scholarly journals Platelet-Activating Factor Acetylhydrolases:  Broad Substrate Specificity and Lipoprotein Binding Does Not Modulate the Catalytic Properties of the Plasma Enzyme

Biochemistry ◽  
2001 ◽  
Vol 40 (15) ◽  
pp. 4539-4549 ◽  
Author(s):  
Jung-Hyun Min ◽  
Cheryl Wilder ◽  
Junken Aoki ◽  
Hiroyuki Arai ◽  
Keizo Inoue ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Catalytic Properties ◽  
Platelet Activating Factor ◽  
Broad Substrate Specificity ◽  
Plasma Enzyme ◽  
Lipoprotein Binding

scholarly journals LASS3 (longevity assurance homologue 3) is a mainly testis-specific (dihydro)ceramide synthase with relatively broad substrate specificity

2006 ◽  
Vol 398 (3) ◽  
pp. 531-538 ◽  
Author(s):  
Yukiko Mizutani ◽  
Akio Kihara ◽  
Yasuyuki Igarashi
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Family Members ◽  
Fatty Acyl ◽  
Ceramide Synthase ◽  
Broad Substrate Specificity ◽  
Acid Protein ◽  
Amino Acid Protein

The LASS (longevity assurance homologue) family members are highly conserved from yeasts to mammals. Five mouse and human LASS family members, namely LASS1, LASS2, LASS4, LASS5 and LASS6, have been identified and characterized. In the present study we cloned two transcriptional variants of hitherto-uncharacterized mouse LASS3 cDNA, which encode a 384-amino-acid protein (LASS3) and a 419-amino-acid protein (LASS3-long). In vivo, [3H]dihydrosphingosine labelling and electrospray-ionization MS revealed that overproduction of either LASS3 isoform results in increases in several ceramide species, with some preference toward those having middle- to long-chain-fatty acyl-CoAs. A similar substrate preference was observed in an in vitro (dihydro)ceramide synthase assay. These results indicate that LASS3 possesses (dihydro)ceramide synthesis activity with relatively broad substrate specificity. We also found that, except for a weak display in skin, LASS3 mRNA expression is limited almost solely to testis, implying that LASS3 plays an important role in this gland.

scholarly journals TheArabidopsisAtSTE24 Is a CAAXProtease with Broad Substrate Specificity

2002 ◽  
Vol 277 (33) ◽  
pp. 29856-29864 ◽  
Author(s):  
Keren Bracha ◽  
Meirav Lavy ◽  
Shaul Yalovsky
Keyword(s):  
Substrate Specificity ◽  
Broad Substrate Specificity

scholarly journals Escherichia coli RNase D. Catalytic properties and substrate specificity.

1981 ◽  
Vol 256 (11) ◽  
pp. 5633-5637 ◽  
Author(s):  
H. Cudny ◽  
R. Zaniewski ◽  
M.P. Deutscher
Keyword(s):  
Escherichia Coli ◽  
Substrate Specificity ◽  
Catalytic Properties

Prediction of amino acid residues participated in substrate recognition by cytochrome P450 subfamilies with broad substrate specificity

2013 ◽  
Vol 26 (2) ◽  
pp. 86-91 ◽  
Author(s):  
Maria S. Zharkova ◽  
Boris N. Sobolev ◽  
Nina Yu. Oparina ◽  
Alexander V. Veselovsky ◽  
Alexander I. Archakov
Keyword(s):  
Cytochrome P450 ◽  
Amino Acid ◽  
Substrate Specificity ◽  
Substrate Recognition ◽  
Amino Acid Residues ◽  
Broad Substrate Specificity
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