Phospholipid dependence and liposome reconstitution of purified hyaluronan synthase.

Phospholipid dependence and liposome reconstitution of purified hyaluronan synthase. Research Abstract Details 

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Phospholipid dependence and liposome reconstitution of purified hyaluronan synthase. Abstract Text:

Paul H Weigel,Zhetcho Kyossev,Lindsey C Torres,

Previous radiation inactivation and enzyme characterization studies demonstrated that the Streptococcus equisimilis hyaluronan synthase (seHAS) is phospholipid-dependent and that cardiolipin (CL) is the best phospholipid for enzyme activation. Here we investigated the ability of seHAS, purified in the absence of added lipid, to be activated by synthetic phosphatidic acid (PA), phosphatidylserine, or CL lipids containing fatty acyl chains of different length or different numbers of double bonds. The most effective lipid was tetraoleoyl CL (TO-CL), whereas tetramyristoyl CL (TM-CL) was ineffective. None of the phosphatidylserine species tested gave significant activation. PAs containing C10 to C18 saturated acyl chains were not effective activators, and neither were oleoyl lyso PA, dilinoleoyl PA, or PA containing one oleoyl chain and either a palmitoyl or stearoyl chain. In contrast, dioleoyl PA stimulated seHAS approximately 10-fold, to approximately 20% of the activity observed with TO-CL. The tested acidic lipids such as PA and CL activated the enzyme most efficiently if they contained only oleic acid. Mixing experiments showed that the enzyme interacts preferentially with TO-CL in the presence of TM-CL. Similarly, seHAS incorporated into phosphotidylcholine-based liposomes showed increasing activity with increasing TO-CL, but not TM-CL, content. Inactivation of membrane-bound seHAS by solubilization with Nonidet P-40 was prevented by TO-CL, but not TM-CL. The pH dependence of seHAS in the presence of synthetic or naturally occurring CLs showed the same pattern of lipid preference between pH 6 and 10.5. Unexpectedly, HAS showed lipid-independent activity at pH 11.5. The results suggest that Class I HAS enzymes are lipid-dependent and that assembly of active seHAS-lipid complexes has high specificity for the phospholipid head group and the nature of the fatty acyl chains.

Phospholipid dependence and liposome reconstitution of purified hyaluronan synthase. Publishing Authors By Initials

PH Weigel,Z Kyossev,LC Torres,

For similar bacteria: gram-positive bacteria: gram-positive cocci: streptococcaceae: streptococcus research abstracts see: bacteria: gram-positive bacteria: gram-positive cocci: streptococcaceae: streptococcus research

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Phospholipid dependence and liposome reconstitution of purified hyaluronan synthase. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: The Journal of biological chemistry

VOLUME: 281

Page Numbers: 36542-51

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 19

MONTH: 09

YEAR: 2006

Phospholipid dependence and liposome reconstitution of purified hyaluronan synthase. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Phospholipid dependence and liposome reconstitution of purified hyaluronan synthase. Keywords Mesh Terms:

KEYWORDS: Streptococcus

MESH TERMS: enzymology

Chemical & Substance for Abstract: Phospholipid dependence and liposome reconstitution of purified hyaluronan synthase. Information

Substance Name: hyaluronan synthase

Registry Number: EC 2.4.1.212

Grant and Affiliation Information for Phospholipid dependence and liposome reconstitution of purified hyaluronan synthase.

AFFILIATION: Department of Biochemistry and Molecular Biology, the Oklahoma Center for Medical Glycobiology, Oklahoma City, Oklahoma 73190, USA. paul-weigel@ouhsc.edu

Country: United States

AGENCY: United States NIGMS

GRANT: GM35978

ACRONYM: GM

MEDLINETA: J Biol Chem

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