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Dr. Sang-Young Chun
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Dr. Che-Hun Jung TOP
Research Interests
1. reaction mechanism of mitochondrial glycerol
phosphate dehydrogenase
2. bio-hydrogen
3. proteomics of plant stress
4. redox regulation of enzymes/proteins
Selected Publications
Che-Hun Jung, Fred C. Hartman, Tse-Yuan S. Lu, and Frank W. Larimer (2000) "D-Ribose-5-phosphate
isomerase from spinach: heterologous.over-expression, purification, characterization, and site-directed
mutagenesis of the recombinant enzyme" Arch. Biochem. Biophys. 373(2), 409-417
Che-Hun Jung and William W. Wells (1998) "Spontaneous conversion of dehydroascorbic acid to ascorbic
acid and L-erythroascorbic acid" Arch. Biochem. Biophys. 354, 9-14
Che-Hun Jung and William W. Wells (1997) "Ascorbic acid is a stimulatory cofactor for mitochondrial
glycerol 3-phosphate dehydrogenase: a possible site of action of ascorbic acid in glucose-coupled
insulin release from pancreatic islets" Biochem. Biophys. Res. Commun. 239, 457-462
Che-Hun Jung and James A. Thomas (1996) "S-thiolated hepatocyte proteins and insulin disulides as
substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione" Arch.
Biochem. Biophys. 335, 61-72 |
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Dr. Oksoo Han
TOP
A. Molecular Mechanistic Studies on the Biosynthesis of Jasmonic Acid.
Jasmonic acid has been proposed to play a role in the response to pathogens and wounding by inducing
expression of several genes including proteinase inhibitors, vegetative storage
proteins, and lipoxygenase enzymes. Our primary interests are molecular
mechanistic studies and engineering of lipoxygenase and allene oxide synthase
in the jasmonic acid biosynthetic pathway. We have characterized stress
responsive biphasic expression pattern of lipoxygenase and currently working on
development of stress-resistant transgenic plant.
B. Mechanistic Studies and Engineering of Protoporphyrinogen Oxidase
Protoporphyrinogen
Oxidase, the last common enzyme in the biosynthesis of heme and chlorophyll,
catalyzes the conversion of protoporphyrinogen IX into protoporphyrin IX by six-electron
oxidation. It is generally accepted that protoporphyrinogen oxidase is the
primary target of diphenyl ether herbicides such as oxyfluorfen and
acifluorfen. Among protoporphyrinogen oxidase known from animals, plants and
bacteria, the one from B. subtilis is resistance to diphenyl ether herbisides.
Therefore, protoporphyrinogen oxidase from B. subtilis is an ideal choice to be
introduced into plants for producing herbicide-resistant transgenic plants. We
have produced diphenyl ether-resistant transgenic rice and are currently working
on the engineering of protoporphyrinogen oxidase.
C. Genetic Engineering of Erythromycin Biosynthetic Enzymes
Erythromycin A, a clinically
valuable anti-infective drug, is produced by Saccharopolyspora erythrea.
Structurally, it consists of a 14-membered macrolactone ring and two
deoxysugars, L-cladinose and D-desosamine. Because of medical and commercial
importance, its biosynthetic genes are extensively studied, including
polyketide synthase genes and 6-deoxyerythronolide B hydroxylase gene. We are interested
in engineering of 6-deoxyerythronolide B hydroxylase (Cytochrome P450eryF) and
TDP-6-Deoxy-L-threo-D-glycero-4-hexulose epimerase.
Selected Publications
Kyu Whan Choi, Oksoo Han, Hee Jae Lee, Young Chae Yun, Yong Ho Kim, Yong In Kuk, Sung Uk Han,
Myojeung Kim, Ja Ock Guh, Generation of Resistance to Diphenyl ether herbicide, Oxyfluorfen, via
Expression of B. subtilis Protoporphyrinogen Oxidase Gene in Transgenic Tobacco, Biosc.Biotech.
Biochem. 62 (3), 558-560, 1998.
Wonyoung Kim, Choonkeun Kim, Oksoo Han, Function of eryBVII gene is to epimerize
TDP-6-deoxy-L-threo-D-glycero-4-hexulose in the Biosynthesis of Erythromycin A, J. Biochem. Mol.
Biol. 32(1), 72-75,1999.
Choonkeun Kim, Haeyoung Kim, Oksoo Han, The role of serine-246 in cytochromeP450eryF-catalyzed
hydroxylation of 6-deoxyerythronolide hydroxylase,Biosci. Biotech. Biochem
. 65, 2001,in press.
Eun-SeonKim, Kyungwhan Back, Myunggi Baik, Eunyoung Choi, Oksoo Han, Sequence of Wound- responsive Lipoxygenase Gene from Maize Seedlings,
>J. Biochem. Mol. Biol. 34, 2001, in press.
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