Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus

Jun Hyuck Lee; Jungdon Bae; Dooil Kim; Yongseok Choi; Young Jun Im; Sukhoon Koh; Joong Su Kim; Mun Kyoung Kim; Gil Bu Kang; Suk In Hong; Dae Sil Lee; Soo Hyun Eom

doi:10.1016/j.bbrc.2006.06.139

Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus

Jun Hyuck Lee, Jungdon Bae, Dooil Kim, Yongseok Choi, Young Jun Im, Sukhoon Koh, Joong Su Kim, Mun Kyoung Kim, Gil Bu Kang, Suk In Hong, Dae Sil Lee, Soo Hyun Eom

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

Abstract

It was recently established that fructose-1,6-bisphosphate (FBP) aldolase (FBA) and tagatose-1,6-bisphosphate (TBP) aldolase (TBA), two class II aldolases, are highly specific for the diastereoselective synthesis of FBP and TBP from glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP), respectively. In this paper, we report on a FBA from the thermophile Thermus caldophilus GK24 (Tca) that produces both FBP and TBP from C₃ substrates. Moreover, the FBP:TBP ratio could be adjusted by manipulating the concentrations of G3P and DHAP. This is the first native FBA known to show dual diastereoselectivity among the FBAs and TBAs characterized thus far. To explain the behavior of this enzyme, the X-ray crystal structure of the Tca FBA in complex with DHAP was determined at 2.2 Å resolution. It appears that as a result of alteration of five G3P binding residues, the substrate binding cavity of Tca FBA has a greater volume than those in the Escherichia coli FBA-phosphoglycolohydroxamate (PGH) and TBA-PGH complexes. We suggest that this steric difference underlies the difference in the diastereoselectivities of these class II aldolases.

Original language	English
Pages (from-to)	616-625
Number of pages	10
Journal	Biochemical and biophysical research communications
Volume	347
Issue number	3
DOIs	https://doi.org/10.1016/j.bbrc.2006.06.139
Publication status	Published - 2006 Sept 1
Externally published	Yes

Bibliographical note

Funding Information:
We thank Professor N. Sakabe and Drs. N. Igarashi and N. Matsugaki for their kind support during data collection at BL18B of the Photon Factory (Tsukuba, Japan). We also thank Dr. H.-S. Lee and K.-H. Kim at BL6B of the Pohang Accelerator Laboratory (Pohang, Korea). This research was supported by a grant from the KRIBB Research Initiative Program.

Keywords

Crystal structure
Fructose-1,6-bisphosphate aldolase
Stereoselectivity
Tagatose-1,6-bisphosphate aldolase

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2006.06.139

Cite this

@article{3ecc0fabc7bd4fe7b803024bc25e5751,

title = "Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus",

abstract = "It was recently established that fructose-1,6-bisphosphate (FBP) aldolase (FBA) and tagatose-1,6-bisphosphate (TBP) aldolase (TBA), two class II aldolases, are highly specific for the diastereoselective synthesis of FBP and TBP from glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP), respectively. In this paper, we report on a FBA from the thermophile Thermus caldophilus GK24 (Tca) that produces both FBP and TBP from C3 substrates. Moreover, the FBP:TBP ratio could be adjusted by manipulating the concentrations of G3P and DHAP. This is the first native FBA known to show dual diastereoselectivity among the FBAs and TBAs characterized thus far. To explain the behavior of this enzyme, the X-ray crystal structure of the Tca FBA in complex with DHAP was determined at 2.2 {\AA} resolution. It appears that as a result of alteration of five G3P binding residues, the substrate binding cavity of Tca FBA has a greater volume than those in the Escherichia coli FBA-phosphoglycolohydroxamate (PGH) and TBA-PGH complexes. We suggest that this steric difference underlies the difference in the diastereoselectivities of these class II aldolases.",

keywords = "Crystal structure, Fructose-1,6-bisphosphate aldolase, Stereoselectivity, Tagatose-1,6-bisphosphate aldolase",

author = "Lee, {Jun Hyuck} and Jungdon Bae and Dooil Kim and Yongseok Choi and Im, {Young Jun} and Sukhoon Koh and Kim, {Joong Su} and Kim, {Mun Kyoung} and Kang, {Gil Bu} and Hong, {Suk In} and Lee, {Dae Sil} and Eom, {Soo Hyun}",

note = "Funding Information: We thank Professor N. Sakabe and Drs. N. Igarashi and N. Matsugaki for their kind support during data collection at BL18B of the Photon Factory (Tsukuba, Japan). We also thank Dr. H.-S. Lee and K.-H. Kim at BL6B of the Pohang Accelerator Laboratory (Pohang, Korea). This research was supported by a grant from the KRIBB Research Initiative Program.",

year = "2006",

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doi = "10.1016/j.bbrc.2006.06.139",

language = "English",

volume = "347",

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journal = "Biochemical and biophysical research communications",

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T1 - Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus

AU - Lee, Jun Hyuck

AU - Bae, Jungdon

AU - Kim, Dooil

AU - Choi, Yongseok

AU - Im, Young Jun

AU - Koh, Sukhoon

AU - Kim, Joong Su

AU - Kim, Mun Kyoung

AU - Kang, Gil Bu

AU - Hong, Suk In

AU - Lee, Dae Sil

AU - Eom, Soo Hyun

N1 - Funding Information: We thank Professor N. Sakabe and Drs. N. Igarashi and N. Matsugaki for their kind support during data collection at BL18B of the Photon Factory (Tsukuba, Japan). We also thank Dr. H.-S. Lee and K.-H. Kim at BL6B of the Pohang Accelerator Laboratory (Pohang, Korea). This research was supported by a grant from the KRIBB Research Initiative Program.

PY - 2006/9/1

Y1 - 2006/9/1

N2 - It was recently established that fructose-1,6-bisphosphate (FBP) aldolase (FBA) and tagatose-1,6-bisphosphate (TBP) aldolase (TBA), two class II aldolases, are highly specific for the diastereoselective synthesis of FBP and TBP from glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP), respectively. In this paper, we report on a FBA from the thermophile Thermus caldophilus GK24 (Tca) that produces both FBP and TBP from C3 substrates. Moreover, the FBP:TBP ratio could be adjusted by manipulating the concentrations of G3P and DHAP. This is the first native FBA known to show dual diastereoselectivity among the FBAs and TBAs characterized thus far. To explain the behavior of this enzyme, the X-ray crystal structure of the Tca FBA in complex with DHAP was determined at 2.2 Å resolution. It appears that as a result of alteration of five G3P binding residues, the substrate binding cavity of Tca FBA has a greater volume than those in the Escherichia coli FBA-phosphoglycolohydroxamate (PGH) and TBA-PGH complexes. We suggest that this steric difference underlies the difference in the diastereoselectivities of these class II aldolases.

AB - It was recently established that fructose-1,6-bisphosphate (FBP) aldolase (FBA) and tagatose-1,6-bisphosphate (TBP) aldolase (TBA), two class II aldolases, are highly specific for the diastereoselective synthesis of FBP and TBP from glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP), respectively. In this paper, we report on a FBA from the thermophile Thermus caldophilus GK24 (Tca) that produces both FBP and TBP from C3 substrates. Moreover, the FBP:TBP ratio could be adjusted by manipulating the concentrations of G3P and DHAP. This is the first native FBA known to show dual diastereoselectivity among the FBAs and TBAs characterized thus far. To explain the behavior of this enzyme, the X-ray crystal structure of the Tca FBA in complex with DHAP was determined at 2.2 Å resolution. It appears that as a result of alteration of five G3P binding residues, the substrate binding cavity of Tca FBA has a greater volume than those in the Escherichia coli FBA-phosphoglycolohydroxamate (PGH) and TBA-PGH complexes. We suggest that this steric difference underlies the difference in the diastereoselectivities of these class II aldolases.

KW - Crystal structure

KW - Fructose-1,6-bisphosphate aldolase

KW - Stereoselectivity

KW - Tagatose-1,6-bisphosphate aldolase

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DO - 10.1016/j.bbrc.2006.06.139

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AN - SCOPUS:33746210081

SN - 0006-291X

VL - 347

SP - 616

EP - 625

JO - Biochemical and biophysical research communications

JF - Biochemical and biophysical research communications

IS - 3

ER -

Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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