scholarly journals Amino acid sequence of a new type of antifreeze protein, from the longhorn sculpin Myoxocephalus octodecimspinosis

FEBS Letters ◽  
1997 ◽  
Vol 402 (1) ◽  
pp. 17-20 ◽  
Author(s):  
Gejing Deng ◽  
David W Andrews ◽  
Richard A Laursen
1997 ◽  
Vol 41 (9) ◽  
pp. 2016-2018 ◽  
Author(s):  
B Perichon ◽  
P Reynolds ◽  
P Courvalin

Enterococcus faecium BM4339 was constitutively resistant to vancomycin (MIC, 64 microg/ml) and to low levels of teicoplanin (MIC, 4 microg/ml). A 605-bp product obtained with the V1 and V2 primers for amplification of genes encoding D-Ala:D-Ala ligases and related glycopeptide resistance proteins was sequenced after cloning. The deduced amino acid sequence had 69% identity with VanA and VanB and 43% identity with VanC, consistent with the finding that BM4339 synthesized peptidoglycan precursors terminating in D-lactate. This new type of glycopeptide resistance phenotype was designated VanD.


1999 ◽  
Vol 43 (9) ◽  
pp. 2161-2164 ◽  
Author(s):  
Marguerite Fines ◽  
Bruno Perichon ◽  
Peter Reynolds ◽  
Daniel F. Sahm ◽  
Patrice Courvalin

ABSTRACT Enterococcus faecalis BM4405 was resistant to low levels of vancomycin (MIC, 16 μg/ml) and was susceptible to teicoplanin (MIC, 0.5 μg/ml). No PCR product was obtained when the total DNA of this clinical isolate was used as a template with primers specific for glycopeptide resistance genes vanA,vanB, vanC, and vanD. However, a 604-bp PCR fragment was obtained when V1 and V2 degenerate primers were used and total DNA was digested with HindIII as a template. The product was cloned and sequenced. The deduced amino acid sequence had greater identity (55%) with VanC than with VanA (45%), VanB (43%), or VanD (44%). This was consistent with the fact that BM4405 synthesized peptidoglycan precursors that terminated ind-serine residues. After induction with vancomycin, weakd,d-dipeptidase and penicillin-insensitived,d-carboxypeptidase activities were detected in cytoplasmic extracts of BM4405, whereas a serine racemase activity was found in the membrane preparation. This new type of acquired glycopeptide resistance was named VanE.


1990 ◽  
Vol 11 (3) ◽  
pp. 181-186 ◽  
Author(s):  
KENICHI HAGIWARA ◽  
TAKESHI SAKAI ◽  
AKIKO MIWA ◽  
NOBUFUMI KAWAI ◽  
TERUMI NAKAJIMA

FEBS Letters ◽  
1985 ◽  
Vol 181 (1) ◽  
pp. 154-156 ◽  
Author(s):  
D.D. Sheumack ◽  
R. Claassens ◽  
N.M. Whiteley ◽  
M.H.H. Howden

1985 ◽  
Vol 225 (1) ◽  
pp. 239-247 ◽  
Author(s):  
J A Gatehouse ◽  
J Gilroy ◽  
M S Hoque ◽  
R R D Croy

The seeds of pea (Pisum sativum L.) contain several proteins in the albumin solubility fraction that are significant components of total cotyledonary protein (5-10%) and are accumulated in developing seeds concurrently with storage-protein synthesis. One of these proteins, of low Mr and designated ‘Psa LA’, has been purified, characterized and sequenced. Psa LA has an Mr of 11000 and contains polypeptides of Mr 6000, suggesting that the protein molecules are dimeric. The amino acid sequence contains 54 residues, with a high content (10/54) of asparagine/aspartate. It has no inhibitory action towards trypsin or chymotrypsin, and is distinct from the inhibitors of those enzymes found in pea seeds, nor does it inhibit hog pancreatic alpha-amylase. The protein contains no methionine, but significant amounts of cysteine (four residues per polypeptide), suggesting a possible role as a sulphur storage protein. However, its sequence is not homologous with low-Mr (2S) storage proteins from castor bean (Ricinus communis) or rape (Brassica napus). Psa LA therefore represents a new type of low-Mr seed protein.


1990 ◽  
Vol 265 (26) ◽  
pp. 15770-15775 ◽  
Author(s):  
H. Yamashita ◽  
S. Theerasilp ◽  
T. Aiuchi ◽  
K. Nakaya ◽  
Y. Nakamura ◽  
...  

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