits. Southern blot and allele-specific PCR analyses indicate that the C. sorokiniana genome possesses a single 7178 bp nuclear NADP-GDH gene. cDNA cloning and sequencing, 5'-RACE-PCR analysis, and RNase protection analysis identified two NADP-GDH mRNAs that are identical with the exception of a 42 nt sequence located within the 5'-coding region of the longer mRNA. The 42 nt sequence, termed an auxon because it serves as an exon or intron, appears to undergo alternative splicing from the precursor mRNA by a process that is regulated by both nutritional and environmental signals. Depending upon whether the auxon is included or excluded in a mature mRNA, the gene can be considered to consist of 22 or 23 exons, respectively. The 2074 and 2116 nt mRNAs encode precursor proteins of 56,350 and 57,850 Da, respectively. The N-termini of the purified mature alpha- and beta-subunits were sequenced, identifying full-length subunits of 53,501 and 52,342 Da, respectively. The sequences of the subunits are identical except for an 11 amino acid extension at the N-terminus of the alpha-subunit. The alpha-subunit has an additional alpha-helical domain at its N-terminus compared with the beta-subunit. By correlating the abundances of the two mRNAs with the levels (and relative turnover rates) of the alpha- and beta-subunit antigens during induction in Chlorella, the larger mRNA is proposed to encode the larger subunit.

Alternative Splicing↗
PubMed2000

Chlorophyll breakdown in Chlorella protothecoides: characterization of degreening and cloning of degreening-related genes.

Chlorella protothecoides cultures grown in a nitrogen-free bleaching medium (BM-N) in the dark rapidly degraded chlorophyll (Chl) to red catabolites. This degreening process was investigated under different growth conditions. Supply of nitrogen to the culture medium (BM+N) inhibited bleaching and the synthesis of catabolites as did the addition to BM-N of cycloheximide or a chelator, 2,2'-bipyridyl. In contrast, chloramphenicol or the protease inhibitor E64 had no effect. During bleaching, Chl breakdown was accompanied by the degradation of cellular proteins such as light-harvesting complex II, cytochrome f and protochlorophyllide oxido-reductase. During growth in BM-N, protease activity increased and proteins immunologically detectable with an antibody against a senescence-enhanced cysteine protease accumulated. cDNAs from BM-N and BM+N cells were used for differential and subtractive screening to isolate cDNAs representing genes with degreening-enhanced expression (dee) in C. protothecoides. Several different dees were identified with different patterns of expression during Chlorella growth but which were all expressed at higher levels during bleaching. Among these, dee4 was most abundant and its expression was exclusive in BM-N cultures. Analysis of the dee sequences showed that they encode different proteins including a novel amino acid carrier (dee4), ferritin, ATP-dependent citrate lyase, a Ca2+-binding protein, MO25, ubiquinone-cytochrome c-reductase and several new proteins.

Algal Proteins↗
PubMed2003

Heterologous expression of cDNAs encoding Chlorella sorokiniana NADP-specific glutamate dehydrogenase wild-type and mutant subunits in Escherichia coli cells and comparison of kinetic and thermal stability properties of their homohexamers.

Full-length cDNAs encoding the alpha- and beta-subunits and a truncated mutant subunit of the Chlorella sorokiniana NADP-GDH isozymes were constructed and expressed in Escherichia coli cells. The kinetic and thermal stability properties of the resultant homohexamers were examined. The electrophoretic mobility of the recombinant alpha- and beta-subunits was identical to that of the native subunits as determined by immunoblotting. The homohexamers were purified by anion-exchange and gel-filtration chromatography. The alpha- and beta-homohexamers that were synthesized in the bacterial cells were shown to have similar Michaelis constants for their substrates as previously shown after synthesis in C. sorokiniana cells (Bascomb and Schmidt, 1987). The alpha homohexamer synthesized in the bacterium was allosteric with respect to NADPH but to a lesser degree than when isolated from the alga. The mutant homohexamer was composed of subunits that were truncated by 40 amino acids at their N-termini. This mutant isozyme was kinetically similar to the larger, anabolic alpha-homohexamer, but it did not display the allosteric response to NADPH shown by the alpha-homohexamer. The three isozymes had significant thermal tolerance and were stable at 50 degrees C. The temperature optimum for catalytic activity for the alpha- and beta-homohexamers was 60 degrees C, and 65 degrees C for the delta40N homohexamer. This study demonstrated that most of the kinetic properties of the Chlorella sorokiniana NADP-GDH isozymes were retained after their synthesis in a heterologous system, and that the distinctive N-terminal domains of these isozymes have dramatic effects on their biochemical characteristics.

Amino Acid Sequence↗
PubMed1981

Purification and properties of adenylyl sulphate:ammonia adenylyltransferase from Chlorella catalysing the formation of adenosine 5' -phosphoramidate from adenosine 5' -phosphosulphate and ammonia.

Extracts of Chlorella pyrenoidosa, Euglena gracilis var. bacillaris, spinach, barley, Dictyostelium discoideum and Escherichia coli form an unknown compound enzymically from adenosine 5'-phosphosulphate in the presence of ammonia. This unknown compound shares the following properties with adenosine 5'-phosphoramidate: molar proportions of constituent parts (1 adenine:1 ribose:1 phosphate:1 ammonia released at low pH), co-electrophoresis in all buffers tested including borate, formation of AMP at low pH through release of ammonia, mass and i.r. spectra and conversion into 5'-AMP by phosphodiesterase. This unknown compound therefore appears to be identical with adenosine 5'-phosphoramidate. The enzyme that catalyses the formation of adenosine 5'-phosphoramidate from ammonia and adenosine 5'-phosphosulphate was purified 1800-fold (to homogeneity) from Chlorella by using (NH(4))(2)SO(4) precipitation and DEAE-cellulose, Sephadex and Reactive Blue 2-agarose chromatography. The purified enzyme shows one band of protein, coincident with activity, at a position corresponding to 60000-65000 molecular weight, on polyacrylamide-gel electrophoresis, and yields three subunits on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of 26000, 21000 and 17000 molecular weight, consistent with a molecular weight of 64000 for the native enzyme. Isoelectrofocusing yields one band of pI4.2. The pH optimum of the enzyme-catalysed reaction is 8.8. ATP, ADP or adenosine 3'-phosphate 5'-phosphosulphate will not replace adenosine 5'-phosphosulphate, and the apparent K(m) for the last-mentioned compound is 0.82mm. The apparent K(m) for ammonia (assuming NH(3) to be the active species) is about 10mm. A large variety of primary, secondary and tertiary amines or amides will not replace ammonia. One mol.prop. of adenosine 5'-phosphosulphate reacts with 1 mol.prop. of ammonia to yield 1 mol.prop. each of adenosine 5'-phosphoramidate and sulphate; no AMP is found. The highly purified enzyme does not catalyse any of the known reactions of adenosine 5'-phosphosulphate, including those catalysed by ATP sulphurylase, adenosine 5'-phosphosulphate kinase, adenosine 5'-phosphosulphate sulphotransferase or ADP sulphurylase. Adenosine 5'-phosphoramidate is found in old samples of the ammonium salt of adenosine 5'-phosphosulphate and can be formed non-enzymically if adenosine 5'-phosphosulphate and ammonia are boiled. In the non-enzymic reaction both adenosine 5'-phosphoramidate and AMP are formed. Thus the enzyme forms adenosine 5'-phosphoramidate by selectively speeding up an already favoured reaction.

Adenosine Monophosphate↗
PubMed2004

Small potassium ion channel proteins encoded by chlorella viruses.

Kcv, a 94-aa protein encoded by Paramecium bursaria chlorella virus 1, is the smallest known protein to form a functional potassium ion channel and basically corresponds to the "pore module" of potassium channels. Both viral replication and channel activity are inhibited by the ion channel blockers barium and amantadine but not by cesium. Genes encoding Kcv-like proteins were isolated from 40 additional chlorella viruses. Differences in 16 of the 94 amino acids were detected, producing six Kcv-like proteins with amino acid substitutions occurring in most of the functional domains of the protein (N terminus, transmembrane 1, pore helix, selectivity filter, and transmembrane 2). The six proteins form functional potassium selective channels in Xenopus oocytes with different properties including altered current kinetics and inhibition by cesium. The amino acid changes together with the different properties observed in the six Kcv-like channels will be used to guide site-directed mutations, either singularly or in combination, to identify key amino acids that confer specific properties to Kcv.

Amino Acid Sequence↗
PubMed1994

Km mutants of the Chlorella monosaccharide/H+ cotransporter randomly generated by PCR.

The HUP1 gene codes for the monosaccharide/H+ cotransporter protein of Chlorella kessleri. The gene is functionally expressed in Schizosaccharomyces pombe. This heterologous system has been used to screen for Km mutants of the Chlorella symporter. Since S. pombe transformed with HUP1 cDNA showed a 1000-fold increase in sensitivity toward the toxic sugar analogue 2-deoxyglucose, we screened for transformants with a decreased 2-deoxyglucose sensitivity. The transformants were produced with HUP1 cDNA randomly mutagenized by PCR. From 73 transformants with decreased 2-deoxyglucose sensitivity, four mutants with increased Km values for D-glucose were obtained. The amino acid exchanges responsible for the increased Km values are located in the center of the putative transmembrane helices V (Q179E), VII (Q298R), and XI (V433L/N436Y). Q179N and Q299N had previously been shown by directed mutagenesis to affect the Km value of the transporter for D-glucose. The drastic mutational changes Q298R and N436Y gave rise to very high Km values; however, the corresponding conservative amino acid changes Q298N or N436Q obtained by directed mutagenesis also result in Km values increased by a factor of 10 or 20, respectively. The data therefore support the proposal that at least helices V, VII, and XI may line the sugar translocation path and determine its specificity. These results are discussed in relation to other sugar transporters and to the interaction of the yeast hexokinase B with D-glucose as known from published crystal structures.

Amino Acid Sequence↗
PubMed2000

Topoisomerase II from Chlorella virus PBCV-1. Characterization of the smallest known type II topoisomerase.

Type II topoisomerases, a family of enzymes that govern topological DNA interconversions, are essential to many cellular processes in eukaryotic organisms. Because no data are available about the functions of these enzymes in the replication of viruses that infect eukaryotic hosts, this led us to express and characterize the first topoisomerase II encoded by one of such viruses. Paramecium bursaria chlorella virus 1 (PBCV-1) infects certain chlorella-like green algae and encodes a 120-kDa protein with a similarity to type II topoisomerases. This protein was expressed in Saccharomyces cerevisiae and was highly active in relaxation of both negatively and positively supercoiled plasmid DNA, catenation of plasmid DNA, and decatenation of kinetoplast DNA networks. Its optimal activity was determined, and the omission of Mg(2+) or its replacement with other divalent cations abolished DNA relaxation. All activities of the recombinant enzyme were ATP dependent. Increasing salt concentrations shifted DNA relaxation from a normally processive mechanism to a distributive mode. Thus, even though the PBCV-1 enzyme is considerably smaller than other eukaryotic topoisomerase II enzymes (whose molecular masses are typically 160-180 kDa), it displays all the catalytic properties expected for a type II topoisomerase.

Chlorella↗