Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Previous studies reached different conclusions about whether class I hyaluronan synthases (HASs) elongate hyaluronic acid (HA) by addition to the reducing or the nonreducing end. Here we used two strategies to determine the direction of HA synthesis by purified class I HASs from Streptococcus equisimilis and Streptococcus pyogenes. In the first strategy we used each of the two UDP-sugar substrates separately to pulse label either the beginning or the end of HA chains. We then quantified the relative rates of radioactive HA degradation by treatment with beta-glycosidases that act at the nonreducing end. The results with both purified HASs demonstrated that HA elongation occurred at the reducing end. In the second strategy, we used purified S. equisimilis HAS, UDP-glucuronic acid, and UDP[beta-32P]-Glc-NAc to radiolabel nascent HA chains. Under conditions of limiting substrate, the 32P-labeled products were separated from the substrates by paper chromatography and identified as HA-[32P]UDP saccharides based on their degradation by snake venom phosphodiesterase or hyaluronidase and by their binding to a specific HA-binding protein. The 32P radioactivity was chased (released) by incubation with unlabeled UDP-sugars, showing that the HA-UDP linkages turn over during HA biosynthesis. In contrast, HA-[32P]UDP products made by the purified class II Pasteurella multocida HAS were not released by adding unlabeled UDP-sugars, consistent with growth at the nonreducing end for this enzyme. The results demonstrate that the streptococcal class I HAS enzymes polymerize HA chains at the reducing end.
 ...
PMID:Hyaluronan biosynthesis by class I streptococcal hyaluronan synthases occurs at the reducing end. 1566 42

When considering the proteins and toxins in snake venom one's thoughts generally migrate to the proteinases, neurotoxins and phospholipases since these families of proteins are comprised by many of the toxins found in venom. However as modern proteomic and transcriptomic venom research has abundantly shown snake venoms are complex and containing numerous families of protein beyond the "big three". In this brief review we will discuss three of the lesser discussed proteins typically found in snake venoms: l-amino acid oxidases (LAAO); hyaluronidases and phosphodiesterases. These proteins have long been known to be part of many venoms' proteomes with reports appearing in the literature as early as 1944 for LAAO, 1947 for hyaluronidase (spreading factor), and 1932 for venom phosphodiesterase. These are more or less contemporary with the first reports (circa 1950) on snake venom proteases. Thus, the relatively modest literature on these snake venom proteins stems not from lack of early discovery but rather more likely to their ostensibly minor role in snake venom pathophysiology. In this review we will provide an overview of the experimental history of these venom proteins, their biochemical and structural features and their role in snake venom toxinology with the aim of bringing a fuller, more comprehensive, understanding of the history of laboratory research on snake venoms. In addition, there are some comments on these proteins from investigators who were actively engaged in their investigation.
 ...
PMID:A brief review of the scientific history of several lesser-known snake venom proteins: l-amino acid oxidases, hyaluronidases and phosphodiesterases. 2301 Jan 65