A point mutation in the N-terminus of ribulose-1,5-bisphosphate carboxylase affects ribulose-1,5-bisphosphate binding

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https://doi.org/10.1007/BF00208233
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Keywords

1,5-bisphosphate carboxylase, Gene mutation (N-terminus), Ribulose, Substrate affinity (ribulose-1,5-bisphosphate)

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A point mutation in the N-terminus of ribulose-1,5-bisphosphate carboxylase affects ribulose-1,5-bisphosphate binding. / Kettleborough, C. A.; Phillips, A. L.; Keys, A. J. et al.
In: Planta, Vol. 184, No. 1, 01.04.1991, p. 35-39.

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

Bibtex

@article{f3388ae719a4455ca5153b9c53836782,

title = "A point mutation in the N-terminus of ribulose-1,5-bisphosphate carboxylase affects ribulose-1,5-bisphosphate binding",

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 nidulans was used to generate novel enzymes. Two conserved residues, threonine 4 and lysine 11 in the N-terminus were changed. The substitution of threonine 4 with serine or valine had little effect on the kinetic parameters. The substitution of lysine 11 with leucine, which is non-polar, increased the Km for ribulose-1,5-bisphosphate from 82 to 190 μM but its replacement with glutamine, which has polar properties, had no appreciable effect.",

keywords = "1,5-bisphosphate carboxylase, Gene mutation (N-terminus), Ribulose, Substrate affinity (ribulose-1,5-bisphosphate)",

author = "Kettleborough, {C. A.} and Phillips, {A. L.} and Keys, {A. J.} and Parry, {M. A.}",

year = "1991",

month = apr,

day = "1",

doi = "10.1007/BF00208233",

language = "English",

volume = "184",

pages = "35--39",

journal = "Planta",

issn = "0032-0935",

publisher = "Springer",

number = "1",

}

RIS

TY - JOUR

T1 - A point mutation in the N-terminus of ribulose-1,5-bisphosphate carboxylase affects ribulose-1,5-bisphosphate binding

AU - Kettleborough, C. A.

AU - Phillips, A. L.

AU - Keys, A. J.

AU - Parry, M. A.

PY - 1991/4/1

Y1 - 1991/4/1

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 nidulans was used to generate novel enzymes. Two conserved residues, threonine 4 and lysine 11 in the N-terminus were changed. The substitution of threonine 4 with serine or valine had little effect on the kinetic parameters. The substitution of lysine 11 with leucine, which is non-polar, increased the Km for ribulose-1,5-bisphosphate from 82 to 190 μM but its replacement with glutamine, which has polar properties, had no appreciable effect.

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 nidulans was used to generate novel enzymes. Two conserved residues, threonine 4 and lysine 11 in the N-terminus were changed. The substitution of threonine 4 with serine or valine had little effect on the kinetic parameters. The substitution of lysine 11 with leucine, which is non-polar, increased the Km for ribulose-1,5-bisphosphate from 82 to 190 μM but its replacement with glutamine, which has polar properties, had no appreciable effect.

KW - 1,5-bisphosphate carboxylase

KW - Gene mutation (N-terminus)

KW - Ribulose

KW - Substrate affinity (ribulose-1,5-bisphosphate)

UR - http://www.scopus.com/inward/record.url?scp=0343315591&partnerID=8YFLogxK

U2 - 10.1007/BF00208233

DO - 10.1007/BF00208233

M3 - Journal article

AN - SCOPUS:0343315591

VL - 184

SP - 35

EP - 39

JO - Planta

JF - Planta

SN - 0032-0935

IS - 1

ER -

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