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N-Formyl-L-alanine Sale

(Synonyms: N-Formylalanine) 目录号 : GC66876

N-Formyl-L-alanine (N-Formylalanine) 是一种可以用于氨基酸合成的丙氨酸衍生物。

N-Formyl-L-alanine Chemical Structure

Cas No.:10512-86-4

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Sample solution is provided at 25 µL, 10mM.

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产品描述

N-Formyl-L-alanine (N-Formylalanine) is an alanine derivative that can be used for amino acid synthesis[1].

[1]. MartÍ-Arbona R, et al. Annotating enzymes of unknown function: N-formimino-L-glutamate deiminase is a member of the amidohydrolase superfamily. Biochemistry. 2006 Feb 21;45(7):1997-2005.

Chemical Properties

Cas No. 10512-86-4 SDF Download SDF
别名 N-Formylalanine
分子式 C4H7NO3 分子量 117.1
溶解度 储存条件 Store at -20°C
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 8.5397 mL 42.6985 mL 85.3971 mL
5 mM 1.7079 mL 8.5397 mL 17.0794 mL
10 mM 0.854 mL 4.2699 mL 8.5397 mL
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Research Update

Beta-ureidopropionase with N-carbamoyl-alpha-L-amino acid amidohydrolase activity from an aerobic bacterium, Pseudomonas putida IFO 12996

Eur J Biochem 1994 Jul 15;223(2):625-30.PMID:8055933DOI:10.1111/j.1432-1033.1994.tb19034.x

beta-Ureidopropionase of aerobic bacterial origin was purified to homogeneity from Pseudomonas putida IFO 12996. The enzyme shows a broad substrate specificity. In addition to beta-ureidopropionate (Km 3.74 mM, Vmax 4.12 U/mg), gamma-ureido-n-butyrate (Km 11.6 mM, Vmax 19.4 U/mg), and several N-carbamoyl-alpha-amino acids, such as N-carbamoylglycine (Km 0.68 mM, Vmax 9.14 x 10(-2) U/mg), N-carbamoyl-L-alanine (Km 1.56 mM, Vmax 1.00 U/mg), N-carbamoyl-L-serine (Km 75.1 mM, Vmax 3.78 U/mg), and N-carbamoyl-DL-alpha-amino-n-butyrate (Km 2.81 mM, Vmax 1.08 U/mg), are also hydrolyzed. The hydrolysis of N-carbamoyl-alpha-amino acids is strictly L enantiomer specific. N-Formyl-L-alanine and N-acetyl-L-alanine are also hydrolyzed by the enzyme, but the rate of hydrolysis is lower than the rate for N-carbamoyl-L-alanine. The enzyme requires a divalent metal ion, such as Co2+, Ni2+ or Mn2+, for activity, and is significantly affected by sulfhydryl reagents. The enzyme consists of two polypeptide chains with identical relative molecular mass M(r) 45000. The broad substrate specificity and metal ion dependence of the enzyme show that the beta-ureidopropionase of this aerobic bacterium is quite different from the beta-ureidopropionases of mammals and anaerobic bacteria.