Studies on the mechanism of hyaluronate lyase action.

Abstract:

:Hyaluronate lyase from streptococci group A was purified by chromatography on DEAE-Sephadex A-50 and on Biogel P-150, thereby enriching it about 1,000-fold and separating it into two enzyme fractions with the same amino acid composition. The photooxidation of hyaluronate lyase in the presence of methylene blue results in rapid inactivation of the enzyme. The histidine content of the enzyme is decreased considerably, but also the content of methionine, tyrosine, and lysine is lowered. The enzyme is inhibited, but incompletely so, by N-tosyl-L-phenyl-alanine-chloromethyl ketone (TPCK) and N-alpha-p-tosyl-L-lysine chloromethyl ketone (TLCK). Hyaluronic acid methyl ester, prepared form hyaluronic acid and diazomethane, is not split by hyaluronate lyase (EC 4.2.2.1.). Hyaluronic acid methyl ester is not a competitive inhibitor of hyaluronate lyase. For the mechanism of the enzymatic elimination reaction a proton transfer between histidine of the enzyme and the carboxylate group of hyaluronate is proposed.

journal_name

Connect Tissue Res

authors

Greiling H,Stuhlsatz HW,Eberhard T,Eberhard A

doi

10.3109/03008207509152171

keywords:

subject

Has Abstract

pub_date

1975-01-01 00:00:00

pages

135-9

issue

2

eissn

0300-8207

issn

1607-8438

journal_volume

3

pub_type

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