Proline inhibition of pyrroline-5-carboxylate reductase: differences in enzymes obtained from animal and tissue culture sources

The complete amino acid sequence for the 148 amino acid flavodoxin from $\text{Desulfovibrio}\text{vulgaris}$ is presented. This is the first flavoenzyme for which both the complete amino acid sequence and a 2.5 Å resolution x-ray diffraction structure are now known. The position of some important residues in the binding of FMN are given. The D. vulgaris sequence is compared with other published flavodoxin sequences.     

Amino terminal amino acid sequence of the major polypeptide subunit of Torpedo californica acetylcholine receptor

The amino terminal sequence of the 40,000 dalton polypeptide subunit of $\text{Torpedo}\text{californica}$ acetylcholine receptor has been determined for twenty-five cycles using automatic microsequencing procedures. The results demonstrate a unique polypeptide sequence for this receptor subunit and quantitation of amino acid recoveries shows that no significant amounts of polypeptides with blocked amino terminii are present.     

Amino acid sequence homology between “α” subunits from Torpedo and Electrophorus acetylcholine receptor

The amino terminal amino acid sequence of the 41,000 dalton subunit of $\text{Electrophorus}\text{electricus}$ acetylcholine receptor has been determined for 35 cycles by automated sequencing procedures. Comparison of the unique polypeptide sequence obtained for this molecule with that of the major subunit of $\text{Torpedo}\text{californica}$ acetylcholine receptor reveals extensive primary structural homology between the two proteins.     

The amino terminal sequences of acid proteases-human pepsin and gastricsin and the protease of Rhizopus chinensis.

The amino acid sequences near the amino termini of human pepsin (34 residues) and gastricsin (24 residues) and the acid protease from $\text{Rhizopus chinensis}$ (27 residues) have been determined using automated Edman degradation. From these results three additional observations were made. First, two structural variants have been observed for human gastricsin and for the $\text{Rhizopus}$ protease. Both cases are apparently genetic in origin. Second, a stretch of sequence in the $\text{Rhizopus}$ protease, residues 14 to 26, is highly homologous to the known sequence of porcine pepsin at the region of residues 11 to 23. Third, the sequences of the NH₂-terminal region of human pepsin and gastrisin are homologous.     

Structure of rhodotorucine A, a novel lipopeptide,inducing mating tube formation in Rhodosporidiumtoruloides

Rhodotorucine $\text{A}$ is a peptidyl factor which induces mating tube formation in $\text{Rhodosporidium}\text{toruloides}$. The amino acid sequence of the factor was determined by Edman degradation and enzymatic hydrolysis. Rhodotorucine $\text{A}$ was shown to contain a lipophilic amino acid, S-farnesyl cysteine, at C-terminus by proton magnetic resonance, mass spectrometry and chemical synthesis. We proposed the following structure for rhodotorucine $\text{A}$. H-Tyr-Pro-Glu-Ile-Ser-Trp-Thr-Arg-Asn-Gly-Cys(S-farnesyl)-OH     

Stimulation by interferon of induction of differentiation of human promyelocytic leukemia cells

F₁-ATPase was isolated from yeast $\text{S.}\text{cerevisiae}$. The constituent subunits 1 and 2 were purified by gel permeation chromatography, and their amino acid compositions determined. Both subunits have a similar composition except for $\text{1}\text{2}$ cystine, methionine, leucine, histidine, and tryptophan. When F₁ is treated for three hours with 5′-p-[³H]fluorosulfonylbenzoyl adenosine in dimethylsulfoxide, 90% of the activity is lost. Disc gel electrophoresis of the modified complex showed that over 90% of the label was associated with subunit 2. A labelled peptide from a $\text{S.}\text{aureus}$ digest of subunit 2 was isolated and sequenced. It had the following amino acid sequence: His-Try¹-Asp-Val-Ala-Ser-Lys-Val-Gln-Glu, whereby Tyr¹ is the modified amino acid residue. This sequence shows homology to other sequences obtained from maize, beef heart, and $\text{E.}\text{coli}$ F₁-ATPases.     

Amino acid sequence of Desulfovibrio gigas ferredoxin: revisions

Reexamination of the amino acid sequence of $\text{Desulfovibrio}$$\text{gigas}$ ferredoxin revealed that the sequence published in 1971 should be revised. This sequence was determined using automatic protein sequencer in liquid phase and in solid phase. Peptides derived from tryptic hydrolysis, $\text{Staphylococcus}$$\text{aureus}$ protease hydrolysis, cyanogen bromide cleavage were used to construct the total sequence. This ferredoxin contains 6 cysteines per minimum molecular weight of 6,400. 4 cysteines are linked to a (4 Fe-4 S) cluster and the two others possibly participate in a disulfide bridge.     

Cytochrome P-450 and drug metabolism in intestinal villous and crypt cells of rats: effect of dietary iron.

The amino acid sequence of the $\text{Spirulina maxima}$ ferredoxin has been determined. $\text{Spirulina maxima}$ is a blue green algae and is a procaryote. The ferredoxins of the plant-algal type sequenced to date have all been isolated from eucaryotes. The $\text{S. maxima}$ ferredoxin was composed of 98 amino acids arranged in a single polypeptide chain.The sequences of the various procaryote-eucaryote ferredoxins are compared and the differences discussed.     

Amino acid sequence of the heme a subunit of bovine heart cytochrome oxidase and sequence homology with hemoglobin.

The amino acid sequence of the 11.6 K dalton heme $\text{a}$ subunit of bovine heart cytochrome oxidase has been completed and is presented here. The sequence investigation has established the positions in the protein of all the possible heme ligands, namely cysteine, methionine, histidine and lysine residues. However, the isolation conditions may have caused the heme $\text{a}$ to migrate from its original site or the heme is caged by peptides as pointed out in Reference 6. The sequence of the heme $\text{a}$ subunit and the β-chain of hemoglobin shows homology. It is possible that these two proteins have arisen from a common ancestor in the distant past.     

Evidence for a change in catalytic properties of glyceraldehyde 3-phosphate dehydrogenase monomers upon their association in a tetramer

The complete amino acid sequence of human spleen apoferritin has been determined. It consists of 174 amino acids, corresponding to M_r20017. The sequence is very similar to that of horse spleen apoferritin (14% difference between the two sequences). Some peptides were isolated and sequenced which could not be placed in the sequence but which are homologous with part of the principal sequence. Automatic sequence determination of a large peptide resulting from acid cleavage allows us to establish the presence of two homologous sequences (in the ratio $\text{80}\text{20}$).     

Sequential homology of the collagenase from eucaryote Hypoderma lineatum with the proteinases of the trypsin family

The sequence of 32 N-terminal amino acid residues of the collagenase from the larvae Hypoderma lineatum of mol. weight 24000 is homologous with the sequences of pancreatic proteinases. This analysis confirms the hypothesis of similarity made on the basis of amino acid composition, physico-chemical properties and inhibition studies. It is proposed that within the trypsin-like family exists a group of eucaryote collagenases with digestive rather than morphogenic function which cleave specifically native collagen at $\text{3}\text{4}$ from its N-terminus.     

The amino acid sequence of the Azotobacter vinelandii flavodoxin.

The amino acid sequence of a group II flavodoxin, the $\text{Azotobacter vinelandii}$ flavodoxin has been determined. The FMN-redox protein was shown to exist as a single polypeptide chain and to contain 179 amino acids. Despite the rather low amino acid sequence homology with the other flavodoxins sequenced, it is concluded that sequences of the group I and group II flavodoxins are homologous. The major differences between the group I and group II flavodoxins appears to be a lengthening in the C-terminal region in the group II flavodoxins.     

Periodic charge distribution in the intermediate filament proteins desmin and vimentin

A helical coiled-coil region of amino acid sequence surrounding the cysteine residue of desmin and vimentin shows a regular pattern of alternating positive and negative charges with periods close to $\text{28}\text{3}$ and $\text{28}\text{10}$ residues. This suggests relationships with the charge distributions of myosin rod and alpha-keratin. The common features may reflect a similar pattern of three-dimensional packing in vivo for each of these molecules.     

Aspartate transaminase from E. coli: amino acid sequences of the NH2-terminal 33 residues and chymotryptic pyridoxyl tetrapeptide.

The amino acid sequences of pyridoxal-binding tetrapeptide and the NH₂-terminal portion of aspartate transaminase from $\text{E.}$$\text{coli}$ B were analyzed and compared with those of the corresponding parts of the cytosolic and mitochondrial isozymes from pig heart. After borohydride reduction and chymotryptic digestion of the $\text{E.}$$\text{coli}$ enzyme, a pyridoxal-containing peptide was isolated, showing the sequence, Ser-Lys(Pxy)-Asn-Phe, identical with that of the cytosolic isozyme. The NH₂-terminal sequence was determined up to 33 residues with a liquid phase sequence analyzer. Nearly the same degree of homology was observed among the NH₂-terminal sequences of the three aspartate transaminases.     

Partial tertiary structure assignment for the acetylcholine receptor on the basis of the hydrophobicity of amino acid sequences and channel location using single group rotation theory

Six transmembrane segments of the α-protein unit of the acetylcholine receptor (AChR) are assigned from the amino acid sequence (M.Toda $\text{et}\text{al}$, Nature 299, 793–797 (1982), two as part of the ion channel using single group rotation (SGR) theory (E.M.Kosower, Abstracts, pp. 52-3, Symposium “Structure and Dynamics of Nucleic Acids and Proteins”, Sept. 1982) and four on the basis of the hydrophobicity of amino acid sequences.     

Primary structure of heat-stable enterotoxin produced by Yersinia enterocolitica

A heat-stable enterotoxin was isolated and purified from the culture supernatant of $\text{Yersinia enterocolitica}$ by reversed-phase high-performance liquid chromatography. The amino acid sequence of the purified toxin was determined to be as follows: Gln-Ala-Cys(X)-Asp-Pro-Pro-Ser-Pro-Pro-Ala-Glu-Val-Ser-Ser-Asp-Trp-Asp-Cys-Cys-Asp-Val-Cys-Cys-Asn-Pro-Ala-Cys-Ala-Gly-Cys (X: not determined). The C-terminal sequence containing 6 half-cystine residues was highly homologous to that of heat-stable enterotoxin of enterotoxigenic $\text{Escherichia coli.}$     

The amino acid sequence of a 27-residue peptide released from the alpha-chain carboxy-terminus during the plasmic digestion of human fibrinogen.

The amino acid sequence of a 27-residue peptide released during the early stages of the plasmin digestion of human fibrinogen has been determined. The corresponding cyanogen bromide fragment has also been isolated from the purified α-chains of fibrinogen, although a separable fraction of those chains lack the fragment, evidently because of $\text{in}$$\text{vivo}$ degradation. The peptide is the carboxy-terminal segment of native α-chains.     

A novel polygalacturonic acid bioflocculant REA-11 produced by<Emphasis Type="Italic"> Corynebacterium glutamicum</Emphasis>: a proposed biosynthetic pathway and experimental confirmation

Corynebacterium glutamicum CCTCC M201005 produces a novel polygalacturonic acid bioflocculant, REA-11, consisting of galacturonic acid as the main structural unit. A biosynthetic pathway of REA-11 in C. glutamicum CCTCC M201005 was proposed. Evidence for the biosynthetic pathway was provided by: (1) analyzing the response upon addition of UDP-glucose to the culture medium; (2) detecting the presence of several key intermediates in the pathway; and (3) correlating the activities of several key enzymes involved in the pathway with the yields of polygalacturonic acid. The production of polygalacturonic acid was improved by 24%, while the activities of UDP-galactose epimerase and UDP-galactose dehydrogenase were improved by 200% and 50%, respectively, upon addition of 100 M UDP-glucose. In addition, the key intermediates in the proposed biosynthetic pathway, such as UDP-glucose, UDP-galactose, and UDP-glucuronic acid, were detected in cell-free extracts. Furthermore, the activities of UDP-glucose pyrophosphorylase (R²=0.97), UDP-galactose epimerase (R²=0.75) and UDP-galactose dehydrogenase (R²=0.89) were well correlated with the yields of polygalacturonic acid when different sugars were used as sole carbon sources. Therefore, the biosynthetic pathway of REA-11 in C. glutamicum CCTCC M201005 starts from phosphate-1-glucose, which was then converted to UDP-glucose by UDP-pyrophosphorylase. Predominantly, the UDP-glucose was converted to UDP-galactose by UDP-galactose epimerase; the latter was further converted to UDP-galacturonic acid by UDP-galactose dehydrogenase, which was presumably polymerized to polygalacturonic acid bioflocculant REA-11 by an unknown glucosyltransferase and a polymerase.     

Isolation of micro glutamic acid-rich protein from bovine brain

An acidic protein, designated as micro glutamic acid-rich protein, was purified to homogeneity from bovine brain extract, and was characterized in its physicochemical properties. The protein had an isoelectric point of 3.9, a molecular weight of 10,000, and was composed of very limited amino acid constituents; $\text{Asp}\text{Asn}$, Thr, Ser, $\text{Glu}\text{Gln}$, Pro, Gly, Ala and Lys, with a relative abundance of glutamic acid/glutamine which accounted for 51 % of the total amino acid composition. The yield of the protein was 750 μg/kg of wet brain tissue. The amino-terminal sequence analysis suggested that the protein arose through proteolysis of the 58,000-dalton precursor protein, that had been reported in a previous paper [Ishioka $\text{et al}$, (1980) Biochim. Biophys. Acta, 625, 281–290].     

The biosynthesis of phosphorylated tyrosine hydroxylase by organ cultures of rat adrenal medulla and superior cervical ganglia: a correction.

Determination of the complete amino acid sequence of the rubredoxin isolated from the sulfate reducing bacterium $\text{Desulfovibrio}$$\text{gigas}$ showed that the molecule consists of a single polypeptide chain of 52 residues. The sequence of the first 42 residues was determined using an automatic Protein Sequencer. Peptides derived from tryptic hydrolysis and from specific cleavage at tryptophan residue were used to construct the total sequence. Compared with the sequence of $\text{Desulfovibrio}$$\text{vulgaris}$ rubredoxin, 37 positions are identical, and with the sequences of $\text{Clostridium}$$\text{pasteurianum}$, $\text{Peptostreptococcus}$$\text{elsdenii}$, $\text{Micrococcus}$$\text{aerogenes}$ and $\text{D.}$$\text{vulgaris}$ rubredoxins, 20 matching residues occur. A crystallographic study of the $\text{D.}$$\text{gigas}$ rubredoxin is in progress.