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2-Carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase: evidence for a wider role in plant Rubisco regulation

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

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2-Carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase: evidence for a wider role in plant Rubisco regulation. / Andralojc, Paul John; Madgwick, Pippa J.; Tao, Yong et al.
In: Biochemical Journal, Vol. 442, No. 3, 15.03.2012, p. 733-742.

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

Harvard

Andralojc, PJ, Madgwick, PJ, Tao, Y, Keys, A, Ward, JL, Beale, MH, Loveland, JE, Jackson, PJ, Willis, AC, Gutteridge, S & Parry, MAJ 2012, '2-Carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase: evidence for a wider role in plant Rubisco regulation', Biochemical Journal, vol. 442, no. 3, pp. 733-742. https://doi.org/10.1042/BJ20111443

APA

Andralojc, P. J., Madgwick, P. J., Tao, Y., Keys, A., Ward, J. L., Beale, M. H., Loveland, J. E., Jackson, P. J., Willis, A. C., Gutteridge, S., & Parry, M. A. J. (2012). 2-Carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase: evidence for a wider role in plant Rubisco regulation. Biochemical Journal, 442(3), 733-742. https://doi.org/10.1042/BJ20111443

Vancouver

Andralojc PJ, Madgwick PJ, Tao Y, Keys A, Ward JL, Beale MH et al. 2-Carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase: evidence for a wider role in plant Rubisco regulation. Biochemical Journal. 2012 Mar 15;442(3):733-742. doi: 10.1042/BJ20111443

Author

Andralojc, Paul John ; Madgwick, Pippa J. ; Tao, Yong et al. / 2-Carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase : evidence for a wider role in plant Rubisco regulation. In: Biochemical Journal. 2012 ; Vol. 442, No. 3. pp. 733-742.

Bibtex

@article{f5ff54e453054c3baf8c9e6e637a3022,
title = "2-Carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase: evidence for a wider role in plant Rubisco regulation",
abstract = "The genes for CA1Pase (2-carboxy-D-arabinitol-1-bisphosphate phosphatase) from French bean, wheat, Arabidopsis and tobacco were identified and cloned. The deduced protein sequence included an N-terminal motif identical with the PGM (phosphoglycerate mutase) active site sequence [LIVM]-x-R-H-G-[EQ]-x-x-[WN]. The corresponding gene from wheat coded for an enzyme with the properties published for CA1Pase. The expressed protein lacked PGM activity but rapidly dephosphorylated 2,3-DPG (2,3-diphosphoglycerate) to 2-phosphoglycerate. DTT (dithiothreitol) activation and GSSG inactivation of this enzyme was pH-sensitive, the greatest difference being apparent at pH 8. The presence of the expressed protein during in vitro measurement of Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) activity prevented a progressive decline in Rubisco turnover. This was due to the removal of an inhibitory bisphosphate that was present in the RuBP (ribulose-1,5-bisphosphate) preparation, and was found to be PDBP (D-glycero-2,3-pentodiulose-1,5- bisphosphate). The substrate specificity of the expressed protein indicates a role for CA1Pase in the removal of 'misfire' products of Rubisco.",
keywords = "2-carboxyarabinitol 1-phosphate (CA1P), D-glycero-2,3-pentodiulose-1,5- bisphosphate (PDBP) phosphatase, Ribulose- 1,5-bisphosphate carboxylase/oxygenase (Rubisco)",
author = "Andralojc, {Paul John} and Madgwick, {Pippa J.} and Yong Tao and Alfred Keys and Ward, {Jane L.} and Beale, {Michael H.} and Loveland, {Jane E.} and Jackson, {Phil J.} and Willis, {Antony C.} and Steven Gutteridge and Parry, {Martin A. J.}",
year = "2012",
month = mar,
day = "15",
doi = "10.1042/BJ20111443",
language = "English",
volume = "442",
pages = "733--742",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "3",

}

RIS

TY - JOUR

T1 - 2-Carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase

T2 - evidence for a wider role in plant Rubisco regulation

AU - Andralojc, Paul John

AU - Madgwick, Pippa J.

AU - Tao, Yong

AU - Keys, Alfred

AU - Ward, Jane L.

AU - Beale, Michael H.

AU - Loveland, Jane E.

AU - Jackson, Phil J.

AU - Willis, Antony C.

AU - Gutteridge, Steven

AU - Parry, Martin A. J.

PY - 2012/3/15

Y1 - 2012/3/15

N2 - The genes for CA1Pase (2-carboxy-D-arabinitol-1-bisphosphate phosphatase) from French bean, wheat, Arabidopsis and tobacco were identified and cloned. The deduced protein sequence included an N-terminal motif identical with the PGM (phosphoglycerate mutase) active site sequence [LIVM]-x-R-H-G-[EQ]-x-x-[WN]. The corresponding gene from wheat coded for an enzyme with the properties published for CA1Pase. The expressed protein lacked PGM activity but rapidly dephosphorylated 2,3-DPG (2,3-diphosphoglycerate) to 2-phosphoglycerate. DTT (dithiothreitol) activation and GSSG inactivation of this enzyme was pH-sensitive, the greatest difference being apparent at pH 8. The presence of the expressed protein during in vitro measurement of Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) activity prevented a progressive decline in Rubisco turnover. This was due to the removal of an inhibitory bisphosphate that was present in the RuBP (ribulose-1,5-bisphosphate) preparation, and was found to be PDBP (D-glycero-2,3-pentodiulose-1,5- bisphosphate). The substrate specificity of the expressed protein indicates a role for CA1Pase in the removal of 'misfire' products of Rubisco.

AB - The genes for CA1Pase (2-carboxy-D-arabinitol-1-bisphosphate phosphatase) from French bean, wheat, Arabidopsis and tobacco were identified and cloned. The deduced protein sequence included an N-terminal motif identical with the PGM (phosphoglycerate mutase) active site sequence [LIVM]-x-R-H-G-[EQ]-x-x-[WN]. The corresponding gene from wheat coded for an enzyme with the properties published for CA1Pase. The expressed protein lacked PGM activity but rapidly dephosphorylated 2,3-DPG (2,3-diphosphoglycerate) to 2-phosphoglycerate. DTT (dithiothreitol) activation and GSSG inactivation of this enzyme was pH-sensitive, the greatest difference being apparent at pH 8. The presence of the expressed protein during in vitro measurement of Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) activity prevented a progressive decline in Rubisco turnover. This was due to the removal of an inhibitory bisphosphate that was present in the RuBP (ribulose-1,5-bisphosphate) preparation, and was found to be PDBP (D-glycero-2,3-pentodiulose-1,5- bisphosphate). The substrate specificity of the expressed protein indicates a role for CA1Pase in the removal of 'misfire' products of Rubisco.

KW - 2-carboxyarabinitol 1-phosphate (CA1P)

KW - D-glycero-2,3-pentodiulose-1,5- bisphosphate (PDBP) phosphatase

KW - Ribulose- 1,5-bisphosphate carboxylase/oxygenase (Rubisco)

U2 - 10.1042/BJ20111443

DO - 10.1042/BJ20111443

M3 - Journal article

C2 - 22132794

AN - SCOPUS:84857864015

VL - 442

SP - 733

EP - 742

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 3

ER -