Tetrahydromethanopterin-dependent serine transhydroxymethylase from Methanobacterium thermoautotrophicum

J. C. Hoyt; A. Oren; J. C. Escalante-Semerena; R. S. Wolfe

doi:10.1007/BF00446773

Tetrahydromethanopterin-dependent serine transhydroxymethylase from Methanobacterium thermoautotrophicum

J. C. Hoyt, A. Oren, J. C. Escalante-Semerena, R. S. Wolfe^*

^*Corresponding author for this work

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

24 Scopus citations

Abstract

Serine transhydroxymethylase of Methanobacterium thermoautotrophicum has been purified to within 95% of homogeneity. Activity was strictly dependent on tetrahydromethanopterin, tetrahydrofolate being unable to serve as the acceptor C₁ units from l-serine. The native protein has a molecular weight of about 102,000 daltons. The enzyme shows maximal activity at 60°C, has a pH optimum of 8.1, and required pyridoxal-5′-phosphate and Mg²⁺ for optimal activity.

Original language	English
Pages (from-to)	153-158
Number of pages	6
Journal	Archives of Microbiology
Volume	145
Issue number	2
DOIs	https://doi.org/10.1007/BF00446773
State	Published - Jul 1986
Externally published	Yes

Keywords

Methanobacterium
Methanogen
Serine transhydroxymethylase
Tetrahydromethanopterin

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10.1007/BF00446773

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title = "Tetrahydromethanopterin-dependent serine transhydroxymethylase from Methanobacterium thermoautotrophicum",

abstract = "Serine transhydroxymethylase of Methanobacterium thermoautotrophicum has been purified to within 95% of homogeneity. Activity was strictly dependent on tetrahydromethanopterin, tetrahydrofolate being unable to serve as the acceptor C1 units from l-serine. The native protein has a molecular weight of about 102,000 daltons. The enzyme shows maximal activity at 60°C, has a pH optimum of 8.1, and required pyridoxal-5′-phosphate and Mg2+ for optimal activity.",

keywords = "Methanobacterium, Methanogen, Serine transhydroxymethylase, Tetrahydromethanopterin",

author = "Hoyt, {J. C.} and A. Oren and Escalante-Semerena, {J. C.} and Wolfe, {R. S.}",

year = "1986",

month = jul,

doi = "10.1007/BF00446773",

language = "אנגלית",

volume = "145",

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AU - Hoyt, J. C.

AU - Oren, A.

AU - Escalante-Semerena, J. C.

AU - Wolfe, R. S.

PY - 1986/7

Y1 - 1986/7

N2 - Serine transhydroxymethylase of Methanobacterium thermoautotrophicum has been purified to within 95% of homogeneity. Activity was strictly dependent on tetrahydromethanopterin, tetrahydrofolate being unable to serve as the acceptor C1 units from l-serine. The native protein has a molecular weight of about 102,000 daltons. The enzyme shows maximal activity at 60°C, has a pH optimum of 8.1, and required pyridoxal-5′-phosphate and Mg2+ for optimal activity.

AB - Serine transhydroxymethylase of Methanobacterium thermoautotrophicum has been purified to within 95% of homogeneity. Activity was strictly dependent on tetrahydromethanopterin, tetrahydrofolate being unable to serve as the acceptor C1 units from l-serine. The native protein has a molecular weight of about 102,000 daltons. The enzyme shows maximal activity at 60°C, has a pH optimum of 8.1, and required pyridoxal-5′-phosphate and Mg2+ for optimal activity.

KW - Methanobacterium

KW - Methanogen

KW - Serine transhydroxymethylase

KW - Tetrahydromethanopterin

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SN - 0302-8933

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JO - Archives of Microbiology

JF - Archives of Microbiology

IS - 2

ER -

Tetrahydromethanopterin-dependent serine transhydroxymethylase from Methanobacterium thermoautotrophicum

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Keywords

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