Kinetic parameters of two rice α-amylase isozymes for oligosaccharide degradation

Masaaki Terashima; Norio Hayashi; Bruce R. Thomas; Raymond L. Rodriguez; Shigeo Katoh

Kinetic parameters of two rice α-amylase isozymes for oligosaccharide degradation

Masaaki Terashima, Norio Hayashi, Bruce R. Thomas, Raymond L. Rodriguez, Shigeo Katoh

Molecular and Cellular Biology

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

8 Scopus citations

Abstract

The rice α-amylase isozymes Amy1A and Amy3D have distinct kinetic parameters and product profiles. For Amy3D, Michaelis constants (K_m) decrease, and molecular activities (k_cat) increase with the chain length of the substrates from maltose to maltoheptaose. Although Amy1A has a lower K_m than Amy3D, the k_cat of Amy1A was much lower than that of Amy3D. Amy1A produces only negligible amounts of glucose, while Amy3D produces glucose as a major product. Glucose regulates the expression of a number of genes in developing seedlings, so Amy3D may have a unique regulatory role in control of seedling development.

Original language	English (US)
Pages (from-to)	9-14
Number of pages	6
Journal	Plant Science
Volume	116
Issue number	1
State	Published - 1996

Keywords

α-amylase
Action pattern
Carbon metabolite signal
Kinetic constant
Oligosaccharide
Rice

ASJC Scopus subject areas

Plant Science
Biochemistry
Biotechnology

Cite this

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title = "Kinetic parameters of two rice α-amylase isozymes for oligosaccharide degradation",

abstract = "The rice α-amylase isozymes Amy1A and Amy3D have distinct kinetic parameters and product profiles. For Amy3D, Michaelis constants (Km) decrease, and molecular activities (kcat) increase with the chain length of the substrates from maltose to maltoheptaose. Although Amy1A has a lower Km than Amy3D, the kcat of Amy1A was much lower than that of Amy3D. Amy1A produces only negligible amounts of glucose, while Amy3D produces glucose as a major product. Glucose regulates the expression of a number of genes in developing seedlings, so Amy3D may have a unique regulatory role in control of seedling development.",

keywords = "α-amylase, Action pattern, Carbon metabolite signal, Kinetic constant, Oligosaccharide, Rice",

author = "Masaaki Terashima and Norio Hayashi and Thomas, {Bruce R.} and Rodriguez, {Raymond L.} and Shigeo Katoh",

year = "1996",

language = "English (US)",

volume = "116",

pages = "9--14",

journal = "Plant Science",

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T1 - Kinetic parameters of two rice α-amylase isozymes for oligosaccharide degradation

AU - Terashima, Masaaki

AU - Hayashi, Norio

AU - Thomas, Bruce R.

AU - Rodriguez, Raymond L.

AU - Katoh, Shigeo

PY - 1996

Y1 - 1996

N2 - The rice α-amylase isozymes Amy1A and Amy3D have distinct kinetic parameters and product profiles. For Amy3D, Michaelis constants (Km) decrease, and molecular activities (kcat) increase with the chain length of the substrates from maltose to maltoheptaose. Although Amy1A has a lower Km than Amy3D, the kcat of Amy1A was much lower than that of Amy3D. Amy1A produces only negligible amounts of glucose, while Amy3D produces glucose as a major product. Glucose regulates the expression of a number of genes in developing seedlings, so Amy3D may have a unique regulatory role in control of seedling development.

AB - The rice α-amylase isozymes Amy1A and Amy3D have distinct kinetic parameters and product profiles. For Amy3D, Michaelis constants (Km) decrease, and molecular activities (kcat) increase with the chain length of the substrates from maltose to maltoheptaose. Although Amy1A has a lower Km than Amy3D, the kcat of Amy1A was much lower than that of Amy3D. Amy1A produces only negligible amounts of glucose, while Amy3D produces glucose as a major product. Glucose regulates the expression of a number of genes in developing seedlings, so Amy3D may have a unique regulatory role in control of seedling development.

KW - α-amylase

KW - Action pattern

KW - Carbon metabolite signal

KW - Kinetic constant

KW - Oligosaccharide

KW - Rice

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AN - SCOPUS:0001129198

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ER -

Kinetic parameters of two rice α-amylase isozymes for oligosaccharide degradation

Abstract

Keywords

ASJC Scopus subject areas

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