N-terminal amino acid sequences of acid proteases: acid proteases from Penicillium roqueforti and Rhizopus chinensis and alignment with penicillopepsin and mammalian proteases

1977 ◽  
Vol 55 (5) ◽  
pp. 504-506 ◽  
Author(s):  
Jean-Claude Gripon ◽  
Sung H. Rhee ◽  
Theo Hofmann
Keyword(s):  
Active Site ◽  
Amino Acid Sequences ◽  
Acid Protease ◽  
Penicillium Roqueforti ◽  
Terminal Sequence ◽  
Terminal Amino Acid ◽  
Amino Terminal ◽  
Rhizopus Chinensis ◽  
Terminal Amino ◽  
Amino Terminal Sequence

The amino-terminal sequence (33 residues) of the acid protease from Penicillium roqueforti has been determined with an automated sequencer. The amino-terminal sequence of Rhizopus pepsin (published by Sepulveda, P., Jackson, K. W. &Tang, J. (1975) Biochem. Biophys. Res. Commun. 63, 1106–1112) has been extended from 27 residues to 39 residues. Also, it was found that two forms of Rhizopus pepsin differ in position 15, where Rhizopus pepsin I has an isoleucine and Rhizopus pepsin II a valine residue. The new sequences have been aligned with the amino-terminal sequences of penicillopepsin (EC 3.4.23.7), pig pepsin (EC 3.4.23.1), calf chymosin (EC 3.4.23.4), human pepsin (EC 3.4.23.2), human gastricsin (EC 3.4.23.3), and cow pepsin (EC 3.4.23.1). Residues 31–35 (numbering based on pig pepsin, Tang, J., Sepulveda, P., Marciniszyn, Jr., J., Chen, K.S.C., Huang. W.-Y., Tao, N., Liu, D. &Lanier, P. (1973) Proc. Natl. Acad. Sci. U.S.A. 70, 3437–3439) are identical in all enzymes. This section contains one of the two aspartic acids (Asp-32) implicated in the active site. The similarity of the sequences provides strong evidence for the homology of these acid proteases.

Rhizopus Acid Proteinases (Rhizopus-pepsins): Properties and Homology with Other Acid Proteinases

1973 ◽  
Vol 51 (6) ◽  
pp. 789-796 ◽  
Author(s):  
J. E. S. Graham ◽  
J. Šodek ◽  
T. Hofmann
Keyword(s):  
Amino Acid ◽  
Methyl Ester ◽  
Active Site ◽  
Amino Acid Sequences ◽  
Acid Proteinase ◽  
Terminal Amino Acid ◽  
Isoelectric Focussing ◽  
Rhizopus Chinensis ◽  
Terminal Amino ◽  
Enzyme I

Commercial acid proteinase from Rhizopus chinensis has been further purified by isoelectric focussing. Two forms of the enzyme (I and II) with very similar properties have been obtained. Like other fungal acid proteinases they activate trypsinogen at pH 3.4 and are inhibited by diazoacetyl norleucine methyl ester. Because of the lability of the label it has not been possible to isolate the active site peptide from a peptic digest. N-terminal amino acid sequences were determined for Rhizopus enzyme I (NH2∙Ala∙Gly∙Val∙Gly∙Thr∙Val∙Pro∙Asx∙Thr), for Rhizopus enzyme II (NH2∙Ala∙Gly∙Val∙Gly∙Thr∙Val∙Pro), and for penicillopepsin (NH2∙Ala∙Ala∙Ser∙Gly∙Val∙Ala∙Thr∙Asn∙Thr∙Pro∙Thr). The similarity in enzymic properties and in the sequence suggests that the Rhizopus enzymes are homologous with penicillopepsin and hence also with mammalian pepsins and calf chymosin.

A major Litomosoides carinii microfilarial sheath glycoprotein (gp22): amino terminal sequence and immunological studies with corresponding synthetic peptides

Parasitology ◽  
1991 ◽  
Vol 103 (3) ◽  
pp. 387-394 ◽  
Author(s):  
G. Bardehle ◽  
F. J. Conraths ◽  
F. Fahrenholz ◽  
M. Hintz ◽  
D. Linder ◽  
...  
Keyword(s):  
Amino Acid ◽  
Synthetic Peptides ◽  
General Pattern ◽  
Amino Sugar ◽  
Amino Acid Sequences ◽  
Terminal Amino Acid ◽  
Amino Terminal ◽  
Terminal Amino ◽  
Amino Terminal Sequence

The major glycoprotein of the sheath of Litomosoides carinii microfilariae (gp22) was analysed for its amino acid and amino sugar composition. It is rich in proline, glutamine/glutamic acid and glycine and contains (N-acetyl)galactosamine. The N-terminal amino acid sequence was determined up to position 37. It consists of a group of 6 repeats of the pentapeptide sequence methionine-glycine-proline-glutamine-proline with two minor modifications in repeats 3–6, while the first two repeats follow the general pattern more loosely. Identical N-terminal amino acid sequences were found in at least two other sheath polypeptides (33 kDa, 39 kDa). Antisera prepared against 3 overlapping synthetic peptides corresponding to the amino terminus of gp22 recognized different epitopes. They all reacted with identical patterns of sheath polypeptides. The antisera failed to recognize antigens of 4th-stage larvae of L. carinii. In contrast, cross-reacting epitopes were detected in other parasite stages. Antisera reacted with material surrounding embryos and microfilariae in the uterus of females, and caused patchy fluorescence on the sheath of blood-derived and in vitro-released microfilariae.

N-Terminal amino acid sequence of rat tonin: homology with serine proteases

1978 ◽  
Vol 56 (9) ◽  
pp. 920-925 ◽  
Author(s):  
N. G. Seidah ◽  
R. Routhier ◽  
M. Caron ◽  
M. Chrétien ◽  
S. Demassieux ◽  
...  
Keyword(s):  
Serine Proteases ◽  
Terminal Sequence ◽  
Renin Substrate ◽  
Amino Terminal ◽  
Single Polypeptide Chain ◽  
Serine Protease Family ◽  
Terminal Amino ◽  
Single Polypeptide ◽  
Carboxy Terminal ◽  
Amino Terminal Sequence

In this paper, we present the amino-terminal sequence of rat tonin, an endopeptidase responsible for the conversion of angiotensinogen, the tetradecapeptide renin substrate, or angiotensin I to angiotensin II. It is shown that isoleucine and proline occupy the amino- and carboxy-terminal residues respectively. The N-terminal sequence analysis permitted the identification of 34 out of the first 40 residue s of the single polypeptide chain composed of 272 amino acids. The se results showed an extensive homology with the sequence of many serine proteases of the trypsin–chymotrypsin family. This information, coupled with the slow inhibition of tonin by diisopropylfluorophosphate, classified this enzyme as a selective endopeptidase of the active serine protease family.

Neisseria pili proteins: amino-terminal amino acid sequences and identification of an unusual amino acid

Biochemistry ◽  
1978 ◽  
Vol 17 (3) ◽  
pp. 442-445 ◽  
Author(s):  
Mark A. Hermodson ◽  
Kirk C. S. Chen ◽  
Thomas M. Buchanan
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Terminal Amino Acid ◽  
Amino Terminal ◽  
Terminal Amino ◽  
Unusual Amino Acid

scholarly journals Rice Embryo Globulins: Amino-Terminal Amino Acid Sequences, cDNA Cloning and Expression

1996 ◽  
Vol 37 (5) ◽  
pp. 612-620 ◽  
Author(s):  
J.-L. Sun ◽  
H. Nakagawa ◽  
S. Karita ◽  
K. Ohmiya ◽  
T. Hattori
Keyword(s):  
Amino Acid ◽  
Cdna Cloning ◽  
Amino Acid Sequences ◽  
Cloning And Expression ◽  
Terminal Amino Acid ◽  
Amino Terminal ◽  
Terminal Amino ◽  
Rice Embryo

scholarly journals Alpha and beta chains of SB and DR antigens are structurally distinct

1982 ◽  
Vol 156 (5) ◽  
pp. 1557-1562 ◽  
Author(s):  
CK Hurley ◽  
S Shaw ◽  
L Nadler ◽  
S Schlossman ◽  
JD Capra
Keyword(s):  
Amino Acid ◽  
Cell Line ◽  
Amino Acid Sequences ◽  
Beta Chain ◽  
Terminal Amino Acid ◽  
Amino Terminal ◽  
Terminal Amino

Limited amino-terminal amino acid sequences of the HLA-controlled SB and DR antigens from the cell line PREISS (DR4/4, SB3/4) show differences in both the alpha and beta chain sequences of the two molecules. SB antigens, like DR antigens, appear to be homologues of the murine I-E antigens.

scholarly journals Amino-terminal amino acid sequences and the evolution of frog (Rana esculenta ) trypsin and chymotrypsin

FEBS Letters ◽  
1980 ◽  
Vol 109 (1) ◽  
pp. 45-49 ◽  
Author(s):  
Wolfgang Pies ◽  
Robert Zwilling ◽  
Richard G. Woodbury ◽  
Hans Neurath
Keyword(s):  
Amino Acid ◽  
Rana Esculenta ◽  
Amino Acid Sequences ◽  
Terminal Amino Acid ◽  
Amino Terminal ◽  
Terminal Amino

Two Nearly Identical Aromatic Compound Hydrolase Genes in a Strong Polychlorinated Biphenyl Degrader,Rhodococcus sp. Strain RHA1

1998 ◽  
Vol 64 (6) ◽  
pp. 2006-2012 ◽  
Author(s):  
Akihiro Yamada ◽  
Hidekazu Kishi ◽  
Katsumi Sugiyama ◽  
Takashi Hatta ◽  
Kanji Nakamura ◽  
...  
Keyword(s):  
Amino Acid ◽  
Polychlorinated Biphenyl ◽  
Blot Hybridization ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Terminal Sequence ◽  
Gene Encoding ◽  
Amino Terminal ◽  
Gene Assay ◽  
Amino Terminal Sequence

ABSTRACT The two 2-hydroxy-6-oxohepta-2,4-dienoate (HOHD) hydrolase genes,etbD1 and etbD2, were cloned from a strong polychlorinated biphenyl (PCB) degrader, Rhodococcus sp. strain RHA1, and their nucleotide sequences were determined. TheetbD2 gene was located in the vicinity of bphAgene homologs and encoded an enzyme whose amino-terminal sequence was very similar to the amino-terminal sequence of the HOHD hydrolase which was purified from RHA1. Using the etbD2 gene fragment as a probe, we cloned the etbD1 gene encoding the purified HOHD hydrolase by colony hybridization. Both genes encode a product having 274 amino acid residues and containing the nucleophile motif conserved in α/β hydrolase fold enzymes. The deduced amino acid sequences were quite similar to the amino acid sequences of the products of the single-ring aromatic hydrolase genes, such as dmpD,cumD, todF, and xylF, and not very similar to the amino acid sequences of the products of bphDgenes from PCB degraders, including RHA1. The two HOHD hydrolase genes and the RHA1 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate (HPDA) hydrolase gene, bphD, were expressed in Escherichia coli, and their relative enzymatic activities were examined. The product ofbphD was very specific to HPDA, and the products ofetbD1 and etbD2 were specific to HOHD. All of the gene products exhibited poor activities against themeta-cleavage product of catechol. These results agreed with the results obtained for BphD and EtbD1 hydrolases purified from RHA1. The three hydrolase genes exhibited similar induction patterns both in an RNA slot blot hybridization analysis and in a reporter gene assay when a promoter probe vector was used. They were induced by biphenyl, ethylbenzene, benzene, toluene, and ortho-xylene. Strain RCD1, an RHA1 mutant strain lacking both the bphDgene and the etbD2 gene, grew well on ethylbenzene. This result suggested that the etbD1 gene product is involved in the meta-cleavage metabolic pathway of ethylbenzene.

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