Ninth Oxford Conference Organised by the Oxford International Biomedical Centre (OIBC)

Conference Report

Ninth Oxford Conference Organised by the Oxford International Biomedical Centre (OIBC)     

低温酶及其冷适应性机制研究进展

生活在极地、深海等常年低温环境中的低温微生物和部分变温生物,能够通过产生低温酶来适应在低温环境中的生长、繁殖和代谢。这些酶在低温或常温条件下具有很高的催化活性,对热却很敏感,在高温时能够快速失活,因此在实际的生产和生活中具有广泛的应用前景。基于这些特性,低温酶的冷适应性机制研究成为了当前的一个热点。较系统地综述了低温酶的来源、特点、生产状况以及具有代表性的几种低温酶的冷适应性机制。     

The Mechanisms and Time Factor of the Enzyme Structure of a Paleosoil

The data on the enzyme activity of paleosoils of archaeological sites are given. It is shown that the activity of phosphatases and urease in soils of ancient settlements is significantly higher than in modern soils: 1.5–2.0 times for urease and 7–15 times for phosphatase in some cultural layers of the Bronze Age. This is related to a large amount of organic material (garbage, rubbish, excrement, and urea), which entered the soil in ancient times and stimulated soil microorganisms to produce a greater amount of enzymes, whose high activity has been preserved for 4000 years. The location of the enzymes was determined by soil fumigation using chloroform and activation of extracellular enzymes by glycine. The release of intracellular enzymes as a result of fumigation caused a significant increase in phosphatase activity in modern soils and soils of ancient settlements in contrast to the virgin paleosoil of the Bronze Age. The treatment by glycine exerted a smaller effect on the activity of phosphatases, but caused a significant increase in urease activity. This may indicate the predominating extracellular localization of urease in paleosoils of ancient settlements, while phosphatase is characterized by both extra- and intracellular localization.

     

Crystal Structures and Enzyme Mechanisms of a Dual Fucose Mutarotase/Ribose Pyranase

Escherichia coli FucU (Fucose Unknown) is a dual fucose mutarotase and ribose pyranase, which shares 44% sequence identity with its human counterpart. Herein, we report the structures of E. coli FucU and mouse FucU bound to l-fucose and delineate the catalytic mechanisms underlying the interconversion between stereoisomers of fucose and ribose. E. coli FucU forms a decameric toroid with each active site formed by two adjacent subunits. While one subunit provides most of the fucose-interacting residues including a catalytic tyrosine residue, the other subunit provides a catalytic His-Asp dyad. This active-site feature is critical not only for the mutarotase activity toward l-fucose but also for the pyranase activity toward d-ribose. Structural and biochemical analyses pointed that mouse FucU assembles into four different oligomeric forms, among which the smallest homodimeric form is most abundant and would be the predominant species under physiological conditions. This homodimer has two fucose-binding sites that are devoid of the His-Asp dyad and catalytically inactive, indicating that the mutarotase and the pyranase activities appear dispensable in vertebrates. The defective assembly of the mouse FucU homodimer into the decameric form is due to an insertion of two residues at the N-terminal extreme, which is a common aspect of all the known vertebrate FucU proteins. Therefore, vertebrate FucU appears to serve for as yet unknown function through the quaternary structural alteration.     

Mechanisms of Hatching in Fish: Secretion of Hatching Enzyme and Enzymatic Choriolysis

SYNOPSIS. Mechanisms of two constituent steps of the hatchingprocess, i.e., secretion of hatching enzyme from the gland cellsand enzymatic choriolysis, in the Medaka, Oryzias latipes, aredescribed. The ultrastructural changes of the hatching glandcells occurring at the initiation of electrically induced secretionas well as of natural secretion were the swelling of each glandcell and the separation of joints of the epithelial cells coveringthe gland cells, followed by a resultant exposure of the apicalpart of the gland cells. These changes, though their triggeringmechanisms are not sufficiently clarified, suggest an interventionof some mechanical stimuli in the initiation of secretion. Decreasein electron density of the secretory granules also occurredimmediately prior to the initiation of secretion. The secreted hatching enzyme was found to dissolve the innerlayer of chorion by attacking the scleroprotein of the innerlayer at some restricted sites and liberating a group of solubleglycoproteins of high molecular weights. This selective digestionappears to be the reason why choriolysis proceeds efficientlyduring a short period of time at hatching.     

Enzyme Mechanisms in Temperature and Pressure Adaptation of Off-Shore Benthic Organisms: The Basic Problem

SYNOPSIS: The degree of participation of any given enzyme reactionin metabolism is not determined by energy-volume relationships,but rather by enzyme affinities for key regulatory ligands.In temperature adaptation, enzyme-substrate affinities oftendecrease as thermal kinetic energy increases, thus compensatingfor temperature-induced changes in reaction velocity at lowsubstrate concentrations. Since the effects of pressure arenot unidirectional (some enzymes are accelerated; some are unaffected;some are decelerated), a more functional solution in pressureadaptation is to elaborate enzymes whose affinities for keymetabolites are pressure independent. In consequence, at physiologicalsubstrate concentrations, the pressure sensitivities of catalysisand control of catalysis are probably held at a minimum.