Knowledge Center Catalog

High substrate specificity factor ribulose bisphosphate carboxylase/oxygenase from eukaryotic marine algae and properties of recombinant cyanobacterial rubisco containing "algal" residue modifications (Record no. 21854)

MARC details
000 -LEADER
fixed length control field 02692nab a22003017a 4500
001 - CONTROL NUMBER
control field G73953
003 - CONTROL NUMBER IDENTIFIER
control field MX-TxCIM
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20170719110428.0
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 121211b |||p||p||||||| |z||| |
022 0# - INTERNATIONAL STANDARD SERIAL NUMBER
International Standard Serial Number 0003-9861
040 ## - CATALOGING SOURCE
Original cataloging agency MX-TxCIM
082 04 - DEWEY DECIMAL CLASSIFICATION NUMBER
Classification number 95-099210
100 1# - MAIN ENTRY--PERSONAL NAME
Personal name Read, B.A.
245 00 - TITLE STATEMENT
Title High substrate specificity factor ribulose bisphosphate carboxylase/oxygenase from eukaryotic marine algae and properties of recombinant cyanobacterial rubisco containing "algal" residue modifications
260 ## - PUBLICATION, DISTRIBUTION, ETC. (IMPRINT)
Date of publication, distribution, etc. 1994
340 ## - PHYSICAL MEDIUM
Material base and configuration Printed
500 ## - GENERAL NOTE
General note references US (DNAL 381 Ar2)
520 ## - SUMMARY, ETC.
Summary, etc. Marine algae play an important role in removing carbon dioxide from the atmosphere. In this investigation, we have determined the substrate specificity factor of ribulose 1,5-bisphosphate carboxylase/oxygenase from several marine chromophytic and rhodophytic algae. The enzymes were purified to homogeneity and all possessed significantly higher substrate specificity factors than the enzymes from terrestrial plants, green algae, or bacteria. There are substantial differences in the sequence in a helix 6 of the large subunit of these enzymes, which is intriguing since residues of this region had been previously shown to influence the ability of ribulose bisphosphate carboxylase to discriminate between CO2 and O2, presumably by influencing the adjacent flexible loop 6 region. Sequence divergence at this and other key regions might contribute to the substantial differences in the substrate specificity factor of the chromophyte/rhodophyte enzyme. Initial studies on probing the basis for the high substrate specificity factor employed single amino acid substitutions in the recombinant cyanobacterial ribulose bisphosphate carboxylase. Residues in the vicinity of loop 6 were changed to reflect the corresponding residues in the chromophyte/rhodophyte large subunit. Some changes in the substrate specificity factor were noted, as were alterations in other important kinetic parameters. Since marine algae show little evidence of photorespiratory metabolism, the high substrate specificity of ribulose bisphosphate carboxylase is consistent with the physiology of these organisms. The results of this study provide further evidence that the properties of this enzyme may evolve or change according to the environment in which the host organism is found
546 ## - LANGUAGE NOTE
Language note English
595 ## - COLLECTION
Collection AGRIS Collection
650 10 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Chemicophysical properties
650 10 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Enzymes
650 10 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Lyases
650 10 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Plant physiology and biochemistry
700 1# - ADDED ENTRY--PERSONAL NAME
Personal name Tabita, F.R.,
Relator term coaut.
773 0# - HOST ITEM ENTRY
Title Archives of biochemistry and biophysics (USA). (Jul 1994). v. 312(1) p. 210-218
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Koha item type Article
Holdings
Date last seen Total Checkouts Full call number Price effective from Koha item type Lost status Damaged status Not for loan Collection code Withdrawn status Home library Current library Date acquired
07/19/2017   95-099210 07/19/2017 Article Not Lost     AGRIS Collection   CIMMYT Knowledge Center: John Woolston Library CIMMYT Knowledge Center: John Woolston Library 07/19/2017

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