2'-carboxy-D-arabitinol 1-phosphate protects ribulose 1,5-bisphosphate carboxylase/oxygenase against proteolytic breakdown

Lancaster Environment Centre

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https://doi.org/10.1046/j.1432-1327.1999.00913.x
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Keywords

2'-carboxy-D-arabitinol 1-phosphate, Photosynthesis, Proteolysis, Ribulose 1,5-bisphosphate carboxylase/oxygenase, Stromal protease

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Research output: Contribution to Journal/Magazine › Journal article › peer-review

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2'-carboxy-D-arabitinol 1-phosphate protects ribulose 1,5-bisphosphate carboxylase/oxygenase against proteolytic breakdown. / Khan, Shahnaz; Andralojc, P. John; Lea, Peter J. et al.
In: European Journal of Biochemistry, Vol. 266, No. 3, 15.12.1999, p. 840-847.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Bibtex

@article{ccfa40b9697e4c92810133fefa189160,

title = "2'-carboxy-D-arabitinol 1-phosphate protects ribulose 1,5-bisphosphate carboxylase/oxygenase against proteolytic breakdown",

abstract = "Trypsin-catalysed cleavage of purified ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) and the resultant irreversible loss of carboxylase activity were prevented by prior incubation with the naturally occurring nocturnal Rubisco inhibitor 2'-carboxy-D-arabitinol 1-phosphate (CA1P), as well as with ribulose 1,5-bisphosphate (RuBP), Mg2+ and CO2, CA1P also protected Rubisco from loss of activity caused by carboxypeptidase A. When similar experiments were carried out using soluble chloroplast proteases, CA1P was again able to protect Rubisco against proteolytic degradation and the consequent irreversible loss of catalytic activity. Thus, CA1P prevents the proteolytic breakdown of Rubisco by endogenous and exogenous proteases. In this way, CA1P may affect the amounts of Rubisco protein available for photosynthetic CO2 assimilation. Rubisco turnover (in the presence of RuBP, Mg2+ and CO2) may confer similar protection against proteases in the light.",

keywords = "2'-carboxy-D-arabitinol 1-phosphate, Photosynthesis, Proteolysis, Ribulose 1,5-bisphosphate carboxylase/oxygenase, Stromal protease",

author = "Shahnaz Khan and Andralojc, {P. John} and Lea, {Peter J.} and Parry, {Martin A J}",

year = "1999",

month = dec,

day = "15",

doi = "10.1046/j.1432-1327.1999.00913.x",

language = "English",

volume = "266",

pages = "840--847",

journal = "European Journal of Biochemistry",

issn = "0014-2956",

publisher = "Wiley-Blackwell",

number = "3",

}

RIS

TY - JOUR

T1 - 2'-carboxy-D-arabitinol 1-phosphate protects ribulose 1,5-bisphosphate carboxylase/oxygenase against proteolytic breakdown

AU - Khan, Shahnaz

AU - Andralojc, P. John

AU - Lea, Peter J.

AU - Parry, Martin A J

PY - 1999/12/15

Y1 - 1999/12/15

N2 - Trypsin-catalysed cleavage of purified ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) and the resultant irreversible loss of carboxylase activity were prevented by prior incubation with the naturally occurring nocturnal Rubisco inhibitor 2'-carboxy-D-arabitinol 1-phosphate (CA1P), as well as with ribulose 1,5-bisphosphate (RuBP), Mg2+ and CO2, CA1P also protected Rubisco from loss of activity caused by carboxypeptidase A. When similar experiments were carried out using soluble chloroplast proteases, CA1P was again able to protect Rubisco against proteolytic degradation and the consequent irreversible loss of catalytic activity. Thus, CA1P prevents the proteolytic breakdown of Rubisco by endogenous and exogenous proteases. In this way, CA1P may affect the amounts of Rubisco protein available for photosynthetic CO2 assimilation. Rubisco turnover (in the presence of RuBP, Mg2+ and CO2) may confer similar protection against proteases in the light.

AB - Trypsin-catalysed cleavage of purified ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) and the resultant irreversible loss of carboxylase activity were prevented by prior incubation with the naturally occurring nocturnal Rubisco inhibitor 2'-carboxy-D-arabitinol 1-phosphate (CA1P), as well as with ribulose 1,5-bisphosphate (RuBP), Mg2+ and CO2, CA1P also protected Rubisco from loss of activity caused by carboxypeptidase A. When similar experiments were carried out using soluble chloroplast proteases, CA1P was again able to protect Rubisco against proteolytic degradation and the consequent irreversible loss of catalytic activity. Thus, CA1P prevents the proteolytic breakdown of Rubisco by endogenous and exogenous proteases. In this way, CA1P may affect the amounts of Rubisco protein available for photosynthetic CO2 assimilation. Rubisco turnover (in the presence of RuBP, Mg2+ and CO2) may confer similar protection against proteases in the light.

KW - 2'-carboxy-D-arabitinol 1-phosphate

KW - Photosynthesis

KW - Proteolysis

KW - Ribulose 1,5-bisphosphate carboxylase/oxygenase

KW - Stromal protease

UR - http://www.scopus.com/inward/record.url?scp=0033573109&partnerID=8YFLogxK

U2 - 10.1046/j.1432-1327.1999.00913.x

DO - 10.1046/j.1432-1327.1999.00913.x

M3 - Journal article

C2 - 10583377

AN - SCOPUS:0033573109

VL - 266

SP - 840

EP - 847

JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

SN - 0014-2956

IS - 3

ER -

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