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Mutations in loop six of the large subunit of ribulose-1,5-bisphosphate carboxylase affect substrate specificity

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

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Mutations in loop six of the large subunit of ribulose-1,5-bisphosphate carboxylase affect substrate specificity. / Parry, M. A. J.; Madgwick, P.; Parmar, S. et al.
In: Planta, Vol. 187, No. 1, 04.1992, p. 109-112.

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

Harvard

Parry, MAJ, Madgwick, P, Parmar, S, Cornelius, MJ & Keys, AJ 1992, 'Mutations in loop six of the large subunit of ribulose-1,5-bisphosphate carboxylase affect substrate specificity', Planta, vol. 187, no. 1, pp. 109-112. https://doi.org/10.1007/BF00201631

APA

Parry, M. A. J., Madgwick, P., Parmar, S., Cornelius, M. J., & Keys, A. J. (1992). Mutations in loop six of the large subunit of ribulose-1,5-bisphosphate carboxylase affect substrate specificity. Planta, 187(1), 109-112. https://doi.org/10.1007/BF00201631

Vancouver

Parry MAJ, Madgwick P, Parmar S, Cornelius MJ, Keys AJ. Mutations in loop six of the large subunit of ribulose-1,5-bisphosphate carboxylase affect substrate specificity. Planta. 1992 Apr;187(1):109-112. doi: 10.1007/BF00201631

Author

Parry, M. A. J. ; Madgwick, P. ; Parmar, S. et al. / Mutations in loop six of the large subunit of ribulose-1,5-bisphosphate carboxylase affect substrate specificity. In: Planta. 1992 ; Vol. 187, No. 1. pp. 109-112.

Bibtex

@article{b83d30be6764471abeab7e167dc164b8,
title = "Mutations in loop six of the large subunit of ribulose-1,5-bisphosphate carboxylase affect substrate specificity",
abstract = "Mutagenesis in vitro of the gene encoding the large subunit of ribulose-1,5-bisphosphate carboxylase/ oxygenase (EC 4.1.1.39) from Anacystis nidulansSynechococcus PCC 6301) was used to generate novel enzymes in Escherichia coli. Residues in C-terminal loop 6 of the β/α barrel structure of the large subunit were changed. Replacement of valine 331 with alanine caused a 90% reduction in Vmax but did not alter the enzyme's relative specificity towards either of its gaseous substrates, CO2 and O2. However replacement of alanine 340 with glutamate decreased the enzyme's specificity for CO2 but had no significant effect on either the Km for ribulose-1,5-bisphosphate or CO2 or on Vmax. In contrast replacing a small cassette of residues 338-341 produced a small increase in the specificity factor.",
keywords = "Gene mutation, Ribulose-1,5-bisphosphate carboxylase, Specificity factor",
author = "Parry, {M. A. J.} and P. Madgwick and S. Parmar and Cornelius, {M. J.} and Keys, {A. J.}",
year = "1992",
month = apr,
doi = "10.1007/BF00201631",
language = "English",
volume = "187",
pages = "109--112",
journal = "Planta",
issn = "0032-0935",
publisher = "Springer",
number = "1",

}

RIS

TY - JOUR

T1 - Mutations in loop six of the large subunit of ribulose-1,5-bisphosphate carboxylase affect substrate specificity

AU - Parry, M. A. J.

AU - Madgwick, P.

AU - Parmar, S.

AU - Cornelius, M. J.

AU - Keys, A. J.

PY - 1992/4

Y1 - 1992/4

N2 - Mutagenesis in vitro of the gene encoding the large subunit of ribulose-1,5-bisphosphate carboxylase/ oxygenase (EC 4.1.1.39) from Anacystis nidulansSynechococcus PCC 6301) was used to generate novel enzymes in Escherichia coli. Residues in C-terminal loop 6 of the β/α barrel structure of the large subunit were changed. Replacement of valine 331 with alanine caused a 90% reduction in Vmax but did not alter the enzyme's relative specificity towards either of its gaseous substrates, CO2 and O2. However replacement of alanine 340 with glutamate decreased the enzyme's specificity for CO2 but had no significant effect on either the Km for ribulose-1,5-bisphosphate or CO2 or on Vmax. In contrast replacing a small cassette of residues 338-341 produced a small increase in the specificity factor.

AB - Mutagenesis in vitro of the gene encoding the large subunit of ribulose-1,5-bisphosphate carboxylase/ oxygenase (EC 4.1.1.39) from Anacystis nidulansSynechococcus PCC 6301) was used to generate novel enzymes in Escherichia coli. Residues in C-terminal loop 6 of the β/α barrel structure of the large subunit were changed. Replacement of valine 331 with alanine caused a 90% reduction in Vmax but did not alter the enzyme's relative specificity towards either of its gaseous substrates, CO2 and O2. However replacement of alanine 340 with glutamate decreased the enzyme's specificity for CO2 but had no significant effect on either the Km for ribulose-1,5-bisphosphate or CO2 or on Vmax. In contrast replacing a small cassette of residues 338-341 produced a small increase in the specificity factor.

KW - Gene mutation

KW - Ribulose-1,5-bisphosphate carboxylase

KW - Specificity factor

U2 - 10.1007/BF00201631

DO - 10.1007/BF00201631

M3 - Journal article

AN - SCOPUS:0001687699

VL - 187

SP - 109

EP - 112

JO - Planta

JF - Planta

SN - 0032-0935

IS - 1

ER -