Schachman HK - Search Results

1

Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains.

Eisenstein E, Markby DW, Schachman HK. Eisenstein E, et al. Among authors: schachman hk. Proc Natl Acad Sci U S A. 1989 May;86(9):3094-8. doi: 10.1073/pnas.86.9.3094. Proc Natl Acad Sci U S A. 1989. PMID: 2566165 Free PMC article.

2

Negative complementation in aspartate transcarbamylase. Analysis of hybrid enzyme molecules containing different arrangements of polypeptide chains from wild-type and inactive mutant catalytic subunits.

Eisenstein E, Han MS, Woo TS, Ritchey JM, Gibbons I, Yang YR, Schachman HK. Eisenstein E, et al. Among authors: schachman hk. J Biol Chem. 1992 Nov 5;267(31):22148-55. J Biol Chem. 1992. PMID: 1429567 Free article.

3

A 70-amino acid zinc-binding polypeptide from the regulatory chain of aspartate transcarbamoylase forms a stable complex with the catalytic subunit leading to markedly altered enzyme activity.

Markby DW, Zhou BB, Schachman HK. Markby DW, et al. Among authors: schachman hk. Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10568-72. doi: 10.1073/pnas.88.23.10568. Proc Natl Acad Sci U S A. 1991. PMID: 1961722 Free PMC article.

4

Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase.

Eisenstein E, Markby DW, Schachman HK. Eisenstein E, et al. Among authors: schachman hk. Biochemistry. 1990 Apr 17;29(15):3724-31. doi: 10.1021/bi00467a019. Biochemistry. 1990. PMID: 2187530

5

Cooperative binding of the bisubstrate analog N-(phosphonacetyl)-L-aspartate to aspartate transcarbamoylase and the heterotropic effects of ATP and CTP.

Newell JO, Markby DW, Schachman HK. Newell JO, et al. Among authors: schachman hk. J Biol Chem. 1989 Feb 15;264(5):2476-81. J Biol Chem. 1989. PMID: 2644262 Free article.

6

Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase.

Robey EA, Wente SR, Markby DW, Flint A, Yang YR, Schachman HK. Robey EA, et al. Among authors: schachman hk. Proc Natl Acad Sci U S A. 1986 Aug;83(16):5934-8. doi: 10.1073/pnas.83.16.5934. Proc Natl Acad Sci U S A. 1986. PMID: 3526345 Free PMC article.

7

1H NMR studies on the catalytic subunit of aspartate transcarbamoylase.

Cohen RE, Takama M, Schachman HK. Cohen RE, et al. Among authors: schachman hk. Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):11881-5. doi: 10.1073/pnas.89.24.11881. Proc Natl Acad Sci U S A. 1992. PMID: 1465412 Free PMC article.

8

Role of a carboxyl-terminal helix in the assembly, interchain interactions, and stability of aspartate transcarbamoylase.

Peterson CB, Schachman HK. Peterson CB, et al. Among authors: schachman hk. Proc Natl Acad Sci U S A. 1991 Jan 15;88(2):458-62. doi: 10.1073/pnas.88.2.458. Proc Natl Acad Sci U S A. 1991. PMID: 1899140 Free PMC article.

9

Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains.

Yang YR, Schachman HK. Yang YR, et al. Among authors: schachman hk. Proc Natl Acad Sci U S A. 1993 Dec 15;90(24):11980-4. doi: 10.1073/pnas.90.24.11980. Proc Natl Acad Sci U S A. 1993. PMID: 8265657 Free PMC article.

10

Random circular permutation of genes and expressed polypeptide chains: application of the method to the catalytic chains of aspartate transcarbamoylase.

Graf R, Schachman HK. Graf R, et al. Among authors: schachman hk. Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11591-6. doi: 10.1073/pnas.93.21.11591. Proc Natl Acad Sci U S A. 1996. PMID: 8876180 Free PMC article.

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